<?xml version="1.0" encoding="UTF-8" standalone="no"?><rss xmlns:atom="http://www.w3.org/2005/Atom" xmlns:blogger="http://schemas.google.com/blogger/2008" xmlns:gd="http://schemas.google.com/g/2005" xmlns:georss="http://www.georss.org/georss" xmlns:itunes="http://www.itunes.com/dtds/podcast-1.0.dtd" xmlns:openSearch="http://a9.com/-/spec/opensearchrss/1.0/" xmlns:thr="http://purl.org/syndication/thread/1.0" version="2.0"><channel><atom:id>tag:blogger.com,1999:blog-1016184987758340627</atom:id><lastBuildDate>Wed, 29 Jul 2026 09:50:06 +0000</lastBuildDate><category>The Cytoplasm</category><category>Histology And Its Methods of Study</category><category>The Cell Nucleus</category><category>Medical Jokes</category><category>Java Application for Medical</category><category>My Coursework</category><category>News</category><category>Others</category><title>De Histology</title><description>Histology For Your Life</description><link>http://dehistology.blogspot.com/</link><managingEditor>noreply@blogger.com (De Histology)</managingEditor><generator>Blogger</generator><openSearch:totalResults>44</openSearch:totalResults><openSearch:startIndex>1</openSearch:startIndex><openSearch:itemsPerPage>25</openSearch:itemsPerPage><language>en-us</language><itunes:explicit>no</itunes:explicit><copyright>deztroyer28</copyright><itunes:subtitle>Histology For Your Life</itunes:subtitle><itunes:category text="Science &amp; Medicine"><itunes:category text="Natural Sciences"/></itunes:category><itunes:author>deztroyer28</itunes:author><itunes:owner><itunes:email>noreply@blogger.com</itunes:email><itunes:name>deztroyer28</itunes:name></itunes:owner><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-7359031553128318435</guid><pubDate>Wed, 29 Jun 2011 13:29:00 +0000</pubDate><atom:updated>2011-06-29T20:29:45.006+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">Medical Jokes</category><title>Warming Up</title><description>&lt;div style="text-align: justify;"&gt;&lt;div style="text-align: justify;"&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhC8lD-Qc05BexUK3qxo_o29bdQgLBTROBBjvlv4MXw0D-nFXk7VaCoOpvRjbUxdvnb8xI67vEZ0wMTFwBBb39hjXPnKiz3kyzMq1BCCzI-AZLkiWmFF8JICa1NwD-VW1V1OVV5TEGycn4/s1600/Screaming+Out.JPG" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="180" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhC8lD-Qc05BexUK3qxo_o29bdQgLBTROBBjvlv4MXw0D-nFXk7VaCoOpvRjbUxdvnb8xI67vEZ0wMTFwBBb39hjXPnKiz3kyzMq1BCCzI-AZLkiWmFF8JICa1NwD-VW1V1OVV5TEGycn4/s320/Screaming+Out.JPG" width="320" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Ketika Dr Badrun sedang mempersiapkan obat yang hendak disuntikkan kepada penderita, tiba-tiba penderita"&gt;When The Doctor was preparing a drug that would be injected to the patient, &lt;/span&gt;&lt;/span&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Ketika Dr Badrun sedang mempersiapkan obat yang hendak disuntikkan kepada penderita, tiba-tiba penderita"&gt;suddenly, &lt;/span&gt;&lt;/span&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Ketika Dr Badrun sedang mempersiapkan obat yang hendak disuntikkan kepada penderita, tiba-tiba penderita"&gt;the patient &lt;/span&gt;&lt;span style="background-color: white;" title="yang sedang berbaring ditempat tidurnya berteriak keras-keras."&gt;who was lying in bed screaming out. &lt;/span&gt;&lt;/span&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span title="Karena heran dr Badrun bertanya :"&gt;The Doctor was &lt;/span&gt;&lt;/span&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span title="Karena heran dr Badrun bertanya :"&gt;surprised, so he asked to the patient:&amp;nbsp;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span title="Karena heran dr Badrun bertanya :"&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span title="Karena heran dr Badrun bertanya :"&gt; &lt;/span&gt;&lt;span title="dr."&gt;The Doctor&lt;/span&gt;&lt;span style="background-color: white;" title="Badrun : “Lho kenapa berteriak-teriak?"&gt; : Well...why are you screaming out ? &lt;/span&gt;&lt;span title="Apa takut disuntik?”"&gt;What is the fear of injections ?&lt;/span&gt;&lt;span style="background-color: white;" title="Penderita : “Tidak dok, saya berteriak sekedar untuk latthan pemanasan saja, sehingga apabila nanti disuntik tidak usah berteriak lagi.”"&gt;&amp;nbsp;&lt;/span&gt;&lt;/span&gt;&lt;br /&gt;
&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Penderita : “Tidak dok, saya berteriak sekedar untuk latthan pemanasan saja, sehingga apabila nanti disuntik tidak usah berteriak lagi.”"&gt;Patients : No...Sir, I screamed just for warming up. So that, &lt;/span&gt;&lt;/span&gt;&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;when I&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;'m&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;shot&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;I will not&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;scream&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;anymore&lt;/span&gt;&lt;/span&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Penderita : “Tidak dok, saya berteriak sekedar untuk latthan pemanasan saja, sehingga apabila nanti disuntik tidak usah berteriak lagi.”"&gt;... :D&lt;/span&gt;&lt;span style="background-color: white;" title="dr."&gt;&amp;nbsp;&lt;/span&gt;&lt;/span&gt;&lt;br /&gt;
&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="dr."&gt;The Doctor&lt;/span&gt;&lt;span style="background-color: white;" title="Badruun : ?!??"&gt; : ?!!?!!?!?!&lt;/span&gt;&lt;/span&gt;</description><link>http://dehistology.blogspot.com/2011/06/warming-up.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhC8lD-Qc05BexUK3qxo_o29bdQgLBTROBBjvlv4MXw0D-nFXk7VaCoOpvRjbUxdvnb8xI67vEZ0wMTFwBBb39hjXPnKiz3kyzMq1BCCzI-AZLkiWmFF8JICa1NwD-VW1V1OVV5TEGycn4/s72-c/Screaming+Out.JPG" width="72"/><thr:total>115</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-6546133486822754256</guid><pubDate>Tue, 28 Jun 2011 13:06:00 +0000</pubDate><atom:updated>2011-06-28T20:06:45.687+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cytoplasm</category><title>Cytosol</title><description>&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiIFFOI6Mzs4SwsIJqxJMoDkqfZzopSOpMtKEAMjVX8cZZNPkrpdwCu_VNFfWKVGnOjQrNDuL6DQA2bhLl8Dwy-sNrmDR-c3knIcfRr8etlUOOIxdKSFLZwmPg95t1qSPQ791ESqLl3bPI/s1600/Cytosol.png" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="343" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiIFFOI6Mzs4SwsIJqxJMoDkqfZzopSOpMtKEAMjVX8cZZNPkrpdwCu_VNFfWKVGnOjQrNDuL6DQA2bhLl8Dwy-sNrmDR-c3knIcfRr8etlUOOIxdKSFLZwmPg95t1qSPQ791ESqLl3bPI/s400/Cytosol.png" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&amp;nbsp;At one time, it was believed that the cytoplasm intervening  between the discrete organelles and deposits was unstructured. This belief was  reinforced by the use of homogenization and centrifugation of the homogenates to  yield fractions consisting of recognizable membrane-bound organelles. The final  supernatant produced by this process, after the separation of organelles, is  called the &lt;b&gt;cytosol.&lt;/b&gt; The cytosol constitutes about half the total volume  of the cell. Homogenization of cells disrupts a delicate &lt;b&gt;microtrabecular  lattice&lt;/b&gt; that incorporates filaments of actin, microtubules, intermediate  filaments, enzymes, and other soluble constituents into a structured cytosol.  The cytosol coordinates the intracellular movements of organelles and provides  an explanation for the viscosity of the cytoplasm. Soluble (not membrane-bound)  enzymes, such as those of the glycolytic pathway, for example, function more  efficiently when organized in a sequence instead of having to rely on random  collisions with their substrates. The cytosol provides a framework for this  organization. It contains thousands of enzymes that produce building blocks for  larger molecules and break down small molecules to liberate energy. All  machinery to synthesize proteins (rRNA, mRNA, tRNA, enzymes, and other factors)  is contained in the cytosol.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Cell Components &amp;amp; Diseases&lt;/b&gt;&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt; &lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff" valign="top"&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;Many diseases are related to molecular  alterations in specific cell components. In several of these diseases,  structural changes can be detected by light or electron microscopy or by  cytochemical techniques. Table 2–5 lists some of these diseases and emphasizes  the importance of understanding the many cell components in pathobiology.&lt;/div&gt;&lt;a href="" name="711983"&gt;&lt;/a&gt; &lt;table bgcolor="#ffffff" border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#cccccc" style="border-left: rgb(102,102,102) 1px solid; border-right: rgb(102,102,102) 1px solid; border-top: rgb(102,102,102) 1px solid;"&gt; &lt;table border="0" cellpadding="3" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td&gt; &lt;div class="tableTitle"&gt;Table 2–5. Some Human and Animal Diseases Related to Altered  Cellular Components.&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td&gt; &lt;table bgcolor="#666666" border="0" cellpadding="3" cellspacing="1"&gt;&lt;colgroup span="5"&gt;&lt;/colgroup&gt; &lt;thead&gt;
&lt;tr class="font12"&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Cell Component Involved&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Disease&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Molecular Defect&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Morphological Change&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Clinical Consequence&lt;/th&gt;&lt;/tr&gt;
&lt;/thead&gt; &lt;tbody&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Mitochondrion&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Mitochondrial  cytopathy&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Defect of oxidative  phosphorylation&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Increase in size and  number of muscle mitochondria&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;High basal metabolism  without hyperthyroidism&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" rowspan="2" valign="top"&gt;Microtubule&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Immotile cilia  syndrome&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Lack of dynein in cilia  and flagella&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Lack of arms of the  doublet microtubules&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Immotile cilia and  flagella with male sterility and chronic respiratory infection&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Mouse (&lt;i&gt;Acomys&lt;/i&gt;)  diabetes &amp;nbsp;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Reduction of tubulin in  pancreatic &lt;img border="0" src="2.%20The%20Cytoplasm_files/betalower.gif" /&gt;  cells&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Reduction of microtubules  in &lt;img border="0" src="2.%20The%20Cytoplasm_files/betalower.gif" /&gt; cells&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;High blood sugar content  (diabetes)&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" rowspan="2" valign="top"&gt;Lysosome&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Metachromatic  leukodystrophy&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Lack of lysosomal  sulfatase&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Accumulation of lipid  (cerebroside) in tissues&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Motor and mental  impairment&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Hurler disease&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Lack of lysosomal &lt;img border="0" src="2.%20The%20Cytoplasm_files/alphalower.gif" /&gt;-&lt;small&gt;L&lt;/small&gt;-iduronidase&amp;nbsp;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Accumulation of dermatan  sulfate in tissues&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Growth and mental  retardation&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Golgi complex&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;I-cell disease&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Phosphotransferase  deficiency&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Inclusion-particle  storage in several cells&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Psychomotor retardation,  bone abnormalities&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff"&gt;&lt;br class="Spacer8" /&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;a href="" name="711897"&gt;&lt;/a&gt; &lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff" valign="top"&gt; &lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Afzelius BA, Eliasson R: Flagellar mutants in  man: on the heterogeneity of the immotile-cilia syndrome. J Ultrastruct Res  1979;69:43. [PMID: 501788] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Aridor M, Balch WE: Integration of endoplasmic  reticulum signaling in health and disease. Nat Med 1999;5:745. [PMID: 10395318]  &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Barrit GJ: &lt;i&gt;Communication Within Animal  Cells&lt;/i&gt;. Oxford University Press, 1992. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Becker WM et al: &lt;i&gt;The World of the Cell&lt;/i&gt;,  4th ed. Benjamin/Cummings, 2000. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Bretscher MS: The molecules of the cell  membrane. Sci Am 1985;253:100. [PMID: 2416050] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brinkley BR: Microtubule organizing centers.  Annu Rev Cell Biol 1985;1:145. [PMID: 3916316] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brown MS et al: Recycling receptors: the  round-trip itinerary of migrant membrane proteins. Cell 1983;32:663. [PMID:  6299572] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cooper GM: &lt;i&gt;The Cell: A Molecular  Approach&lt;/i&gt;. ASM Press/Sinauer Associates, Inc., 1997. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: &lt;i&gt;A Guided Tour of the Living  Cell&lt;/i&gt;. Freeman, 1984. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: Microbodies in the living cell. Sci  Am 1983;248:74. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Dustin P: &lt;i&gt;Microtubules&lt;/i&gt;, 2nd ed.  Springer-Verlag, 1984. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Farquhar MG: Progress in unraveling pathways of  Golgi traffic. Annu Rev Cell Biol 1985;1:447. [PMID: 3916320] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Fawcett D: &lt;i&gt;The Cell&lt;/i&gt;, 2nd ed. Saunders,  1981. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Krstíc RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Mitchison TJ, Cramer LP: Actin-based cell  motility and cell locomotion. Cell 1996;84:371. [PMID: 8608590] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Osborn M, Weber K: Intermediate filaments:  cell-type-specific markers in differentiation and pathology. Cell 1982;31:303.  [PMID: 6891619] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Pfeffer SR, Rothman JE: Biosynthetic protein  transport and sorting in the endoplasmic reticulum. Annu Rev Biochem  1987;56:829. [PMID: 3304148] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rothman J: The compartmental organization of  the Golgi apparatus. Sci Am 1985;253:74. [PMID: 3929377] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Simons K, Ikonen E: How cells handle  cholesterol. Science 2000;290:1721. [PMID: 11099405] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Tzagoloff A: &lt;i&gt;Mitochondria&lt;/i&gt;. Plenum, 1982.  &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Weber K, Osborn M: The molecules of the cell  matrix. Sci Am 1985;253:110. [PMID: 4071030] &lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/cytosol.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiIFFOI6Mzs4SwsIJqxJMoDkqfZzopSOpMtKEAMjVX8cZZNPkrpdwCu_VNFfWKVGnOjQrNDuL6DQA2bhLl8Dwy-sNrmDR-c3knIcfRr8etlUOOIxdKSFLZwmPg95t1qSPQ791ESqLl3bPI/s72-c/Cytosol.png" width="72"/><thr:total>9</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-4276850224198188130</guid><pubDate>Sun, 26 Jun 2011 12:34:00 +0000</pubDate><atom:updated>2011-06-26T19:56:47.946+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cytoplasm</category><title>Cytoplasmic Deposits</title><description>&lt;div style="background-color: white; text-align: justify;"&gt;Cytoplasmic deposits are usually transitory components of the cytoplasm,  composed mainly of accumulated metabolites or other substances. The accumulated  molecules occur in several forms, one of them being lipid droplets in adipose  tissue, adrenal cortex cells, and liver cells (Figure 2–38). Carbohydrate  accumulations are also visible in several cells in the form of glycogen. After  impregnation with lead salts, glycogen appears as collections of electron-dense  particles (Figure 2–39). Proteins are stored in glandular cells as &lt;b&gt;secretory  granules&lt;/b&gt; or &lt;b&gt;secretory vesicles&lt;/b&gt; (Figure 2–29); under stimulation,  these proteins are periodically released into the extracellular medium.&lt;/div&gt;&lt;div style="background-color: white; text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="background-color: white; text-align: justify;"&gt;&lt;b&gt;Figure 2-38&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="background-color: white; clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgL3lpr2Y5NSUOROAgLET2Odu0qqF9vUNU4qM4_tJSVG7Gd_UehN9amIsYIxutLt5N1Zq9f1LkF3lYHlcCC2f25ebVlfJWzDbcZdgX8dY4MaS1KCC7SL2FbKTy8X9PMDaL6_9yrrXOjHes/s1600/Figure+2-38.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="293" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgL3lpr2Y5NSUOROAgLET2Odu0qqF9vUNU4qM4_tJSVG7Gd_UehN9amIsYIxutLt5N1Zq9f1LkF3lYHlcCC2f25ebVlfJWzDbcZdgX8dY4MaS1KCC7SL2FbKTy8X9PMDaL6_9yrrXOjHes/s320/Figure+2-38.bmp" width="320" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="background-color: white; text-align: justify;"&gt;&lt;/div&gt;&lt;table bgcolor="#ffffff" border="0" cellpadding="3" cellspacing="1" style="background-color: white;"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="font11"&gt;&lt;span class="font11"&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=4276850224198188130" name="711973"&gt;&lt;/a&gt; &lt;/span&gt;&lt;br /&gt;
&lt;div class="font11"&gt;&lt;span class="font11"&gt;Section of adrenal gland showing lipid droplets (L) and abundant  anomalous mitochondria (M).  &lt;small&gt;x&lt;/small&gt;19,000.&lt;/span&gt;&lt;/div&gt;&lt;div class="font11"&gt;&lt;span class="font11"&gt;&lt;br /&gt;
&lt;/span&gt;&lt;/div&gt;&lt;div class="font11"&gt;&lt;span class="font11"&gt;&lt;b&gt;Figure 2-39&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;span class="font11"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjjzly1cC8m2zqU2wYX8xU3PrRWBK9dYIfWz9jEyNxm_moF2NI4PosOmq0YvmCqEvKGNH1CDkcqkJovU7XaOotYkHMOdr6lywPLF4bhhiqBI8ZVMf561AB46VlRJ7kWMA7qyMzJEZZxeZw/s1600/Figure+2-39.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="340" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjjzly1cC8m2zqU2wYX8xU3PrRWBK9dYIfWz9jEyNxm_moF2NI4PosOmq0YvmCqEvKGNH1CDkcqkJovU7XaOotYkHMOdr6lywPLF4bhhiqBI8ZVMf561AB46VlRJ7kWMA7qyMzJEZZxeZw/s400/Figure+2-39.bmp" width="400" /&gt;&lt;/a&gt;&lt;/span&gt;&lt;/div&gt;&lt;br /&gt;
&lt;div class="font11" style="text-align: justify;"&gt;Electron micrograph of a section of a liver cell showing  glycogen deposits as accumulations of electron-dense particles (arrows). The  dark structures with a dense core are peroxisomes. Mitochondria (M) are also  shown. &lt;small&gt;x&lt;/small&gt;30,000.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Deposits of colored substances—&lt;b&gt;pigments&lt;/b&gt;—are often  found in cells (Figure 2–40). They may be synthesized by the cell (eg, in the  skin melanocytes) or come from outside the body (eg, carotene). One of the most  common pigments is &lt;b&gt;lipofuscin,&lt;/b&gt; a yellowish-brown substance present mainly  in permanent cells (eg, neurons, cardiac muscle) that increases in quantity with  age. Its chemical constitution is complex. It is believed that granules of  lipofuscin derive from secondary lysosomes and represent deposits of  indigestible substances. A widely distributed pigment, &lt;b&gt;melanin&lt;/b&gt; is  abundant in the epidermis and in the pigment layer of the retina in the form of  dense intracellular membrane-limited granules.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-40&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEieWvd7AmL0xmhQmVDtYMkzfhmd5RngircToS8u0y7wT9kKpg5SZHpLb4sGnwQxFHvT553bwPUCoxC43wf6dsNmdCHrDezoOuyOHFeuvpA7ElAtxsGOQTr416jXgMC7eUiXj7reVINj_fA/s1600/Figure+2-40.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="383" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEieWvd7AmL0xmhQmVDtYMkzfhmd5RngircToS8u0y7wT9kKpg5SZHpLb4sGnwQxFHvT553bwPUCoxC43wf6dsNmdCHrDezoOuyOHFeuvpA7ElAtxsGOQTr416jXgMC7eUiXj7reVINj_fA/s400/Figure+2-40.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Section of amphibian liver shows cells with pigment deposit (PD)  in the cytoplasm, a macrophage (M), hepatocytes (H), and a neutrophil leukocyte  (N). In this resin-embedded material it is possible to see mitochondria (pale  red) and lysosomes (blue) in the cytoplasm of the hepatocytes. Only with resin  embedding is it possible to obtain such information. Giemsa stain. Medium  magnification.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff" valign="top"&gt;&lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Afzelius BA, Eliasson R: Flagellar mutants in  man: on the heterogeneity of the immotile-cilia syndrome. J Ultrastruct Res  1979;69:43. [PMID: 501788] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Aridor M, Balch WE: Integration of endoplasmic  reticulum signaling in health and disease. Nat Med 1999;5:745. [PMID: 10395318]  &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Barrit GJ: &lt;i&gt;Communication Within Animal  Cells&lt;/i&gt;. Oxford University Press, 1992. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Becker WM et al: &lt;i&gt;The World of the Cell&lt;/i&gt;,  4th ed. Benjamin/Cummings, 2000. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Bretscher MS: The molecules of the cell  membrane. Sci Am 1985;253:100. [PMID: 2416050] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brinkley BR: Microtubule organizing centers.  Annu Rev Cell Biol 1985;1:145. [PMID: 3916316] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brown MS et al: Recycling receptors: the  round-trip itinerary of migrant membrane proteins. Cell 1983;32:663. [PMID:  6299572] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cooper GM: &lt;i&gt;The Cell: A Molecular  Approach&lt;/i&gt;. ASM Press/Sinauer Associates, Inc., 1997. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: &lt;i&gt;A Guided Tour of the Living  Cell&lt;/i&gt;. Freeman, 1984. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: Microbodies in the living cell. Sci  Am 1983;248:74. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Dustin P: &lt;i&gt;Microtubules&lt;/i&gt;, 2nd ed.  Springer-Verlag, 1984. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Farquhar MG: Progress in unraveling pathways of  Golgi traffic. Annu Rev Cell Biol 1985;1:447. [PMID: 3916320] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Fawcett D: &lt;i&gt;The Cell&lt;/i&gt;, 2nd ed. Saunders,  1981. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Krstíc RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Mitchison TJ, Cramer LP: Actin-based cell  motility and cell locomotion. Cell 1996;84:371. [PMID: 8608590] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Osborn M, Weber K: Intermediate filaments:  cell-type-specific markers in differentiation and pathology. Cell 1982;31:303.  [PMID: 6891619] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Pfeffer SR, Rothman JE: Biosynthetic protein  transport and sorting in the endoplasmic reticulum. Annu Rev Biochem  1987;56:829. [PMID: 3304148] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rothman J: The compartmental organization of  the Golgi apparatus. Sci Am 1985;253:74. [PMID: 3929377] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Simons K, Ikonen E: How cells handle  cholesterol. Science 2000;290:1721. [PMID: 11099405] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Tzagoloff A: &lt;i&gt;Mitochondria&lt;/i&gt;. Plenum, 1982.  &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Weber K, Osborn M: The molecules of the cell  matrix. Sci Am 1985;253:110. [PMID: 4071030] &lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;</description><link>http://dehistology.blogspot.com/2011/06/cytoplasmic-deposits.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgL3lpr2Y5NSUOROAgLET2Odu0qqF9vUNU4qM4_tJSVG7Gd_UehN9amIsYIxutLt5N1Zq9f1LkF3lYHlcCC2f25ebVlfJWzDbcZdgX8dY4MaS1KCC7SL2FbKTy8X9PMDaL6_9yrrXOjHes/s72-c/Figure+2-38.bmp" width="72"/><thr:total>10</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-1429560221881760797</guid><pubDate>Sat, 25 Jun 2011 12:21:00 +0000</pubDate><atom:updated>2011-06-25T19:21:57.313+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cytoplasm</category><title>Intermediate Filaments</title><description>&lt;div class="contentBody" style="text-align: justify;"&gt;Ultrastructural and immunocytochemical investigations  reveal that a third major filamentous structure is present in eukaryotic cells.  In addition to the thin (actin) and thick (myosin) filaments, cells contain a  class of intermediate-sized filaments with an average diameter of 10–12 nm  (Figure 2–37 and Table 2–4). Several proteins that form intermediate filaments  have been isolated and localized by immunocytochemical means.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-37&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhHFZ2AvLKDkj21NCx0j9Fo1wh2z8bQ8UQq0Hq6Fi8ZpgYyR93Gmo2ooPRX5yWe-LH2c8pRfvrrirUQMgh2tTWENXDDib_vicchJCkLbZoG7e9pJQk9L4oPN-0-1tzLlXs8Nb7SDCrQhME/s1600/Figure+2-37.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhHFZ2AvLKDkj21NCx0j9Fo1wh2z8bQ8UQq0Hq6Fi8ZpgYyR93Gmo2ooPRX5yWe-LH2c8pRfvrrirUQMgh2tTWENXDDib_vicchJCkLbZoG7e9pJQk9L4oPN-0-1tzLlXs8Nb7SDCrQhME/s320/Figure+2-37.bmp" width="310" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Electron micrograph of a skin epithelial cell showing  intermediate filaments of keratin associated with desmosomes.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt; &lt;/div&gt;&lt;table bgcolor="#ffffff" border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#cccccc" style="border-left: rgb(102,102,102) 1px solid; border-right: rgb(102,102,102) 1px solid; border-top: rgb(102,102,102) 1px solid;"&gt;&lt;table border="0" cellpadding="3" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td&gt; &lt;div class="tableTitle"&gt;Table 2–4. Examples of Intermediate Filaments Found in  Eukaryotic Cells.&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td&gt; &lt;table bgcolor="#666666" border="0" cellpadding="3" cellspacing="1"&gt;&lt;colgroup span="3"&gt;&lt;/colgroup&gt; &lt;thead&gt;
&lt;tr class="font12"&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Filament Type&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Cell Type&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Examples&lt;/th&gt;&lt;/tr&gt;
&lt;/thead&gt; &lt;tbody&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Keratins&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Epithelium&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Both keratinizing and  nonkeratinizing epithelia &lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Vimentin&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Mesenchymal cells&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Fibroblasts,  chondroblasts, macrophages, endothelial cells, vascular smooth muscle&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Desmin&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Muscle&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Striated and smooth  muscle (except vascular smooth muscle)&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Gilial fibrillary acidic  proteins&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Glial cells&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Astrocytes&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Neurofilaments&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Neurons&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Nerve cell body and  processes&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff"&gt;&lt;br class="Spacer8" /&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;a href="" name="711882"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Keratins&lt;/b&gt; (Gr. &lt;i&gt;keras&lt;/i&gt;, horn) are a family of  approximately 20 proteins found in epithelia. They are encoded by a family of  genes and have different chemical and immunological properties. This diversity  of keratin is related to the various roles these proteins play in the epidermis,  nails, hooves, horns, feathers, scales, and the like that provide animals with  defense against abrasion and loss of water and heat.&lt;/div&gt;&lt;a href="" name="711883"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Vimentin&lt;/b&gt; filaments are characteristic of cells of  mesenchymal origin. (Mesenchyme is an embryonic tissue.) Vimentin is a single  protein (56–58 kDa) and may copolymerize with desmin or glial fibrillary acidic  protein.&lt;/div&gt;&lt;a href="" name="711884"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Desmin&lt;/b&gt; (&lt;b&gt;skeletin&lt;/b&gt;) is found in smooth muscle  and in the Z disks of skeletal and cardiac muscle (53–55 kDa).&lt;/div&gt;&lt;a href="" name="711885"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Glial filaments&lt;/b&gt; (&lt;b&gt;glial fibrillary acidic  protein&lt;/b&gt;) are characteristic of astrocytes but are not found in neurons,  muscle, mesenchymal cells, or epithelia (51 kDa).&lt;/div&gt;&lt;a href="" name="711886"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Neurofilaments&lt;/b&gt; consist of at least three  high-molecular-weight polypeptides (68, 140, and 210 kDa). Intermediate filament  proteins have different chemical structures and different roles in cellular  function.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt; &lt;/div&gt;&lt;div class="contentBody"&gt;&lt;span style="color: red;"&gt;&lt;b&gt;&lt;i&gt;Medical Application&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;a href="" name="711888"&gt;&lt;/a&gt; &lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;The presence of a specific type of intermediate  filament in tumors can reveal which cell originated the tumor, information  important for diagnosis and treatment (see Table 1–1). Identification of  intermediate filament proteins by means of immunocytochemical methods is a  routine procedure.&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Afzelius BA, Eliasson R: Flagellar mutants in  man: on the heterogeneity of the immotile-cilia syndrome. J Ultrastruct Res  1979;69:43. [PMID: 501788] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Aridor M, Balch WE: Integration of endoplasmic  reticulum signaling in health and disease. Nat Med 1999;5:745. [PMID: 10395318]  &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Barrit GJ: &lt;i&gt;Communication Within Animal  Cells&lt;/i&gt;. Oxford University Press, 1992. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Becker WM et al: &lt;i&gt;The World of the Cell&lt;/i&gt;,  4th ed. Benjamin/Cummings, 2000. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Bretscher MS: The molecules of the cell  membrane. Sci Am 1985;253:100. [PMID: 2416050] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brinkley BR: Microtubule organizing centers.  Annu Rev Cell Biol 1985;1:145. [PMID: 3916316] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brown MS et al: Recycling receptors: the  round-trip itinerary of migrant membrane proteins. Cell 1983;32:663. [PMID:  6299572] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cooper GM: &lt;i&gt;The Cell: A Molecular  Approach&lt;/i&gt;. ASM Press/Sinauer Associates, Inc., 1997. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: &lt;i&gt;A Guided Tour of the Living  Cell&lt;/i&gt;. Freeman, 1984. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: Microbodies in the living cell. Sci  Am 1983;248:74. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Dustin P: &lt;i&gt;Microtubules&lt;/i&gt;, 2nd ed.  Springer-Verlag, 1984. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Farquhar MG: Progress in unraveling pathways of  Golgi traffic. Annu Rev Cell Biol 1985;1:447. [PMID: 3916320] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Fawcett D: &lt;i&gt;The Cell&lt;/i&gt;, 2nd ed. Saunders,  1981. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Krstíc RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Mitchison TJ, Cramer LP: Actin-based cell  motility and cell locomotion. Cell 1996;84:371. [PMID: 8608590] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Osborn M, Weber K: Intermediate filaments:  cell-type-specific markers in differentiation and pathology. Cell 1982;31:303.  [PMID: 6891619] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Pfeffer SR, Rothman JE: Biosynthetic protein  transport and sorting in the endoplasmic reticulum. Annu Rev Biochem  1987;56:829. [PMID: 3304148] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rothman J: The compartmental organization of  the Golgi apparatus. Sci Am 1985;253:74. [PMID: 3929377] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Simons K, Ikonen E: How cells handle  cholesterol. Science 2000;290:1721. [PMID: 11099405] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Tzagoloff A: &lt;i&gt;Mitochondria&lt;/i&gt;. Plenum, 1982.  &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Weber K, Osborn M: The molecules of the cell  matrix. Sci Am 1985;253:110. [PMID: 4071030] &lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/intermediate-filaments.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhHFZ2AvLKDkj21NCx0j9Fo1wh2z8bQ8UQq0Hq6Fi8ZpgYyR93Gmo2ooPRX5yWe-LH2c8pRfvrrirUQMgh2tTWENXDDib_vicchJCkLbZoG7e9pJQk9L4oPN-0-1tzLlXs8Nb7SDCrQhME/s72-c/Figure+2-37.bmp" width="72"/><thr:total>7</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-7825110175625201302</guid><pubDate>Fri, 24 Jun 2011 14:04:00 +0000</pubDate><atom:updated>2011-06-24T21:04:48.730+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cytoplasm</category><title>Actin Filaments</title><description>&lt;div class="contentBody" style="text-align: justify;"&gt;Contractile activity in muscle cells results primarily from  an interaction between two proteins: actin and myosin. Actin is present in  muscle as a thin (5–7 nm in diameter) filament composed of globular subunits  organized into a double-stranded helix (Figure 2–36). Structural and biochemical  studies reveal that there are several types of actin and that this protein is  present in all cells.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-36&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg2AGpCzogv_jwuqNSNBkXd_TPhvbmrIPGRr5ygI3HT3HMQdGuoRG20TP-TTdFGvS-iRAKeLTvHLhn1hb6aQUbEOTa69sFn7DvnJmEEr2JBVaUxwLXNJmirxhp1vOlvQNbcZ1Zk1rfkux0/s1600/Figure+2-36.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg2AGpCzogv_jwuqNSNBkXd_TPhvbmrIPGRr5ygI3HT3HMQdGuoRG20TP-TTdFGvS-iRAKeLTvHLhn1hb6aQUbEOTa69sFn7DvnJmEEr2JBVaUxwLXNJmirxhp1vOlvQNbcZ1Zk1rfkux0/s320/Figure+2-36.bmp" width="216" /&gt;&lt;/a&gt;&lt;span class="font11"&gt;The cytosolic actin filament. Actin dimers  are added to the plus (+) end and removed at the minus (–) end, dynamically  lengthening or shortening the filament, as required by the cell. (Redrawn and  reproduced, with permission, from Junqueira LC, Carneiro J: &lt;i&gt;Biologia Celular  e Molecular&lt;/i&gt;, 6th ed. Editora Guanabara, 1997.)&lt;/span&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Within cells, microfilaments can be organized in many  forms. &lt;/div&gt;&lt;div&gt; &lt;/div&gt;&lt;dl class="font12" style="text-align: justify;"&gt;&lt;dd class="font12List"&gt;1. In skeletal muscle, they assume a paracrystalline array  integrated with thick (16-nm) myosin filaments.  &lt;/dd&gt;&lt;dd class="font12List"&gt;2. In most cells, actin filaments form a thin sheath just  beneath the plasmalemma, called the &lt;b&gt;cell cortex.&lt;/b&gt; These filaments appear  to be associated with membrane activities such as endocytosis, exocytosis, and  cell migratory activity.  &lt;/dd&gt;&lt;dd class="font12List"&gt;3. Actin filaments are intimately associated with several  cytoplasmic organelles, vesicles, and granules. The filaments are believed to  play a role in moving and shifting cytoplasmic components (cytoplasmic  streaming).  &lt;/dd&gt;&lt;dd class="font12List"&gt;4. Actin filaments are associated with myosin and form a  "purse-string" ring of filaments whose constriction results in the cleavage of  mitotic cells.  &lt;/dd&gt;&lt;dd class="font12List"&gt;5. In most cells, actin filaments are found scattered in  what appears to be an unorganized fashion within the cytoplasm (Figure  2–31).&lt;/dd&gt;&lt;/dl&gt;&lt;div style="text-align: justify;"&gt;&lt;a href="" name="711878"&gt;&lt;/a&gt; &lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Although actin filaments in muscle cells are structurally  stable, in nonmuscle cells they readily dissociate and reassemble. Actin  filament polymerization appears to be under the direct control of minute changes  in Ca&lt;sup&gt;2+&lt;/sup&gt; and cyclic AMP levels. A large number of actin-binding  proteins have been demonstrated in a wide variety of cells, and much current  research is focused on how these proteins regulate the state of polymerization  and lateral aggregation of actin filaments. Their importance can be deduced from  the fact that only about half the cell's actin is in the form of  filaments.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;a href="" name="711879"&gt;&lt;/a&gt; &lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Presumably, most actin filament-related activities depend  upon the interaction of &lt;b&gt;myosin&lt;/b&gt; with actin. (The structure and activity of  the thick myosin filaments are described in the section on muscle tissues.)&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Afzelius BA, Eliasson R: Flagellar mutants in  man: on the heterogeneity of the immotile-cilia syndrome. J Ultrastruct Res  1979;69:43. [PMID: 501788] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Aridor M, Balch WE: Integration of endoplasmic  reticulum signaling in health and disease. Nat Med 1999;5:745. [PMID: 10395318]  &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Barrit GJ: &lt;i&gt;Communication Within Animal  Cells&lt;/i&gt;. Oxford University Press, 1992. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Becker WM et al: &lt;i&gt;The World of the Cell&lt;/i&gt;,  4th ed. Benjamin/Cummings, 2000. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Bretscher MS: The molecules of the cell  membrane. Sci Am 1985;253:100. [PMID: 2416050] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brinkley BR: Microtubule organizing centers.  Annu Rev Cell Biol 1985;1:145. [PMID: 3916316] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brown MS et al: Recycling receptors: the  round-trip itinerary of migrant membrane proteins. Cell 1983;32:663. [PMID:  6299572] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cooper GM: &lt;i&gt;The Cell: A Molecular  Approach&lt;/i&gt;. ASM Press/Sinauer Associates, Inc., 1997. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: &lt;i&gt;A Guided Tour of the Living  Cell&lt;/i&gt;. Freeman, 1984. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: Microbodies in the living cell. Sci  Am 1983;248:74. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Dustin P: &lt;i&gt;Microtubules&lt;/i&gt;, 2nd ed.  Springer-Verlag, 1984. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Farquhar MG: Progress in unraveling pathways of  Golgi traffic. Annu Rev Cell Biol 1985;1:447. [PMID: 3916320] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Fawcett D: &lt;i&gt;The Cell&lt;/i&gt;, 2nd ed. Saunders,  1981. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Krstíc RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Mitchison TJ, Cramer LP: Actin-based cell  motility and cell locomotion. Cell 1996;84:371. [PMID: 8608590] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Osborn M, Weber K: Intermediate filaments:  cell-type-specific markers in differentiation and pathology. Cell 1982;31:303.  [PMID: 6891619] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Pfeffer SR, Rothman JE: Biosynthetic protein  transport and sorting in the endoplasmic reticulum. Annu Rev Biochem  1987;56:829. [PMID: 3304148] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rothman J: The compartmental organization of  the Golgi apparatus. Sci Am 1985;253:74. [PMID: 3929377] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Simons K, Ikonen E: How cells handle  cholesterol. Science 2000;290:1721. [PMID: 11099405] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Tzagoloff A: &lt;i&gt;Mitochondria&lt;/i&gt;. Plenum, 1982.  &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Weber K, Osborn M: The molecules of the cell  matrix. Sci Am 1985;253:110. [PMID: 4071030] &lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;&amp;nbsp;&lt;/b&gt;&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/actin-filaments.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg2AGpCzogv_jwuqNSNBkXd_TPhvbmrIPGRr5ygI3HT3HMQdGuoRG20TP-TTdFGvS-iRAKeLTvHLhn1hb6aQUbEOTa69sFn7DvnJmEEr2JBVaUxwLXNJmirxhp1vOlvQNbcZ1Zk1rfkux0/s72-c/Figure+2-36.bmp" width="72"/><thr:total>6</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-4188981741575843630</guid><pubDate>Thu, 23 Jun 2011 12:58:00 +0000</pubDate><atom:updated>2011-06-23T19:58:42.903+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cytoplasm</category><title>Microtubules</title><description>&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;&lt;i&gt;The cytoplasmic cytoskeleton&lt;/i&gt;&lt;/b&gt; is a complex network of  microtubules, actin filaments (microfilaments), and intermediate filaments.  These structural proteins provide for the shaping of cells and also play an  important role in the movements of organelles and intracytoplasmic vesicles. The  cytoskeleton also participates in the movement of entire cells.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=3100391851858561221" name="711860"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentHead5" style="text-align: justify;"&gt;&lt;b&gt;Microtubules&lt;/b&gt;&lt;/div&gt;&lt;div class="contentHead5" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=3100391851858561221" name="711861"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;Within the cytoplasmic matrix of eukaryotic cells are  tubular structures known as microtubules (Figures 2–30, 2–31, and 2–32).  Microtubules are also found in cytoplasmic processes called cilia (Figure 2–33)  and flagella. They have an outer diameter of 24 nm, consisting of a dense wall 5  nm thick and a hollow core 14 nm wide. Microtubules are variable in length, and  individual tubules can attain lengths of several micrometers. Occasionally, arms  or bridges are found linking two or more tubules (Figure 2–34).&lt;br /&gt;
&lt;br /&gt;
&lt;b&gt;Figure 2–30&lt;/b&gt;&lt;br /&gt;
&lt;div class="font11"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjxMWFAzjzrRv5kUdpIP5Z0b1OEJ2iHKiHSDdHAba8eMLgfZmV_diigtoIOpKBY5I0ERvN_d7mbGCPIjvrxiJMOIrLkNdN0LCKV7bccSjWJ5ajbKbmXccvE0spdFxWhlx_sdvFabLkXFIE/s1600/Figure+2-30.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjxMWFAzjzrRv5kUdpIP5Z0b1OEJ2iHKiHSDdHAba8eMLgfZmV_diigtoIOpKBY5I0ERvN_d7mbGCPIjvrxiJMOIrLkNdN0LCKV7bccSjWJ5ajbKbmXccvE0spdFxWhlx_sdvFabLkXFIE/s400/Figure+2-30.bmp" width="201" /&gt;&lt;/a&gt;&lt;span class="font11"&gt;Molecular organization of a microtubule. In  this polarized structure there is an alternation of the two subunits (&lt;img border="0" src="2.%20The%20Cytoplasm_files/alphalower.gif" /&gt; and &lt;img border="0" src="2.%20The%20Cytoplasm_files/betalower.gif" /&gt;) of the tubulin  molecule. Tubulin molecules are arranged to form 13 protofilaments, as seen in  the cross section in the upper part of the drawing.&lt;/span&gt;&lt;/div&gt;&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;b&gt;Figure 2-31&lt;/b&gt;&lt;br /&gt;
&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhsBMtY9OVi77EBEEAE1Cpyjc03J6juQbcMCVasEa57U7j6OFgyT1HzZ7rfvtLCUecBkAU15CjBKmZtc9_DCs3fift3ErLh_peWL4jbxIRH-RHZYnb2VqumpXzTI03hhtyu-qIAcu0Yecg/s1600/Figure+2-31.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="220" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhsBMtY9OVi77EBEEAE1Cpyjc03J6juQbcMCVasEa57U7j6OFgyT1HzZ7rfvtLCUecBkAU15CjBKmZtc9_DCs3fift3ErLh_peWL4jbxIRH-RHZYnb2VqumpXzTI03hhtyu-qIAcu0Yecg/s400/Figure+2-31.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11"&gt;Electron micrograph of fibroblast cytoplasm. Note the actin  filaments (AF) and microtubules (MT). &lt;small&gt;x&lt;/small&gt;60,000. (Courtesy of E  Katchburian.)&lt;/div&gt;&lt;div class="font11"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="font11"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11"&gt;&lt;b&gt;Figure 2-32&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhs_TFJJoVAno7eHUbUS81I2fZIdCfbB48GWE4DJOl9PFLACJPymA8A1B2NggssY2IFiaYC3RQWPxYbEPf7qDFEs3nXe4u_wthKNC4G1-pgJMetkd6qDgBIEVd5BG6giuarFbya6Oxc1AM/s1600/Figure+2-32.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhs_TFJJoVAno7eHUbUS81I2fZIdCfbB48GWE4DJOl9PFLACJPymA8A1B2NggssY2IFiaYC3RQWPxYbEPf7qDFEs3nXe4u_wthKNC4G1-pgJMetkd6qDgBIEVd5BG6giuarFbya6Oxc1AM/s400/Figure+2-32.bmp" width="233" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11"&gt;Electron micrograph of a section of a photosensitive retinal  cell. Note the accumulation of transversely sectioned microtubules (arrows).  Reduced slightly from &lt;small&gt;x&lt;/small&gt;80,000.&lt;/div&gt;&lt;div class="font11"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11"&gt;&lt;b&gt;Figure 2-33&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjCHLDI9kUDTWN7LIqrnVnwEHkhJHNYGHXPtWtKLIhcccLWUrFC6t-IETCcaNdO-GTWozbJjSYkkIeI0yTI5qT8qAVz_DXaGNEaA47836Xnex6Gb5P77HFUOrzBgXRHoshd3qSCyh369TU/s1600/Figure+2-33.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="258" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjCHLDI9kUDTWN7LIqrnVnwEHkhJHNYGHXPtWtKLIhcccLWUrFC6t-IETCcaNdO-GTWozbJjSYkkIeI0yTI5qT8qAVz_DXaGNEaA47836Xnex6Gb5P77HFUOrzBgXRHoshd3qSCyh369TU/s320/Figure+2-33.bmp" width="320" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11"&gt;Photomicrograph of the epithelium covering the inner surface of  the respiratory airways. Most cells in this epithelium contain numerous cilia in  their apices (free upper extremities). N, cell nuclei; M, cytoplasmic mucus  secretion, which appears dark in this preparation. H&amp;amp;E stain. High  magnification.&lt;/div&gt;&lt;div class="font11"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="font11"&gt;&lt;b&gt;Figure 2-34&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiCjOp3gGVfQ9tO7AcD9aSekGR1pMRcBoxedL9yl7lZ4aV-TphxpOaT4xQZ6_RpDj2y2VO_e5ywUyEwK4l1sgNAkXfnkEUieUVouPv3lFGAcXSNahEc3cc_ndXl_maq8mxGz78nWp0SY60/s1600/Figure+2-34.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiCjOp3gGVfQ9tO7AcD9aSekGR1pMRcBoxedL9yl7lZ4aV-TphxpOaT4xQZ6_RpDj2y2VO_e5ywUyEwK4l1sgNAkXfnkEUieUVouPv3lFGAcXSNahEc3cc_ndXl_maq8mxGz78nWp0SY60/s400/Figure+2-34.bmp" width="295" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11"&gt;Schematic representation of microtubules, cilia, and centrioles.  &lt;b&gt;A:&lt;/b&gt; Microtubules as seen in the electron microscope after fixation with  tannic acid in glutaraldehyde. The unstained tubulin subunits are delineated by  the dense tannic acid. Cross sections of tubules reveal a ring of 13 subunits of  dimers arranged in a spiral. Changes in microtubule length are due to the  addition or loss of individual tubulin subunits. &lt;b&gt;B:&lt;/b&gt; A cross section  through a cilium reveals a core of microtubules called an axoneme. The axoneme  consists of two central microtubules surrounded by nine microtubule doublets. In  the doublets, microtubule A is complete and consists of 13 subunits, whereas  microtubule B shares two or three heterodimers with A. When activated by ATP,  the dynein arms link adjacent tubules and provide for the sliding of doublets  against each other. &lt;b&gt;C:&lt;/b&gt; Centrioles consist of nine microtubule triplets  linked together in a pinwheel-like arrangement. In the triplets, microtubule A  is complete and consists of 13 subunits, whereas microtubules B and C share  tubulin subunits. Under normal circumstances, these organelles are found in  pairs with the centrioles disposed at right angles to one another.&lt;/div&gt;&lt;div class="font11"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody"&gt;The subunit of a microtubule is a heterodimer composed of  &lt;img border="0" src="2.%20The%20Cytoplasm_files/alphalower.gif" /&gt; and &lt;img border="0" src="2.%20The%20Cytoplasm_files/betalower.gif" /&gt; &lt;b&gt;tubulin&lt;/b&gt;  molecules of closely related amino acid composition, each with a molecular mass  of about 50 kDa.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-create.g?blogID=1016184987758340627" name="711863"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody"&gt;Under appropriate conditions (&lt;i&gt;in vivo&lt;/i&gt; or &lt;i&gt;in  vitro&lt;/i&gt;), tubulin subunits polymerize to form microtubules. With special  staining procedures, tubulin can be seen as heterodimers organized into a  spiral. A total of 13 units is present in one complete turn of the spiral  (Figure 2–34).&lt;/div&gt;&lt;a href="http://www.blogger.com/post-create.g?blogID=1016184987758340627" name="711864"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody"&gt;Polymerization of tubulins to form microtubules &lt;i&gt;in  vivo&lt;/i&gt; is directed by a variety of structures collectively known as  &lt;b&gt;microtubule-organizing centers&lt;/b&gt;. These structures include cilia, basal  bodies, and centrosomes. Microtubule growth, via subunit polymerization, occurs  more rapidly at one end of existing microtubules. This end is referred to as the  plus (+) end, and the other extremity is the minus (–) end. Tubulin  polymerization is under control of the concentration of Ca&lt;sup&gt;2+&lt;/sup&gt; and of  the microtubule-associated proteins, or &lt;b&gt;MAPs.&lt;/b&gt; Microtubule stability is  variable; for example, microtubules of cilia are stable, whereas microtubules of  the mitotic spindle have a short duration. The antimitotic alkaloid colchicine  binds specifically to tubulin, and when the complex tubulin–colchicine binds to  microtubules, it prevents the addition of more tubulin in the plus (+)  extremity. Mitotic microtubules are broken down because the depolymerization  continues, mainly at the minus (–) end, and the lost tubulin units are not  replaced. Another alkaloid that interferes with the mitotic microtubule is  taxol, which accelerates the formation of microtubules but at the same time  stabilizes them. All cytosolic tubulin is used in stable microtubules, and no  tubulin is left for the formation of the mitotic spindle. Another alkaloid,  vinblastine, acts by depolymerizing formed microtubules and, in a second step,  aggregating to form paracrystalline arrays of tubulin.&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;span style="color: red;"&gt;&lt;b&gt;&lt;i&gt;Medical Application&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;a href="http://www.blogger.com/post-create.g?blogID=1016184987758340627" name="711866"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBodyWithMargin"&gt;The antimitotic alkaloids are useful tools in  cell biology (eg, colchicine is used to arrest chromosomes in metaphase and to  prepare karyotypes) and in cancer chemotherapy (eg, vinblastine, vincristine,  and taxol are used to arrest cell proliferation in tumors). Because tumor cells  proliferate rapidly, they are more affected by antimitotic drugs than are normal  cells. However, chemotherapy has many undesirable consequences. For example,  some normal blood-forming cells and the epithelial cells that cover the  digestive tract also show a high rate of proliferation and are adversely  affected by chemotherapy.&lt;/div&gt;&lt;div class="contentBodyWithMargin"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;a href="http://www.blogger.com/post-create.g?blogID=1016184987758340627" name="711867"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody"&gt;Cytoplasmic microtubules are stiff structures that play a  significant role in the development and maintenance of cell shape. They are  usually present in a proper orientation, either to effect development of a given  cellular asymmetry or to maintain it. Procedures that disrupt microtubules  result in the loss of this cellular asymmetry.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-create.g?blogID=1016184987758340627" name="711868"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody"&gt;Microtubules also participate in the intracellular  transport of organelles and vesicles. Examples include axoplasmic transport in  neurons, melanin transport in pigment cells, chromosome movements by the mitotic  spindle, and vesicle movements among different cell compartments. In each of  these examples, movement is related to the presence of complex microtubule  networks, and such activities are suspended if microtubules are disrupted. The  transport guided by microtubules is under the control of special proteins called  &lt;b&gt;motor proteins,&lt;/b&gt; which use energy to move molecules and vesicles.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-create.g?blogID=1016184987758340627" name="711869"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody"&gt;Microtubules provide the basis for several complex  cytoplasmic components, including centrioles, basal bodies, cilia, and flagella.  &lt;b&gt;Centrioles&lt;/b&gt; are cylindrical structures (0.15 &lt;img border="0" src="2.%20The%20Cytoplasm_files/mulower.gif" /&gt;m in diameter and 0.3–0.5  &lt;img border="0" src="2.%20The%20Cytoplasm_files/mulower.gif" /&gt;m in length) composed  primarily of short, highly organized microtubules (Figure 2–34). Each centriole  shows nine sets of microtubules arranged in triplets. The microtubules are so  close together that adjacent microtubules of a triplet share a common wall.  Close to the nucleus of nondividing cells is a &lt;b&gt;centrosome&lt;/b&gt; (Figure 2–35)  made of a pair of centrioles surrounded by a granular material. In each pair,  the long axes of the centrioles are at right angles to each other. Before cell  division, more specifically during the S period of the interphase, each  centrosome duplicates itself so that now each centrosome has two pairs of  centrioles. During mitosis, the centrosomes divide in two, move to opposite  poles of the cell, and become organizing centers for the microtubules of the  mitotic spindle.&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;b&gt;Figure 2-35&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgx-uqa8j4KIOGYXAAR2WeT-HD0C7amqPIg05bDA3CD-5ofTSBTkq8iZBCTD34QxIvUIPqJ39xwcuMgA53IvlpbEiGmxWlijm4nXCHHf6HpOpwIEIAEsjIFmc2ShKWq0w0BMDL-GnurMrw/s1600/Figure+2-35.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgx-uqa8j4KIOGYXAAR2WeT-HD0C7amqPIg05bDA3CD-5ofTSBTkq8iZBCTD34QxIvUIPqJ39xwcuMgA53IvlpbEiGmxWlijm4nXCHHf6HpOpwIEIAEsjIFmc2ShKWq0w0BMDL-GnurMrw/s320/Figure+2-35.bmp" width="300" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11"&gt;Drawing of a centrosome with its granular protein material  surrounding a pair of centrioles, one shown at a right angle to the other. Each  centriole is composed of nine bundles of microtubules, with three microtubules  per bundle.&lt;/div&gt;&lt;div class="font11"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;b&gt;Cilia&lt;/b&gt; and &lt;b&gt;flagella&lt;/b&gt; (singular, cilium,  flagellum) are motile processes, covered by cell membrane, with a highly  organized microtubule core. Ciliated cells typically possess a large number of  cilia, each about 2–3 &lt;img border="0" src="2.%20The%20Cytoplasm_files/mulower.gif" /&gt;m in length. Flagellated cells have only one flagellum, with a length  close to 100 &lt;img border="0" src="2.%20The%20Cytoplasm_files/mulower.gif" /&gt;m. In  humans, the spermatozoa are the only cell type with a flagellum. The main  function of cilia is to sweep fluid from the surface of cell sheets. Both cilia  and flagella possess the same core organization.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-create.g?blogID=1016184987758340627" name="711871"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody"&gt;This core consists of nine pairs of microtubules  surrounding two central microtubules. This sheaf of microtubules, possessing a  &lt;b&gt;9&lt;/b&gt; + &lt;b&gt;2 pattern,&lt;/b&gt; is called an axoneme (Gr. &lt;i&gt;axon&lt;/i&gt;, axis, +  &lt;i&gt;nema&lt;/i&gt;, thread). Each of the nine peripheral pairs shares a common wall  (Figure 2–34). The microtubules in the central pair are enclosed within a  &lt;b&gt;central sheath.&lt;/b&gt; Adjacent peripheral pairs are linked to each other by  protein bridges called &lt;b&gt;nexins&lt;/b&gt; and to the central sheath by &lt;b&gt;radial  spokes.&lt;/b&gt; The microtubules of each pair are identified as A and B. Microtubule  A is complete, with 13 heterodimers, whereas B has only 10 heterodimers (in a  cross section). Extending from the surface of microtubule A are pairs of arms  formed by the protein &lt;b&gt;dynein,&lt;/b&gt; which has ATPase activity.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-create.g?blogID=1016184987758340627" name="711872"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody"&gt;At the base of each cilium or flagellum is a &lt;b&gt;basal  body,&lt;/b&gt; essentially similar to a centriole, that controls the assembly of the  axoneme.&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;span style="color: red;"&gt;&lt;b&gt;&lt;i&gt;Medical Application&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;a href="http://www.blogger.com/post-create.g?blogID=1016184987758340627" name="711874"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBodyWithMargin"&gt;Several mutations have been described in the  proteins of the cilia and flagella. They are responsible for the &lt;i&gt;&lt;b&gt;immotile  cilia syndrome,&lt;/b&gt;&lt;/i&gt; the symptoms of which are immotile spermatozoa, male  infertility, and chronic respiratory infections caused by the lack of the  cleansing action of cilia in the respiratory tract.&lt;/div&gt;&lt;div class="contentBodyWithMargin"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Bretscher MS: The molecules of the cell  membrane. Sci Am 1985;253:100. [PMID: 2416050] &lt;/td&gt;&lt;/tr&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: Microbodies in the living cell. Sci  Am 1983;248:74. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Dustin P: &lt;i&gt;Microtubules&lt;/i&gt;, 2nd ed.  Springer-Verlag, 1984. &lt;/td&gt;&lt;/tr&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Krstíc RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Mitchison TJ, Cramer LP: Actin-based cell  motility and cell locomotion. Cell 1996;84:371. [PMID: 8608590] &lt;/td&gt;&lt;/tr&gt;
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&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
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&lt;/div&gt;&lt;div class="font11"&gt;&lt;/div&gt;&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/microtubules.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjxMWFAzjzrRv5kUdpIP5Z0b1OEJ2iHKiHSDdHAba8eMLgfZmV_diigtoIOpKBY5I0ERvN_d7mbGCPIjvrxiJMOIrLkNdN0LCKV7bccSjWJ5ajbKbmXccvE0spdFxWhlx_sdvFabLkXFIE/s72-c/Figure+2-30.bmp" width="72"/><thr:total>3</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-8493183615468321208</guid><pubDate>Wed, 22 Jun 2011 17:34:00 +0000</pubDate><atom:updated>2011-06-23T19:26:06.943+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cytoplasm</category><title>Proteasomes, Peroxisomes, &amp; Secretory Vesicles</title><description>&lt;div style="text-align: justify;"&gt;&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Proteasomes&lt;/b&gt; &lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Proteasomes are multiple-protease complexes that digest proteins targeted for  destruction by attachment to ubiquitin. Protein degradation is essential to  remove excess enzyme and other proteins that become unnecessary to the cell  after they perform their normal functions, and also to remove proteins that were  incorrectly folded. Protein encoded by virus should also be destroyed.  Proteasomes deal primarily with proteins as individual molecules, whereas  lysosomes digest bulk material introduced into the cell or whole organelles and  vesicles.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8493183615468321208" name="711848"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;The proteasome has a core particle with the shape of a  barrel made of four rings stacked on each other. At each end of the core  particle is a regulatory particle that contains ATPase and recognizes proteins  with ubiquitin molecules attached. Ubiquitin is a small protein (76 amino acids)  found in all cells and is highly conserved during evolution—it has virtually the  same structure from bacteria to humans. Ubiquitin targets proteins for  destruction as follows. A molecule of ubiquitin binds to a lysine residue in the  protein to be degraded. Then other ubiquitin molecules attach to the first one;  the complex is recognized by the regulatory particle; the protein is unfolded by  the ATPases using energy from ATP; and the protein is translocated into the core  particle, where it is broken into peptides of about eight amino acids each.  These peptides are transferred to the cytosol by a process yet unknown. The  ubiquitin molecules are released by the regulatory particles for reuse.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8493183615468321208" name="711849"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;The eight-amino acid peptides may be broken down to amino  acids by cytosol enzymes, or they may have other destinations (eg, in some cells  they participate in the immune response).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead5"&gt;&lt;b&gt;Peroxisomes&lt;/b&gt; &lt;b&gt;(Microbodies)&lt;/b&gt;&lt;/div&gt;&lt;div class="contentHead5"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8493183615468321208" name="711851"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;Peroxisomes (peroxide + &lt;i&gt;soma&lt;/i&gt;, body) are spherical  membrane-limited organelles whose diameter ranges from 0.5 to 1.2 m (see Figure 2–39). Like  the mitochondria, they utilize oxygen but do not produce ATP and do not  participate directly in cellular metabolism. Peroxisomes oxidize specific  organic substrates by removing hydrogen atoms that are transferred to molecular  oxygen (O&lt;sub&gt;2&lt;/sub&gt;). This activity produces hydrogen peroxide  (H&lt;sub&gt;2&lt;/sub&gt;O&lt;sub&gt;2&lt;/sub&gt;), a substance that is very damaging to the cell.  However, H&lt;sub&gt;2&lt;/sub&gt;O&lt;sub&gt;2&lt;/sub&gt; is eliminated by the enzyme &lt;b&gt;catalase,&lt;/b&gt;  which is present in peroxisomes. Catalase transfers oxygen atoms from  H&lt;sub&gt;2&lt;/sub&gt;O&lt;sub&gt;2&lt;/sub&gt; to several compounds and also decomposes  H&lt;sub&gt;2&lt;/sub&gt;O&lt;sub&gt;2&lt;/sub&gt; to H&lt;sub&gt;2&lt;/sub&gt;O and O&lt;sub&gt;2&lt;/sub&gt; (2  H&lt;sub&gt;2&lt;/sub&gt;O&lt;sub&gt;2&lt;/sub&gt;  2 H&lt;sub&gt;2&lt;/sub&gt;O + O&lt;sub&gt;2&lt;/sub&gt;). Catalase activity also has clinical  implications. It degrades several toxic molecules and prescription drugs,  particularly in liver and kidney peroxisomes. For example, 50% of ingested ethyl  alcohol is degraded to acetic aldehyde in liver and kidney peroxisomes. Liver  and kidney peroxisomes show a higher variation in their enzyme complement than  do other peroxisomes. Their homogeneous matrix contains &lt;small&gt;D&lt;/small&gt;- and  &lt;small&gt;L&lt;/small&gt;-amino oxidases, catalase, and hydroxyacid oxidase. In some  species, but not humans, a crystalline nucleoid is present that is composed of  urate oxidase.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8493183615468321208" name="711852"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;Peroxisomes contain enzymes involved in lipid metabolism.  Thus, the -oxidation of long-chain fatty acids (18 carbons and longer) is  preferentially accomplished by peroxisomal enzymes that differ from their  mitochondrial counterparts. Certain reactions leading to the formation of bile  acids and cholesterol also have been localized in highly purified peroxisomal  fractions.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8493183615468321208" name="711853"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;Peroxisomal enzymes are synthesized on free cytosolic  polyribosomes, with a small sequence of amino acids located near the carboxyl  terminus that functions as an import signal. Proteins with this signal are  recognized by receptors located in the membrane of peroxisomes and internalized  into the organelle. The peroxisome grows in size and is divided into two smaller  peroxisomes, by a mechanism not completely understood.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;span style="color: red;"&gt;&lt;b&gt;&lt;i&gt;Medical Application&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8493183615468321208" name="711855"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;A large number of disorders arise from defective  peroxisomal proteins, because this organelle is involved in several metabolic  pathways. Probably the most common peroxisomal disorder is X-chromosome-linked  adrenoleukodystrophy, caused by a defective integral membrane protein that  participates in transporting very long-chain fatty acids into the peroxisome for -oxidation.  Accumulation of these fatty acids in body fluids destroys the myelin sheaths in  nerve tissue, causing severe neurological symptoms. Deficiency in peroxisomal  enzymes causes the fatal Zellweger syndrome, with severe muscular impairment,  liver and kidney lesions, and disorganization of the central and peripheral  nervous systems. Electron microscopy reveals empty peroxisomes in liver and  kidney cells of these patients.&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;b&gt;Secretory Vesicles, or Granules &lt;/b&gt;&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Secretory vesicles are found in those cells that store a  product until its release is signaled by a metabolic, hormonal, or neural  message (regulated secretion). These vesicles are surrounded by a membrane and  contain a concentrated form of the secretory product (Figure 2–29). The contents  of some secretory vesicles may be up to 200 times more concentrated than those  in the cisternae of the RER. Secretory vesicles containing digestive enzymes are  referred to as &lt;b&gt;zymogen granules.&lt;/b&gt;&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-29&lt;/b&gt;&lt;br /&gt;
&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEh4KgbJ9_-OOqFCHNUA8ZtbEeFJCgtNDKTyge8QiJnYOQYc4Hx1iV-Lx4x1GpTgHpfUxM_s1GT924gaUT1wsamukCtc7okBQlA9U-G7hy82S4QAueDhLcf35pN-KF6wvn-ANUfkthP3tCw/s1600/Figure+2-29.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEh4KgbJ9_-OOqFCHNUA8ZtbEeFJCgtNDKTyge8QiJnYOQYc4Hx1iV-Lx4x1GpTgHpfUxM_s1GT924gaUT1wsamukCtc7okBQlA9U-G7hy82S4QAueDhLcf35pN-KF6wvn-ANUfkthP3tCw/s320/Figure+2-29.bmp" width="305" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt; &lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Electron micrograph of a pancreatic acinar cell from the rat.  Numerous mature secretory granules (S) are seen in association with condensing  vacuoles (C) and the Golgi complex (G). &lt;small&gt;x&lt;/small&gt;18,900.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff" valign="top"&gt;&lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Afzelius BA, Eliasson R: Flagellar mutants in  man: on the heterogeneity of the immotile-cilia syndrome. J Ultrastruct Res  1979;69:43. [PMID: 501788] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Aridor M, Balch WE: Integration of endoplasmic  reticulum signaling in health and disease. Nat Med 1999;5:745. [PMID: 10395318]  &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Barrit GJ: &lt;i&gt;Communication Within Animal  Cells&lt;/i&gt;. Oxford University Press, 1992. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Becker WM et al: &lt;i&gt;The World of the Cell&lt;/i&gt;,  4th ed. Benjamin/Cummings, 2000. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Bretscher MS: The molecules of the cell  membrane. Sci Am 1985;253:100. [PMID: 2416050] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brinkley BR: Microtubule organizing centers.  Annu Rev Cell Biol 1985;1:145. [PMID: 3916316] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brown MS et al: Recycling receptors: the  round-trip itinerary of migrant membrane proteins. Cell 1983;32:663. [PMID:  6299572] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cooper GM: &lt;i&gt;The Cell: A Molecular  Approach&lt;/i&gt;. ASM Press/Sinauer Associates, Inc., 1997. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: &lt;i&gt;A Guided Tour of the Living  Cell&lt;/i&gt;. Freeman, 1984. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: Microbodies in the living cell. Sci  Am 1983;248:74. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Dustin P: &lt;i&gt;Microtubules&lt;/i&gt;, 2nd ed.  Springer-Verlag, 1984. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Farquhar MG: Progress in unraveling pathways of  Golgi traffic. Annu Rev Cell Biol 1985;1:447. [PMID: 3916320] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Fawcett D: &lt;i&gt;The Cell&lt;/i&gt;, 2nd ed. Saunders,  1981. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Krstíc RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Mitchison TJ, Cramer LP: Actin-based cell  motility and cell locomotion. Cell 1996;84:371. [PMID: 8608590] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Osborn M, Weber K: Intermediate filaments:  cell-type-specific markers in differentiation and pathology. Cell 1982;31:303.  [PMID: 6891619] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Pfeffer SR, Rothman JE: Biosynthetic protein  transport and sorting in the endoplasmic reticulum. Annu Rev Biochem  1987;56:829. [PMID: 3304148] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rothman J: The compartmental organization of  the Golgi apparatus. Sci Am 1985;253:74. [PMID: 3929377] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Simons K, Ikonen E: How cells handle  cholesterol. Science 2000;290:1721. [PMID: 11099405] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Tzagoloff A: &lt;i&gt;Mitochondria&lt;/i&gt;. Plenum, 1982.  &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Weber K, Osborn M: The molecules of the cell  matrix. Sci Am 1985;253:110. [PMID: 4071030] &lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt; &lt;/b&gt;&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/proteasomes.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEh4KgbJ9_-OOqFCHNUA8ZtbEeFJCgtNDKTyge8QiJnYOQYc4Hx1iV-Lx4x1GpTgHpfUxM_s1GT924gaUT1wsamukCtc7okBQlA9U-G7hy82S4QAueDhLcf35pN-KF6wvn-ANUfkthP3tCw/s72-c/Figure+2-29.bmp" width="72"/><thr:total>13</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-202228522941333908</guid><pubDate>Tue, 21 Jun 2011 13:05:00 +0000</pubDate><atom:updated>2011-06-21T22:00:39.875+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cytoplasm</category><title>Lysosomes</title><description>&lt;div style="text-align: justify;"&gt;Lysosomes are sites of intracellular digestion and turnover of cellular components. Lysosomes (Gr. lysis, solution, + soma, body) are membrane-limited vesicles that contain a large variety of hydrolytic enzymes (more than 40) whose main function is intracytoplasmic digestion (Figures 2–24, 2–25, and 2–26). Lysosomes are particularly abundant in cells exhibiting phagocytic activity (eg, macrophages, neutrophilic leukocytes). Although the nature and activity of lysosomal enzymes vary depending on the cell type, the most common enzymes are acid phosphatase, ribonuclease, deoxyribonuclease, proteases, sulfatases, lipases, and beta-glucuronidase. As can be seen from this list, lysosomal enzymes are capable of breaking down most biological macromolecules. Lysosomal enzymes have optimal activity at an acidic pH.&lt;/div&gt;&lt;br /&gt;
&lt;b&gt;Figure 2-24&lt;/b&gt;&lt;br /&gt;
&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgpbjgMsdWPZGAfp-QNw9qJCAe1HV2CdKLwpg1174ch0UrvgS890HoOo6YPdMnSJ1sJ0lq7VuMOJcuEr-tF88c5E28CUETtymiVDrJ19jh4ALwwcVNHTDCTRFw6Hvn-l9Mzu6TzdT3BaDo/s1600/Figure+2-24.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgpbjgMsdWPZGAfp-QNw9qJCAe1HV2CdKLwpg1174ch0UrvgS890HoOo6YPdMnSJ1sJ0lq7VuMOJcuEr-tF88c5E28CUETtymiVDrJ19jh4ALwwcVNHTDCTRFw6Hvn-l9Mzu6TzdT3BaDo/s320/Figure+2-24.bmp" style="cursor: move;" width="200" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Photomicrograph of a kidney tubule whose lumen appears in the center as a long slit. The numerous dark-stained cytoplasmic granules are lysosomes (L), organelles abundant in these kidney cells. The cell nuclei (N), some showing a nucleolus, are also seen in the photograph as dark-stained corpuscles. Toluidine blue stain. High magnification.&lt;/div&gt;&lt;br /&gt;
&lt;b&gt;Figure 2-25&lt;/b&gt;&lt;br /&gt;
&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjdwudtUlW_DNFG3cz2bmj2V8gpksnNWZDKzpI5AxpCWMK2s6ANjJ_FAMsMPwCAV9-mkxKE8_nbgUSHFwOg4SxlAPH-UB-pr0ZL6esYApqwvWIPKyDQritHeveH0DrpuLGo_G-IwP_Essg/s1600/Figure+2-25.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjdwudtUlW_DNFG3cz2bmj2V8gpksnNWZDKzpI5AxpCWMK2s6ANjJ_FAMsMPwCAV9-mkxKE8_nbgUSHFwOg4SxlAPH-UB-pr0ZL6esYApqwvWIPKyDQritHeveH0DrpuLGo_G-IwP_Essg/s320/Figure+2-25.bmp" width="314" /&gt;&lt;/a&gt;&lt;/div&gt;Electron micrograph of a macrophage. Note the abundant cytoplasmic extensions (arrows). In the center is a centriole (C) surrounded by Golgi cisternae (G). Secondary lysosomes (L) are abundant. x15,000.&lt;br /&gt;
&lt;br /&gt;
&lt;b&gt;Figure 2-26&lt;/b&gt;&lt;br /&gt;
&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEglZbANufrPE5iklVqYzRPzMwCO8C4ATXyNWOLCPRCnum-81mOayQ0x86MLxVwEIF8AES-IqfEBB0EMlvcUWKTplCcN_P9bS3AvJlye1s5AbLn0vqGuVgEGTVy7-E-XjIF_uROad-iLDvk/s1600/Figure+2-26.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEglZbANufrPE5iklVqYzRPzMwCO8C4ATXyNWOLCPRCnum-81mOayQ0x86MLxVwEIF8AES-IqfEBB0EMlvcUWKTplCcN_P9bS3AvJlye1s5AbLn0vqGuVgEGTVy7-E-XjIF_uROad-iLDvk/s320/Figure+2-26.bmp" width="226" /&gt;&lt;/a&gt;&lt;/div&gt;Electron micrograph showing four dark secondary lysosomes surrounded by numerous mitochondria.&lt;br /&gt;
&lt;br /&gt;
&lt;div style="text-align: justify;"&gt;Lysosomes, which are usually spherical, range in diameter from 0.05 to 0.5 micrometer and present a uniformly granular, electron-dense appearance in electron micrographs. In a few cells, such as macrophages and neutrophilic leukocytes, primary lysosomes are larger, up to 0.5 micrometer in diameter, and thus are just visible with the light microscope.&lt;/div&gt;&lt;br /&gt;
&lt;div style="text-align: justify;"&gt;The enveloping membrane separates the lytic enzymes from the cytoplasm, preventing the lysosomal enzymes from attacking and digesting cytoplasmic components. The fact that the lysosomal enzymes are practically inactive at the pH of the cytosol (~7.2) is an additional protection of the cell against leakage of lysosomal enzymes.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Lysosomal enzymes are synthesized and segregated in the RER and subsequently transferred to the Golgi complex, where the enzymes are modified and packaged as lysosomes. These enzymes have oligosaccharides attached to them with one or more of the mannose residues phosphorylated at the 6´ position by a phosphotransferase. There are receptors for mannose 6-phosphate-containing proteins in the RER and Golgi complex that allow these proteins to be diverted from the main secretory pathway and segregated in lysosomes.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Lysosomes that have not entered into a digestive event are identified as primary lysosomes.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Lysosomes can digest material taken into the cell from its environment. The material is taken into a phagosome or phagocytic vacuole (Figure 2–27); primary lysosomes then fuse with the membrane of the phagosome and empty their hydrolytic enzymes into the vacuole. Digestion follows, and the composite structure is now termed a secondary lysosome.&lt;/div&gt;&lt;br /&gt;
&lt;b&gt;Figure 2-27&lt;/b&gt;&lt;br /&gt;
&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhAV-n_G-MC5iIBLvwQUKmGKK1_wLKYdzcsQvi6WB8YwD8msAg6syhPO_gvtFDNwO3FConfhGJf00fqMFElvn7mG-jA2TLjckZerwGgg1bAvGCHudzMKBJi7Ju6tM63vcRDctBSzl5cl2o/s1600/Figure+2-27.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhAV-n_G-MC5iIBLvwQUKmGKK1_wLKYdzcsQvi6WB8YwD8msAg6syhPO_gvtFDNwO3FConfhGJf00fqMFElvn7mG-jA2TLjckZerwGgg1bAvGCHudzMKBJi7Ju6tM63vcRDctBSzl5cl2o/s400/Figure+2-27.bmp" width="370" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Current concepts of the functions of lysosomes. Synthesis occurs in the rough endoplasmic reticulum (RER), and the enzymes are packaged in the Golgi complex. Note the heterophagosomes, in which bacteria are being destroyed, and the autophagosomes, with RER and mitochondria in the process of digestion. Heterophagosomes and autophagosomes are secondary lysosomes. The result of their digestion can be excreted, but sometimes the secondary lysosome creates a residual body, containing remnants of undigested molecules. In some cells, such as osteoclasts, the lysosomal enzymes are secreted to the extracellular environment. Nu, nucleolus.&lt;/div&gt;&lt;br /&gt;
&lt;div style="text-align: justify;"&gt;Secondary lysosomes are generally 0.2–2 micrometer in diameter and present a heterogeneous appearance in electron microscopes because of the wide variety of materials they may be digesting.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;After digestion of the contents of the secondary lysosome, nutrients diffuse through the lysosomal-limiting membrane and enter the cytosol. Indigestible compounds are retained within the vacuoles, which are now called residual bodies (Figures 2–27 and 2–28). In some long-lived cells (eg, neurons, heart muscle), large quantities of residual bodies accumulate and are referred to as lipofuscin, or age pigment.&lt;/div&gt;&lt;br /&gt;
&lt;b&gt;Figure 2-28&lt;/b&gt;&lt;br /&gt;
&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEinKAQ4MViVdt-boTe8Nch9pJdio19j5S1nPBxnjhAKl48q8c5W6qSfrL3MHAoZRUjbMb3224Wa8xFMo1bML3-oAHT9PHUOIjcSDf7JqlHSvJNsUncYqFeA7mGUYP2sUJkrMCBDiFrouEs/s1600/Figure+2-28.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="232" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEinKAQ4MViVdt-boTe8Nch9pJdio19j5S1nPBxnjhAKl48q8c5W6qSfrL3MHAoZRUjbMb3224Wa8xFMo1bML3-oAHT9PHUOIjcSDf7JqlHSvJNsUncYqFeA7mGUYP2sUJkrMCBDiFrouEs/s320/Figure+2-28.bmp" width="320" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Section of a pancreatic acinar cell showing autophagosomes. Upper right: Two portions of the rough endoplasmic reticulum segregated by a membrane. Center: An autophagosome containing mitochondria (arrow) plus rough endoplasmic reticulum. Left: A residual body, with indigestible material. Arrowhead shows a cluster of coated vesicles.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Another function of lysosomes concerns the turnover of cytoplasmic organelles. Under certain conditions, a membrane may enclose organelles or portions of cytoplasm. Primary lysosomes fuse with this structure and initiate the lysis of the enclosed cytoplasm. The resulting secondary lysosomes are known as autophagosomes (Gr. autos, self, + phagein, to eat, + soma, body), indicating that their contents are intracellular in origin. Cytoplasmic digestion by autophagosomes is enhanced in secretory cells that have accumulated excess secretory product. The digested products of lysosomal hydrolysis are recycled by the cell to be reutilized by the cytoplasm.&lt;/div&gt;&lt;br /&gt;
&lt;div style="color: red;"&gt;&lt;i&gt;&lt;b&gt;Medical Apllication&lt;/b&gt;&lt;/i&gt;&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;In some cases, primary lysosomes release their  contents extracellularly, and their enzymes act in the extracellular milieu. An  example is the destruction of bone matrix by the collagenases synthesized and  released by osteoclasts during normal bone tissue formation (see Chapter 8:  Bone). Lysosomal enzymes acting in the extracellular milieu also play a  significant role in the response to inflammation or injury. Several possible  pathways relating to lysosome activities are schematically illustrated in Figure  2–27.&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;a href="" name="711844"&gt;&lt;/a&gt; &lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;Lysosomes play an important role in the  metabolism of several substances in the human body, and consequently many  diseases have been ascribed to deficiencies of lysosomal enzymes. In  metachromatic leukodystrophy, there is an intracellular accumulation of sulfated  cerebrosides caused by lack of lysosomal sulfatases. In most of these diseases,  a specific lysosomal enzyme is absent or inactive, and certain molecules (eg,  glycogen, cerebrosides, gangliosides, sphingomyelin, glycosaminoglycans) are not  digested. As a result, these substances accumulate in the cells, interfering  with their normal functions. This diversity of affected cell types explains the  variety of clinical symptoms observed in lysosomal diseases (Table 2–3).&lt;/div&gt;&lt;div class="contentBodyWithMargin"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;a href="" name="711981"&gt;&lt;/a&gt; &lt;table bgcolor="#ffffff" border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#cccccc" style="border-left: rgb(102,102,102) 1px solid; border-right: rgb(102,102,102) 1px solid; border-top: rgb(102,102,102) 1px solid;"&gt; &lt;table border="0" cellpadding="3" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td&gt; &lt;div class="tableTitle"&gt;Table 2–3. Examples of Diseases Caused by Lysosomal Enzyme  Failure and Accumulation of Undigested Material in Different Cell Types.&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td&gt; &lt;table bgcolor="#666666" border="0" cellpadding="3" cellspacing="1"&gt;&lt;colgroup span="3"&gt;&lt;/colgroup&gt; &lt;thead&gt;
&lt;tr class="font12"&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Disease&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Faulty Enzyme&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Main Organs Affected&lt;/th&gt;&lt;/tr&gt;
&lt;/thead&gt; &lt;tbody&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Hurler disease&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;alfa-&lt;small&gt;L&lt;/small&gt;-Iduronidase&amp;nbsp;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Skeleton and nervous  system&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Sanfilippo syndrome  A&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Heparan sulfate  sulfamidase&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Skeleton and nervous  system&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Tay-Sachs&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Hexosaminidase-A&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Nervous system&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Gaucher&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;beta-&lt;small&gt;D&lt;/small&gt;-Glycosidase&amp;nbsp;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Liver and  spleen&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;I-cell disease&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Phosphotransferase&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Skeleton and nervous  system&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff"&gt;&lt;br class="Spacer8" /&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;a href="" name="711845"&gt;&lt;/a&gt; &lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;I-cell disease (inclusion cell disease) is a rare  inherited condition clinically characterized by defective physical growth and  mental retardation and is due to a deficiency in a phosphorylating enzyme  normally present in the Golgi complex. Lysosomal enzymes coming from the RER are  not phosphorylated in the Golgi complex. Nonphosphorylated protein molecules are  not separated to form lysosomes, instead following the main secretory pathway.  The secreted lysosomal enzymes are present in the blood of patients with I-cell  disease, whereas their lysosomes are empty. Cells of these patients show large  inclusion granules that interfere with normal cellular metabolism.&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff" valign="top"&gt; &lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Afzelius BA, Eliasson R: Flagellar mutants in  man: on the heterogeneity of the immotile-cilia syndrome. J Ultrastruct Res  1979;69:43. [PMID: 501788] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Aridor M, Balch WE: Integration of endoplasmic  reticulum signaling in health and disease. Nat Med 1999;5:745. [PMID: 10395318]  &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Barrit GJ: &lt;i&gt;Communication Within Animal  Cells&lt;/i&gt;. Oxford University Press, 1992. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Becker WM et al: &lt;i&gt;The World of the Cell&lt;/i&gt;,  4th ed. Benjamin/Cummings, 2000. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Bretscher MS: The molecules of the cell  membrane. Sci Am 1985;253:100. [PMID: 2416050] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brinkley BR: Microtubule organizing centers.  Annu Rev Cell Biol 1985;1:145. [PMID: 3916316] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brown MS et al: Recycling receptors: the  round-trip itinerary of migrant membrane proteins. Cell 1983;32:663. [PMID:  6299572] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cooper GM: &lt;i&gt;The Cell: A Molecular  Approach&lt;/i&gt;. ASM Press/Sinauer Associates, Inc., 1997. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: &lt;i&gt;A Guided Tour of the Living  Cell&lt;/i&gt;. Freeman, 1984. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: Microbodies in the living cell. Sci  Am 1983;248:74. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Dustin P: &lt;i&gt;Microtubules&lt;/i&gt;, 2nd ed.  Springer-Verlag, 1984. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Farquhar MG: Progress in unraveling pathways of  Golgi traffic. Annu Rev Cell Biol 1985;1:447. [PMID: 3916320] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Fawcett D: &lt;i&gt;The Cell&lt;/i&gt;, 2nd ed. Saunders,  1981. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Krstíc RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Mitchison TJ, Cramer LP: Actin-based cell  motility and cell locomotion. Cell 1996;84:371. [PMID: 8608590] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Osborn M, Weber K: Intermediate filaments:  cell-type-specific markers in differentiation and pathology. Cell 1982;31:303.  [PMID: 6891619] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Pfeffer SR, Rothman JE: Biosynthetic protein  transport and sorting in the endoplasmic reticulum. Annu Rev Biochem  1987;56:829. [PMID: 3304148] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rothman J: The compartmental organization of  the Golgi apparatus. Sci Am 1985;253:74. [PMID: 3929377] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Simons K, Ikonen E: How cells handle  cholesterol. Science 2000;290:1721. [PMID: 11099405] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Tzagoloff A: &lt;i&gt;Mitochondria&lt;/i&gt;. Plenum, 1982.  &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Weber K, Osborn M: The molecules of the cell  matrix. Sci Am 1985;253:110. [PMID: 4071030] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/lysosomes.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgpbjgMsdWPZGAfp-QNw9qJCAe1HV2CdKLwpg1174ch0UrvgS890HoOo6YPdMnSJ1sJ0lq7VuMOJcuEr-tF88c5E28CUETtymiVDrJ19jh4ALwwcVNHTDCTRFw6Hvn-l9Mzu6TzdT3BaDo/s72-c/Figure+2-24.bmp" width="72"/><thr:total>39</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-1829345242173690885</guid><pubDate>Tue, 21 Jun 2011 12:45:00 +0000</pubDate><atom:updated>2011-06-21T19:45:32.579+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cytoplasm</category><title>Golgi Complex (Golgi Apparatus)</title><description>&lt;div style="text-align: justify;"&gt;The Golgi complex completes posttranslational modifications and packages and  places an address on products that have been synthesized by the cell. This  organelle is composed of smooth membrane-limited &lt;b&gt;cisternae&lt;/b&gt; (Figures 2–21,  2–22, and 2–23). In highly polarized cells, such as mucus-secreting goblet cells  (Figure 4–31), the Golgi complex occupies a characteristic position in the  cytoplasm between the nucleus and the apical plasma membrane.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;Figure 2-21&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjcKzV-27Wgzz1vSA2U17CpUcqOIJOF1egq-34PVDz3_az70mhdCFkC0fBnL0_6Ykfpd_9nEFwfh4ieYQ4BgaBmBhOweir0VdCQ1OUlTPNcrrTAMk4wWmVWgHsBFm0JX6Mvg9nUKQmMzO0/s1600/Figure+2-21.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="247" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjcKzV-27Wgzz1vSA2U17CpUcqOIJOF1egq-34PVDz3_az70mhdCFkC0fBnL0_6Ykfpd_9nEFwfh4ieYQ4BgaBmBhOweir0VdCQ1OUlTPNcrrTAMk4wWmVWgHsBFm0JX6Mvg9nUKQmMzO0/s320/Figure+2-21.bmp" width="320" /&gt;&lt;/a&gt;Three-dimensional representation of a Golgi complex. Through  transport vesicles that fuse with the Golgi &lt;i&gt;cis&lt;/i&gt; face, the complex  receives several types of molecules produced in the rough endoplasmic reticulum  (RER). After Golgi processing, these molecules are released from the Golgi  &lt;i&gt;trans&lt;/i&gt; face in larger vesicles to constitute secretory vesicles,  lysosomes, or other cytoplasmic components.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-22&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEi37vIGPUlzc1vIpvAZ0PNfAGMOpnrKvkxg-doxyx9i1BFE-FAu3eV9IclpB69S1Q1Wpm400q0JG19onSZF3lwgYdIZxybtRswh1MrDJkXoq1bxf0Mf1m3gdfAllrVQfgH8x7DS1o3IsEg/s1600/Figure+2-22.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="292" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEi37vIGPUlzc1vIpvAZ0PNfAGMOpnrKvkxg-doxyx9i1BFE-FAu3eV9IclpB69S1Q1Wpm400q0JG19onSZF3lwgYdIZxybtRswh1MrDJkXoq1bxf0Mf1m3gdfAllrVQfgH8x7DS1o3IsEg/s320/Figure+2-22.bmp" width="320" /&gt;&lt;/a&gt;&lt;span class="font11"&gt;Electron micrograph of a Golgi complex of a  mucous cell. To the right is a cisterna (arrow) of the rough endoplasmic  reticulum containing granular material. Close to it are small vesicles  containing this material. This is the &lt;i&gt;cis&lt;/i&gt; face of the complex. In the  center are flattened and stacked cisternae of the Golgi complex. Dilatations can  be observed extending from the ends of the cisternae. These dilatations  gradually detach themselves from the cisternae and fuse, forming the secretory  granules (&lt;b&gt;1&lt;/b&gt;, &lt;b&gt;2&lt;/b&gt;, and &lt;b&gt;3&lt;/b&gt;). This is the &lt;i&gt;trans&lt;/i&gt; face. Near  the plasma membrane of two neighboring cells is endoplasmic reticulum with a  smooth section (SER) and a rough section (RER). &lt;small&gt;x&lt;/small&gt;30,000.  &lt;b&gt;Inset:&lt;/b&gt; The Golgi complex as seen in 1-m sections of epididymis  cells impregnated with silver. &lt;small&gt;x&lt;/small&gt;1200.&lt;/span&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;span class="font11"&gt;&lt;b&gt;Figure 2-23&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhvXceuh_3elAv0QhBHKGFL4H2JTnr3r-AUZMsqvbyYW7g6zHv8D2WEltU9_7vbMjDKFTcHdGlVZEteAuT9OiNsjCW851D3zLpt_t8gGjMQ-lflQCgQ_bzhgbzyqTYi6Gr8JDuF39B9ND4/s1600/Figure+2-23.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhvXceuh_3elAv0QhBHKGFL4H2JTnr3r-AUZMsqvbyYW7g6zHv8D2WEltU9_7vbMjDKFTcHdGlVZEteAuT9OiNsjCW851D3zLpt_t8gGjMQ-lflQCgQ_bzhgbzyqTYi6Gr8JDuF39B9ND4/s400/Figure+2-23.bmp" width="326" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;span class="font11"&gt;Main events occurring during trafficking and  sorting of proteins through the Golgi complex. Numbered at the left are the main  molecular processes that take place in the compartments indicated. Note that the  labeling of lysosomal enzymes starts early in the &lt;i&gt;cis&lt;/i&gt; Golgi network. In  the &lt;i&gt;trans&lt;/i&gt; Golgi network, the glycoproteins combine with specific  receptors that guide them to their destination. On the left side of the drawing  is the returning flux of membrane, from the Golgi to the endoplasmic reticulum.  (Redrawn and reproduced, with permission, from Junqueira LC, Carneiro J:  &lt;i&gt;Biologia Celular e Molecular&lt;/i&gt;, 6th ed. Editora Guanabara,  1997.)&lt;/span&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;In most cells, there is also polarity in Golgi structure  and function. Near the Golgi complex, the RER can sometimes be seen budding off  small vesicles (transport vesicles) that shuttle newly synthesized proteins to  the Golgi complex for further processing. The Golgi cisterna nearest this point  is called the forming, convex, or &lt;i&gt;cis&lt;/i&gt; face. On the opposite side of the  Golgi complex, which is the maturing, concave, or &lt;i&gt;trans&lt;/i&gt; face, large Golgi  vacuoles accumulate (Figure 2–21). These are sometimes called &lt;b&gt;condensing  vacuoles.&lt;/b&gt;&lt;/div&gt;&lt;a href="" name="711831"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;These structures bud from the Golgi cisternae, generating  vesicles that will transport proteins to various sites. Cytochemical methods and  the electron microscope have shown that the Golgi cisternae present different  enzymes at different &lt;i&gt;cis–trans&lt;/i&gt; levels and that the Golgi complex is  important in the glycosylation, sulfating, phosphorylation, and limited  proteolysis of proteins. Furthermore, the Golgi complex initiates packing,  concentration, and storage of secretory products. Figure 2–23 provides an  overall view of the currently accepted concepts regarding transit of material  through the Golgi complex.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff" valign="top"&gt; &lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Afzelius BA, Eliasson R: Flagellar mutants in  man: on the heterogeneity of the immotile-cilia syndrome. J Ultrastruct Res  1979;69:43. [PMID: 501788] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Aridor M, Balch WE: Integration of endoplasmic  reticulum signaling in health and disease. Nat Med 1999;5:745. [PMID: 10395318]  &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Barrit GJ: &lt;i&gt;Communication Within Animal  Cells&lt;/i&gt;. Oxford University Press, 1992. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Becker WM et al: &lt;i&gt;The World of the Cell&lt;/i&gt;,  4th ed. Benjamin/Cummings, 2000. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Bretscher MS: The molecules of the cell  membrane. Sci Am 1985;253:100. [PMID: 2416050] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brinkley BR: Microtubule organizing centers.  Annu Rev Cell Biol 1985;1:145. [PMID: 3916316] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brown MS et al: Recycling receptors: the  round-trip itinerary of migrant membrane proteins. Cell 1983;32:663. [PMID:  6299572] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cooper GM: &lt;i&gt;The Cell: A Molecular  Approach&lt;/i&gt;. ASM Press/Sinauer Associates, Inc., 1997. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: &lt;i&gt;A Guided Tour of the Living  Cell&lt;/i&gt;. Freeman, 1984. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: Microbodies in the living cell. Sci  Am 1983;248:74. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Dustin P: &lt;i&gt;Microtubules&lt;/i&gt;, 2nd ed.  Springer-Verlag, 1984. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Farquhar MG: Progress in unraveling pathways of  Golgi traffic. Annu Rev Cell Biol 1985;1:447. [PMID: 3916320] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Fawcett D: &lt;i&gt;The Cell&lt;/i&gt;, 2nd ed. Saunders,  1981. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Krstíc RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Mitchison TJ, Cramer LP: Actin-based cell  motility and cell locomotion. Cell 1996;84:371. [PMID: 8608590] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Osborn M, Weber K: Intermediate filaments:  cell-type-specific markers in differentiation and pathology. Cell 1982;31:303.  [PMID: 6891619] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Pfeffer SR, Rothman JE: Biosynthetic protein  transport and sorting in the endoplasmic reticulum. Annu Rev Biochem  1987;56:829. [PMID: 3304148] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rothman J: The compartmental organization of  the Golgi apparatus. Sci Am 1985;253:74. [PMID: 3929377] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Simons K, Ikonen E: How cells handle  cholesterol. Science 2000;290:1721. [PMID: 11099405] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Tzagoloff A: &lt;i&gt;Mitochondria&lt;/i&gt;. Plenum, 1982.  &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Weber K, Osborn M: The molecules of the cell  matrix. Sci Am 1985;253:110. [PMID: 4071030] &lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/golgi-complex-golgi-apparatus.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjcKzV-27Wgzz1vSA2U17CpUcqOIJOF1egq-34PVDz3_az70mhdCFkC0fBnL0_6Ykfpd_9nEFwfh4ieYQ4BgaBmBhOweir0VdCQ1OUlTPNcrrTAMk4wWmVWgHsBFm0JX6Mvg9nUKQmMzO0/s72-c/Figure+2-21.bmp" width="72"/><thr:total>3</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-4844197134622515206</guid><pubDate>Mon, 20 Jun 2011 15:50:00 +0000</pubDate><atom:updated>2011-06-20T22:50:20.046+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">Others</category><title>Hematopoesis in Humans</title><description>&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiZIkoimemf1XzrfZuIT1Niiv0kWEqY_1CN_KKM69yd507CC3d4Ygtz9bTVYwzaCZIYJRdkhDCDUevTbkb7eiVtHFY7yDT4vbBNEz4cl4qxjz69Q-RCGTuCbmbAxffQagn6Y-1v5Z1Tz8w/s1600/Hematopoiesis+Diagram.png" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="261" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiZIkoimemf1XzrfZuIT1Niiv0kWEqY_1CN_KKM69yd507CC3d4Ygtz9bTVYwzaCZIYJRdkhDCDUevTbkb7eiVtHFY7yDT4vbBNEz4cl4qxjz69Q-RCGTuCbmbAxffQagn6Y-1v5Z1Tz8w/s400/Hematopoiesis+Diagram.png" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/hematopoesis-in-humans.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiZIkoimemf1XzrfZuIT1Niiv0kWEqY_1CN_KKM69yd507CC3d4Ygtz9bTVYwzaCZIYJRdkhDCDUevTbkb7eiVtHFY7yDT4vbBNEz4cl4qxjz69Q-RCGTuCbmbAxffQagn6Y-1v5Z1Tz8w/s72-c/Hematopoiesis+Diagram.png" width="72"/><thr:total>1</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-6119399933056473902</guid><pubDate>Sun, 19 Jun 2011 05:09:00 +0000</pubDate><atom:updated>2011-06-19T12:21:00.295+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">My Coursework</category><title>Mammary Gland (Histology)</title><description>&lt;i&gt;&lt;b&gt;Nonlactating Mammary Gland&lt;/b&gt;&lt;/i&gt;&lt;br /&gt;
&lt;div style="text-align: justify;"&gt;The mammary gland consists of 15–25 separate tubuloalveolar glands in the lobules of the mammary gland, which are separated by connective tissue and adipose tissue. Their alveoli are fully developed only in the course of pregnancy and lactation. Alveoli are rarely present in quiescent glands that do not lactate, especially in nulliparous women. This figure shows the central secretory duct (&lt;b&gt;&lt;i&gt;sinus lactiferi&lt;/i&gt;&lt;/b&gt;)&lt;b&gt; 1&lt;/b&gt; . Tubuli with blind ends and incompletely developed ducts (&lt;b&gt;&lt;i&gt;ductus lactiferi&lt;/i&gt;&lt;/b&gt;) branch from it. Note the loose sheath of cellular connective tissue &lt;b&gt;2&lt;/b&gt; . It is clearly distinguished from the &lt;b&gt;coarse fibrous connective tissue stroma&lt;/b&gt; &lt;b&gt;3&lt;/b&gt; . Quiescent, nonlactating human mammary gland.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;Figure 591&lt;/b&gt;&lt;i&gt; &lt;/i&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEj-yP61cF6PQ0G85HR5TAVZ2wSI8TMVd4WfAqx63Vqfw53ut2Ff_BkkSCNOrpfUN_18J2Q9vTysYZBW03GClcijBziUNcSFQfDjQwe6WMQaEeEeBti2xCpSrXbb62zBqUHVpZ1S3QWsouw/s1600/Non-Lactating+Mammary+Gland.JPG" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="230" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEj-yP61cF6PQ0G85HR5TAVZ2wSI8TMVd4WfAqx63Vqfw53ut2Ff_BkkSCNOrpfUN_18J2Q9vTysYZBW03GClcijBziUNcSFQfDjQwe6WMQaEeEeBti2xCpSrXbb62zBqUHVpZ1S3QWsouw/s400/Non-Lactating+Mammary+Gland.JPG" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Info:&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;1. Sinus lactiferi&lt;br /&gt;
2. Connective tissue sheath&lt;br /&gt;
3. Coarse fibrous collagenous connective tissue&lt;/b&gt;&lt;br /&gt;
&lt;span style="font-size: x-small;"&gt;&lt;i&gt;Stain: alum hematoxylin-eosin; magnification: × 80&lt;/i&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;i&gt;&lt;b&gt;Lactating Mammary Gland&lt;/b&gt;&lt;/i&gt;&lt;br /&gt;
The secretory ducts of the mammary gland start to sprout during pregnancy. &lt;i&gt;&lt;b&gt;Alveoli&lt;/b&gt;&lt;/i&gt; and lobules form. The connective tissue recedes and the gland parenchyma increases. At the height of lactation (the figure), differently shaped alveoli are found in close proximity of each other. They are separated by delicate connective tissue fibers. The &lt;b&gt;&lt;i&gt;gland epithelium&lt;/i&gt;&lt;/b&gt; &lt;b&gt;1&lt;/b&gt; has different heights, dependent on its secretory state. Lactating mammary gland. Secretory products are visible in some of the gland lumina (cf. Fig. 593).&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&amp;nbsp;&lt;b&gt;&amp;nbsp;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;b&gt;Figure 592&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjdBiRD9ysOB9LgVBvFZobvIIWXkAQLHzCOpKb7DeLR1DLhsvehZG6yGCaTQnqRNhf37TNVAiBMaI9FPXTGMlZDiVxuK4QAvk0f7tDARuoJXTeaBtjhasZ1K4i0BEqwci6CYqVCqKyPuY4/s1600/Lactating+Mammary+Gland.JPG" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="232" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjdBiRD9ysOB9LgVBvFZobvIIWXkAQLHzCOpKb7DeLR1DLhsvehZG6yGCaTQnqRNhf37TNVAiBMaI9FPXTGMlZDiVxuK4QAvk0f7tDARuoJXTeaBtjhasZ1K4i0BEqwci6CYqVCqKyPuY4/s400/Lactating+Mammary+Gland.JPG" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;Info :&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;b&gt;1. Alveoli&lt;br /&gt;
2. Connective tissue septa&lt;/b&gt;&lt;br /&gt;
&lt;span style="font-size: x-small;"&gt;&lt;i&gt;Stain: azan; magnification: × 80&lt;/i&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;span style="font-size: x-small;"&gt;&lt;span style="font-size: small;"&gt;In the active, lactating mammary gland, the epithelium of the alveoli features a rich ergastoplasm and apical fat droplets. It shows different heights. The usual preparations display round empty spaces 1 where fat droplets have been (cf. Figs. 594, 595). The apical cell membrane may rupture or, in other places, bulge dome-like into the lumen. These attributes are characteristic of apocrine glands (see Fig.133). There are patches with &lt;b&gt;secretory product&lt;/b&gt; &lt;b&gt;2&lt;/b&gt; and occasionally sloughed-off epithelial cells (upper figure). Elaborately &lt;b&gt;branchedmyoepithelial cells&lt;/b&gt; &lt;b&gt;3&lt;/b&gt; form an incomplete layer around the alveolar wall.&amp;nbsp;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;span style="font-size: x-small;"&gt;&lt;b&gt;&lt;span style="font-size: small;"&gt;Figure 593&lt;/span&gt;&lt;/b&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEie036upaFgYS-mkAcudDOm-iI3WRETS-e62USHHOub139FPUhRM8o_BywgQVdW1bN74AW3xnuAF6kDfrh9AXdplOmi1_15Df4gRUSKsEZ1Rxv8tIvwq0MXtrXo6Tmoug8hXWEf17o-tec/s1600/Lactating+Mammary+Gland+Part+2.JPG" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="227" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEie036upaFgYS-mkAcudDOm-iI3WRETS-e62USHHOub139FPUhRM8o_BywgQVdW1bN74AW3xnuAF6kDfrh9AXdplOmi1_15Df4gRUSKsEZ1Rxv8tIvwq0MXtrXo6Tmoug8hXWEf17o-tec/s400/Lactating+Mammary+Gland+Part+2.JPG" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;span style="font-size: x-small;"&gt;&lt;span style="font-size: small;"&gt;Info : &lt;/span&gt;&lt;b&gt;&lt;span style="font-size: small;"&gt;&lt;br /&gt;
&lt;/span&gt;&lt;/b&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;span style="font-size: x-small;"&gt;&lt;b&gt;&lt;span style="font-size: small;"&gt;1. Secretory product in gland cells (vacuoles)&lt;br /&gt;
2. Secretory product&lt;br /&gt;
3. Myoepithelial cells&lt;/span&gt;&lt;/b&gt;&lt;i&gt;&lt;span style="font-size: x-small;"&gt;Stain: alum hematoxylin-eosin; magnification: × 160&lt;/span&gt;&lt;/i&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;span style="font-size: x-small;"&gt;&lt;span style="font-size: small;"&gt;The fat droplets of the milk are blackened with osmium tetroxide in this section of a lactating mammary gland. They correspond to the vacuoles, which are seen in Fig. 593. Note that small droplets combine to larger spheres in some places. The gland cells and the connective tissue are stained yellowish brown.&lt;/span&gt;&lt;i&gt;&lt;span style="font-size: x-small;"&gt; &lt;/span&gt;&lt;/i&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;br /&gt;
&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;b&gt;Figure 594&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhax7kw0kTjLp9Qwe8RBcnKST0TT403wQuZxxsgASdx4wd74Y5zjoNlZtYEWITw44An1N2pdjqLaH8nlRlm6zuO81HP44HOC05u5o7NmbZfNvuIs1o2vhp5yLu41W3ygi3QJiTN-5UfwZo/s1600/Lactating+Mammary+Gland+Part+3.JPG" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="247" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhax7kw0kTjLp9Qwe8RBcnKST0TT403wQuZxxsgASdx4wd74Y5zjoNlZtYEWITw44An1N2pdjqLaH8nlRlm6zuO81HP44HOC05u5o7NmbZfNvuIs1o2vhp5yLu41W3ygi3QJiTN-5UfwZo/s400/Lactating+Mammary+Gland+Part+3.JPG" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: center;"&gt;&lt;span style="font-size: small;"&gt;&lt;b&gt;&amp;nbsp;&lt;/b&gt;&lt;span style="font-size: x-small;"&gt;&lt;i&gt;Stain: osmium tetroxide; magnification: × 160&lt;/i&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;br /&gt;
&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;The lactating mammary gland concomitantly synthesizes several different substances, which are released into the alveoli. During periods of lactation, the secretory cells produce fat droplets (see Fig.594). They combine to larger droplets and are moved to the apical cell region. Finally, they become part of vesicular formations at the plasmalemma (apical protrusions) and are pinched off as milk droplets.&lt;br /&gt;
The figure displays two &lt;b&gt;membrane encased fat droplets&lt;/b&gt; &lt;b&gt;1&lt;/b&gt; in the alveolar lumen. The large central, membrane encased fat droplet is still connected to the plasmalemma. It will obviously be pinched off shortly. At the same time, the &lt;b&gt;ergastoplasm&lt;/b&gt; &lt;b&gt;2&lt;/b&gt; of the gland cells in conjunction with the Golgi apparatus biosynthesize proteins, in particular casein and α-lactalbumin and packaged as secretory vesicles. The small &lt;b&gt;casein granules 4&lt;/b&gt; have a dense structure. They are osmiophil and can therefore easily be found. Casein granules fuse with the plasmalemma and are released by exocytosis. Four gland cells with many protein vesicles 4 are visible in this section. The gland cells have an elaborate endoplasmic reticulum 2 (ergastoplasm), &lt;b&gt;Golgi complexes 3&lt;/b&gt; and mitochondria. Sporadically, &lt;b&gt;casein granules&lt;/b&gt; are already present &lt;b&gt;in the lumen of the alveoli 5 &lt;/b&gt;.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
Lactating mammary gland from a guinea pig&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;Figure 595&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjFCOHhYS6sq-tJM35q8KYqm5qAqEEgozT5od8wO-N-opwBC8j9wMCvK4d6qVYwhMAkM3-RHqht-6PCTxmk1dPuc01RFlGtjkXES6cJFZQHU9DC_f4m_SyqJwwHBuaQfMrdkEMQn-7ZJfI/s1600/Lactating+Mammary+Gland+Part+4.JPG" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="248" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjFCOHhYS6sq-tJM35q8KYqm5qAqEEgozT5od8wO-N-opwBC8j9wMCvK4d6qVYwhMAkM3-RHqht-6PCTxmk1dPuc01RFlGtjkXES6cJFZQHU9DC_f4m_SyqJwwHBuaQfMrdkEMQn-7ZJfI/s400/Lactating+Mammary+Gland+Part+4.JPG" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Info :&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;1. Membrane-encased fat droplet&lt;br /&gt;
2. Ergastoplasm&lt;br /&gt;
3. Golgi apparatus&lt;br /&gt;
4. Vacuole with casein granule&lt;br /&gt;
5. Casein granule in the alveolar lumen&lt;/b&gt;&lt;br /&gt;
&lt;span style="font-size: x-small;"&gt;&lt;i&gt;Electron microscopy; magnification: × 6000&lt;/i&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;Reference :&lt;/b&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;span class="short_text" id="result_box" lang="en"&gt;Kuehnel, &lt;i&gt;Color Atlas of Cytology, Histology, and Microscopic Anatomy&lt;/i&gt;, 4th ed. 2003.&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/mammary-gland.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEj-yP61cF6PQ0G85HR5TAVZ2wSI8TMVd4WfAqx63Vqfw53ut2Ff_BkkSCNOrpfUN_18J2Q9vTysYZBW03GClcijBziUNcSFQfDjQwe6WMQaEeEeBti2xCpSrXbb62zBqUHVpZ1S3QWsouw/s72-c/Non-Lactating+Mammary+Gland.JPG" width="72"/><thr:total>7</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-7868529206961660412</guid><pubDate>Sat, 18 Jun 2011 11:58:00 +0000</pubDate><atom:updated>2011-06-18T18:58:27.264+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cytoplasm</category><title>Ribosomes</title><description>&lt;div class="contentBody" style="text-align: justify;"&gt;Ribosomes are small electron-dense particles, about 20  &lt;small&gt;x&lt;/small&gt; 30 nm in size. They are composed of four types of rRNA and  almost 80 different proteins.&lt;/div&gt;&lt;a href="" name="711813"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;There are two classes of ribosomes. One class is found in  prokaryotes, chloroplasts, and mitochondria; the other is found in eukaryotic  cells. Both classes of ribosomes are composed of two different-sized  subunits.&lt;/div&gt;&lt;a href="" name="711814"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;In eukaryotic cells, the RNA molecules of both subunits are  synthesized within the nucleus. Their numerous proteins are synthesized in the  cytoplasm and then enter the nucleus and associate with rRNAs. Subunits then  leave the nucleus, via nuclear pores, to enter the cytoplasm and participate in  protein synthesis.&lt;/div&gt;&lt;a href="" name="711815"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Ribosomes are intensely basophilic because of the presence  of numerous phosphate groups of the constituent rRNA that act as polyanions.  Thus, sites in the cytoplasm that are rich in ribosomes stain intensely with  basic dyes, such as methylene and toluidine blue. These basophilic sites also  stain with hematoxylin.&lt;/div&gt;&lt;a href="" name="711816"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;The individual ribosomes (Figure 2–15A) are held together  by a strand of mRNA to form &lt;b&gt;polyribosomes&lt;/b&gt; (&lt;b&gt;polysomes&lt;/b&gt;). The message  carried by mRNA is a code for the amino acid sequence of proteins being  synthesized by the cell, and the ribosomes play a crucial role in decoding, or  translating, this message during protein synthesis. Proteins synthesized for use  within the cell and destined to remain in the cytosol (eg, hemoglobin in  immature erythrocytes) are synthesized on polyribosomes existing as isolated  clusters within the cytoplasm. Polyribosomes that are attached to the membranes  of the endoplasmic reticulum (via their large subunits) translate mRNAs that  code for proteins that are segregated into the cisternae of the reticulum  (Figure 2–15B). These proteins can be secreted (eg, pancreatic and salivary  enzymes) or stored in the cell (eg, enzymes of lysosomes, proteins within  granules of white blood cells [leukocytes]). In addition, integral proteins of  the plasma membrane are synthesized on polyribosomes attached to membranes of  the endoplasmic reticulum (Figure 2–6).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-15&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgoIZU9lGel1guqZMyapVMZv98_nvJj1ox33-ASjJ7GuKX-SBAAk0r6VQjx2ksRw4gMwixQX0qG66BD6UG_z1hC6VYnjSdNIM2I-Sw3VSekSNHIMYL2agJGukL2HYV_z7FOh7JNd83Gb14/s1600/Figure+2-15.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="231" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgoIZU9lGel1guqZMyapVMZv98_nvJj1ox33-ASjJ7GuKX-SBAAk0r6VQjx2ksRw4gMwixQX0qG66BD6UG_z1hC6VYnjSdNIM2I-Sw3VSekSNHIMYL2agJGukL2HYV_z7FOh7JNd83Gb14/s400/Figure+2-15.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Diagram illustrating (&lt;b&gt;A&lt;/b&gt;) the concept that cells  synthesizing proteins (represented here by spirals) that are to remain within  the cytoplasm possess (free) polyribosomes (ie, nonadherent to the endoplasmic  reticulum). In &lt;b&gt;B&lt;/b&gt;, where the proteins are segregated in the endoplasmic  reticulum and may eventually be extruded from the cytoplasm (export proteins),  not only do the polyribosomes adhere to the membranes of rough endoplasmic  reticulum, but the proteins produced by them are injected into the interior of  the organelle across its membrane. In this way, the proteins, especially enzymes  such as ribonucleases and proteases, which could have undesirable effects on the  cytoplasm, are separated from it.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead5"&gt;&lt;b&gt;Endoplasmic Reticulum&lt;/b&gt;&lt;/div&gt;&lt;div class="contentHead5"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;a href="" name="711818"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;The cytoplasm of eukaryotic cells contains an anastomosing  network of intercommunicating channels and sacs formed by a continuous membrane,  which encloses a space called a &lt;b&gt;cisterna.&lt;/b&gt; In sections, cisternae appear  separated, but high-resolution microscopy of whole cells reveals that they are  continuous. This membrane system is called the endoplasmic reticulum (Figure  2–16). In many places the cytosolic side of the membrane is covered by  polyribosomes synthesizing protein molecules, which are injected into the  cisternae. This permits the distinction between the two types of endoplasmic  reticulum: &lt;b&gt;rough&lt;/b&gt; and &lt;b&gt;smooth&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-16&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhkEuQqnV_NFp9GzHmBrHTPqTNXp-Vj63-sbTQ6nD1H4QuoBKqA8Ntx4Oy9F_crh7fEWIQuy4mI3Kw0NFy3AdRfQgOGByHnBRPAL1dudHL1vUQBwyfRvrCtthvCub4GttE_zcEMqkwfDdY/s1600/Figure+2-16.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="226" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhkEuQqnV_NFp9GzHmBrHTPqTNXp-Vj63-sbTQ6nD1H4QuoBKqA8Ntx4Oy9F_crh7fEWIQuy4mI3Kw0NFy3AdRfQgOGByHnBRPAL1dudHL1vUQBwyfRvrCtthvCub4GttE_zcEMqkwfDdY/s400/Figure+2-16.bmp" width="400" /&gt;&lt;/a&gt;The endoplasmic reticulum is an anastomosing network of  intercommunicating channels and sacs formed by a continuous membrane. Note that  the smooth endoplasmic reticulum (foreground) is devoid of ribosomes, the small  dark dots that are present in the rough endoplasmic reticulum (background). The  cisternae of the smooth reticulum are tubular, whereas in the rough reticulum  they are flat sacs.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead8"&gt;&lt;i&gt;&lt;b&gt;Rough Endoplasmic Reticulum&lt;/b&gt;&lt;/i&gt;&lt;/div&gt;&lt;a href="" name="711820"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Rough endoplasmic reticulum (RER) is prominent in cells  specialized for protein secretion, such as pancreatic acinar cells (digestive  enzymes), fibroblasts (collagen), and plasma cells (immunoglobulins). The RER  consists of saclike as well as parallel stacks of flattened cisternae (Figure  2–13), limited by membranes that are continuous with the outer membrane of the  nuclear envelope. The name "rough endoplasmic reticulum" alludes to the presence  of polyribosomes on the cytosolic surface of this structure's membrane (Figures  2–16 and 2–17). The presence of polyribosomes also confers basophilic staining  properties on this organelle when viewed with the light microscope.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-17&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiIH9pODdImNpTyElBBM6QZ1dFGur-6d0m0oZpC8_wvm5OES3bH5d_2qR8Gue805KEZjCodjqYsuOAj3-rJIWQF-xuS-TdemDBjNDyOrVhh8Wbo63GhqFMvGPhak9R6tvfqqfpXhWzkltg/s1600/Figure+2-17.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="252" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiIH9pODdImNpTyElBBM6QZ1dFGur-6d0m0oZpC8_wvm5OES3bH5d_2qR8Gue805KEZjCodjqYsuOAj3-rJIWQF-xuS-TdemDBjNDyOrVhh8Wbo63GhqFMvGPhak9R6tvfqqfpXhWzkltg/s320/Figure+2-17.bmp" width="320" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Schematic representation of a small portion of the rough  endoplasmic reticulum to show the shape of its cisternae and the presence of  numerous ribosomes that are part of polyribosomes. It should be kept in mind  that the cisternae appear separated in sections made for electron microscopy,  but they form a continuous tunnel in the cytoplasm.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;The principal function of the RER is to segregate proteins  not destined for the cytosol. Additional functions include the initial (core)  glycosylation of glycoproteins, the synthesis of phospholipids, the assembly of  multichain proteins, and certain posttranslational modifications of newly formed  polypeptides.&lt;/div&gt;&lt;a href="" name="711822"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;All protein synthesis begins on polyribosomes that are not  attached to the endoplasmic reticulum. mRNAs of proteins destined to be  segregated in the endoplasmic reticulum contain an additional sequence of bases  at their 5´ end that codes for approximately 20–25 mainly hydrophobic amino  acids called the &lt;b&gt;signal sequence.&lt;/b&gt; Upon translation, the signal sequence  interacts with a complex of six nonidentical polypeptides plus a 7S RNA molecule  that is referred to as the &lt;b&gt;signal-recognition particle&lt;/b&gt; (&lt;b&gt;SRP&lt;/b&gt;). The  SRP inhibits further polypeptide elongation until the SRP–polyribosome complex  binds to a receptor in the membrane of the RER, the &lt;b&gt;docking protein.&lt;/b&gt; Upon  binding to the docking protein, the SRP is released from the polyribosomes,  allowing the translation to continue (Figure 2–18).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-18&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgOxcYq-uEwELagu_wuinrQnUKzivwuJ6iELwVJlf5SqLwj9OqUpWSgC9Wy_QoWukRPHcEyc7Cl8n9EcFV5O_Uh_6WRR0glwyTdvwmg-3jlJu-SslaPVzVtAVugRBK7ZJA5DtRPlJ8NcEk/s1600/Figure+2-18.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="192" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgOxcYq-uEwELagu_wuinrQnUKzivwuJ6iELwVJlf5SqLwj9OqUpWSgC9Wy_QoWukRPHcEyc7Cl8n9EcFV5O_Uh_6WRR0glwyTdvwmg-3jlJu-SslaPVzVtAVugRBK7ZJA5DtRPlJ8NcEk/s320/Figure+2-18.bmp" width="320" /&gt;&lt;/a&gt;The transport of proteins across the membrane of the rough  endoplasmic reticulum (RER). The ribosomes bind to mRNA, and the signal peptide  is initially bound to a signal-recognition particle (SRP). Ribosomes bind to the  RER by interacting with the SRP and a ribosomal receptor. The signal peptide is  then removed by a signal peptidase (not shown). These interactions cause the  opening of a pore through which the protein is extruded into the RER.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Once inside the lumen of the RER, a specific enzyme, signal  peptidase, located at the inner surface of the RER removes the signal sequence.  Translation of the protein continues, accompanied by intracisternal secondary  and tertiary structural changes as well as certain posttranslational  modifications such as hydroxylation, glycosylation, sulfating, and  phosphorylation.&lt;/div&gt;&lt;a href="" name="711824"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Proteins synthesized in the RER can have several  destinations: intracellular storage (eg, in lysosomes and specific granules of  leukocytes), provisional intracellular storage of proteins for export (eg, in  the pancreas, some endocrine cells), and as a component of other membranes (eg,  integral proteins). Figure 2–19 shows several cell types with clear differences  in the destination of the proteins they synthesize.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-19&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEheNxHDW1To_WUiowwaXutEqb0uFoYMtMjjoda9ntCBMrZORR6347id89O-1AiNZcOCc-wP1djnT3EWKJFb3adsWsUKv1sCJIwalJi_FhGqvKsgbW3yVLmh9E2eZawr9U1S0diqacxP5S0/s1600/Figure+2-19.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEheNxHDW1To_WUiowwaXutEqb0uFoYMtMjjoda9ntCBMrZORR6347id89O-1AiNZcOCc-wP1djnT3EWKJFb3adsWsUKv1sCJIwalJi_FhGqvKsgbW3yVLmh9E2eZawr9U1S0diqacxP5S0/s400/Figure+2-19.bmp" width="348" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;The ultrastructure of a cell that synthesizes (but does not  secrete) proteins on free polyribosomes (&lt;b&gt;A&lt;/b&gt;); a cell that synthesizes,  segregates, and stores proteins in organelles (&lt;b&gt;B&lt;/b&gt;); a cell that  synthesizes, segregates, and directly exports proteins (&lt;b&gt;C&lt;/b&gt;); and a cell  that synthesizes, segregates, stores in supranuclear granules, and exports  proteins (&lt;b&gt;D&lt;/b&gt;).&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead8"&gt;&lt;i&gt;&lt;b&gt;Smooth Endoplasmic Reticulum&lt;/b&gt;&lt;/i&gt;&lt;/div&gt;&lt;a href="" name="711826"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Smooth endoplasmic reticulum (SER) also takes the form of a  membranous network within the cell; however, its ultrastructure differs from  that of RER in two ways. First, SER lacks the associated polyribosomes that  characterize RER. SER membranes therefore appear smooth rather than granular.  Second, its cisternae are more tubular and more likely to appear as a profusion  of interconnected channels of various shapes and sizes than as stacks of  flattened cisternae (Figures 2–16 and 4–36). SER is continuous with the RER  (Figure 2–16).&lt;/div&gt;&lt;a href="" name="711827"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;SER is associated with a variety of specialized functional  capabilities. In cells that synthesize steroid hormones (eg, cells of the  adrenal cortex), SER occupies a large portion of the cytoplasm and contains some  of the enzymes required for steroid synthesis (Figure 4–36). SER is abundant in  liver cells, where it is responsible for the oxidation, conjugation, and  methylation processes employed by the liver to degrade certain hormones and  neutralize noxious substances such as barbiturates. Another important function  of SER is the synthesis of phospholipids for all cell membranes. The  phospholipid molecules are transferred from the SER to other membranes (1) by  vesicles that detach and are moved along cytoskeletal elements by the action of  motor proteins, (2) through direct communication with the RER, or (3) by  transfer proteins (Figure 2–20). SER contains the enzyme glucose-6-phosphatase,  which is involved in the utilization of glucose originating from glycogen in  liver cells. This enzyme is also found in RER, an example of the lack of  absolute partitioning of functions between these organelles. SER participates in  the contraction process in muscle cells, where it appears in a specialized form,  called the &lt;b&gt;sarcoplasmic reticulum,&lt;/b&gt; that is involved in the sequestration  and release of the calcium ions that regulate muscular contraction (see Chapter  10: Muscle Tissue).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-20&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiFrcpLm_i4rF46Luj5zQWbrqvczXzC5MPUb2GE5dmQHQhwZOd7RxQ8j1NH5U_vuPLqXg0pzVP_Wr2DQGpgbrzf2zMq-XPW-OO-iB2yqCp5yT6fF0oAYrzFjpQ2ibNBqNNuJZ7yZhXTF_U/s1600/Figure+2-20.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="262" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiFrcpLm_i4rF46Luj5zQWbrqvczXzC5MPUb2GE5dmQHQhwZOd7RxQ8j1NH5U_vuPLqXg0pzVP_Wr2DQGpgbrzf2zMq-XPW-OO-iB2yqCp5yT6fF0oAYrzFjpQ2ibNBqNNuJZ7yZhXTF_U/s320/Figure+2-20.bmp" width="320" /&gt;&lt;/a&gt; Schematic representation of a phospholipid-transporting  amphipathic protein. Phospholipid molecules are transported from lipid-rich  (SER) to lipid-poor membranes. (Redrawn and reproduced, with permission, from  Junqueira LC, Carneiro J: &lt;i&gt;Biologia Celular e Molecular&lt;/i&gt;, 6th ed. Editora  Guanabara, 1997.)&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;&amp;nbsp;&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Afzelius BA, Eliasson R: Flagellar mutants in  man: on the heterogeneity of the immotile-cilia syndrome. J Ultrastruct Res  1979;69:43. [PMID: 501788] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Becker WM et al: &lt;i&gt;The World of the Cell&lt;/i&gt;,  4th ed. Benjamin/Cummings, 2000. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brinkley BR: Microtubule organizing centers.  Annu Rev Cell Biol 1985;1:145. [PMID: 3916316] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cooper GM: &lt;i&gt;The Cell: A Molecular  Approach&lt;/i&gt;. ASM Press/Sinauer Associates, Inc., 1997. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: &lt;i&gt;A Guided Tour of the Living  Cell&lt;/i&gt;. Freeman, 1984. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Dustin P: &lt;i&gt;Microtubules&lt;/i&gt;, 2nd ed.  Springer-Verlag, 1984. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Farquhar MG: Progress in unraveling pathways of  Golgi traffic. Annu Rev Cell Biol 1985;1:447. [PMID: 3916320] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Fawcett D: &lt;i&gt;The Cell&lt;/i&gt;, 2nd ed. Saunders,  1981. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Krstíc RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rothman J: The compartmental organization of  the Golgi apparatus. Sci Am 1985;253:74. [PMID: 3929377] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Weber K, Osborn M: The molecules of the cell  matrix. Sci Am 1985;253:110. [PMID: 4071030] &lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="font11" style="text-align: justify;"&gt; &lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/ribosomes.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgoIZU9lGel1guqZMyapVMZv98_nvJj1ox33-ASjJ7GuKX-SBAAk0r6VQjx2ksRw4gMwixQX0qG66BD6UG_z1hC6VYnjSdNIM2I-Sw3VSekSNHIMYL2agJGukL2HYV_z7FOh7JNd83Gb14/s72-c/Figure+2-15.bmp" width="72"/><thr:total>3</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-7173078132398779467</guid><pubDate>Sat, 18 Jun 2011 11:39:00 +0000</pubDate><atom:updated>2011-06-18T18:39:47.540+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cytoplasm</category><title>Mitochondria</title><description>&lt;div style="text-align: justify;"&gt;Mitochondria (Gr. mitos, thread, + chondros, granule) are spherical or filamentous organelles 0.5–1 m wide that can attain a length of up to 10 m (Figure 2–11). They tend to accumulate in parts of the cytoplasm at which the utilization of energy is more intense, such as the apical ends of ciliated cells (Figure 17–3), in the middle piece of spermatozoa (Figure 21–10), or at the base of ion-transferring cells (Figure 4–25).&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;Figure 2-11 &lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEizqa_lFGi-Z07Y3TVZswfsjfl_q2UI-mdfff5VPK13u8vWkbKVwQGRpXb8mYoratnb-yZDC1E5oM4RJU4jKbKXvg_1uaUw-R_Mda19tU40yGwW4UnsPXa_hJAxwxv958hZcQ6ftRZaUkk/s1600/Figure+2-11.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEizqa_lFGi-Z07Y3TVZswfsjfl_q2UI-mdfff5VPK13u8vWkbKVwQGRpXb8mYoratnb-yZDC1E5oM4RJU4jKbKXvg_1uaUw-R_Mda19tU40yGwW4UnsPXa_hJAxwxv958hZcQ6ftRZaUkk/s320/Figure+2-11.bmp" width="201" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Photomicrograph of the stomach inner covering. The large cells  show many round and elongated mitochondria in the cytoplasm. The central nuclei  are also clearly seen. High magnification.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;These organelles transform the chemical energy of the  metabolites present in cytoplasm into energy that is easily accessible to the  cell. About 50% of this energy is stored as high-energy phosphate bonds in ATP  molecules, and the remaining 50% is dissipated as heat used to maintain body  temperature. Through the activity of the enzyme ATPase, ATP promptly releases  energy when required by the cell to perform any type of work, whether it is  osmotic, mechanical, electrical, or chemical.&lt;/div&gt;&lt;a href="" name="711802"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Mitochondria have a characteristic structure under the  electron microscope (Figures 2–12 and 2–13A). They are composed of an  &lt;b&gt;outer&lt;/b&gt; and an &lt;b&gt;inner mitochondrial membrane;&lt;/b&gt; the inner membrane  projects folds, termed &lt;b&gt;cristae&lt;/b&gt;, into the interior of the mitochondrion.  These membranes enclose two compartments. The compartment located between the  two membranes is termed the &lt;b&gt;intermembrane space.&lt;/b&gt; The inner membrane  encloses the other compartment—the intercristae, or matrix, space. Compared with  other cell membranes, mitochondrial membranes contain a large number of protein  molecules. Most mitochondria have flat, shelflike cristae in their interiors  (Figures 2–12 and 2–13A), whereas cells that secrete steroids (eg, adrenal  gland; see Chapter 4: Epithelial Tissue) frequently contain tubular cristae  (Figure 4–36). The cristae increase the internal surface area of mitochondria  and contain enzymes and other components of oxidative phosphorylation and  electron transport systems. The adenosine diphosphate (ADP) to ATP  phosphorylating system is localized in globular structures connected to the  inner membrane by cylindrical stalks (Figure 2–12). The globular structures are  a complex of proteins with ATP synthetase activity that, in the presence of ADP  plus inorganic phosphate and energy, forms ATP. The chemiosmotic theory suggests  that ATP synthesis occurs at the expense of a flow of protons across this  globular unit (Figure 2–14).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-12&lt;/b&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEh6BEghZzPu6javL_986vxeR0nm1Kb_5XRni_KkJ7zseM7J933ZDMdeAk6AkTRrfy__HZSKgzQ9C615P2HKv2khNtqOxbMHG5pu9oR9H1Q5D-4Eav0gttOv9aG5NJqCSoFmkFhry5aI2OM/s1600/Figure+2-12.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="278" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEh6BEghZzPu6javL_986vxeR0nm1Kb_5XRni_KkJ7zseM7J933ZDMdeAk6AkTRrfy__HZSKgzQ9C615P2HKv2khNtqOxbMHG5pu9oR9H1Q5D-4Eav0gttOv9aG5NJqCSoFmkFhry5aI2OM/s320/Figure+2-12.bmp" width="320" /&gt;&lt;/a&gt;Three-dimensional representation of a mitochondrion with its  cristae penetrating the matrix space. Note that two membranes delimiting an  intermembrane space form the wall of the mitochondrion. The cristae are covered  with globular units that participate in the formation of ATP.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&amp;nbsp;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&amp;nbsp;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&amp;nbsp;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&amp;nbsp;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&amp;nbsp;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&amp;nbsp;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&amp;nbsp;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&amp;nbsp;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;&amp;nbsp;&lt;/b&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;Figure 2-13&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjZ9p86mYd1nOigDV1bMgxwd61ccKx2A__99LSnPL5xDpQS9Ze8qnlhm2kRVyv9lWW9INrarRbYWQuhzyBKNFShLWPRELZ0tyq51hrV1aT6XY_kdjuvm-lcrPGMFgDpwBEShFMCpmM-4NY/s1600/Figure+2-13.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="280" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjZ9p86mYd1nOigDV1bMgxwd61ccKx2A__99LSnPL5xDpQS9Ze8qnlhm2kRVyv9lWW9INrarRbYWQuhzyBKNFShLWPRELZ0tyq51hrV1aT6XY_kdjuvm-lcrPGMFgDpwBEShFMCpmM-4NY/s400/Figure+2-13.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Structural lability of mitochondria. &lt;b&gt;A:&lt;/b&gt; Electron  micrograph of a section of rat pancreas. A mitochondrion with its membranes,  cristae (C), and matrix (M) is seen in the center. Numerous flattened cisternae  of rough endoplasmic reticulum with ribosomes on their cytoplasmic surfaces are  also visible. &lt;small&gt;x&lt;/small&gt;50,000. &lt;b&gt;B:&lt;/b&gt; Electron micrograph of striated  muscle from a patient with mitochondrial myopathy. The mitochondria (arrows) are  profoundly modified, showing marked swelling of the matrix.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;Figure 2-14&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjBOXoz6SwwGri2q9hlZ2ziFD_mHIR8eMhpoVl0_mL65nJe3qaVPoRwn2XH-IhbO9uT-iZJxjbnh377PqK6gnY904UxJDplZnvBKR1z9UbtuR4n_xaxTHh3JVO_UWZVZG-5e5-9Xg_YPqw/s1600/Figure+2-14.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="250" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjBOXoz6SwwGri2q9hlZ2ziFD_mHIR8eMhpoVl0_mL65nJe3qaVPoRwn2XH-IhbO9uT-iZJxjbnh377PqK6gnY904UxJDplZnvBKR1z9UbtuR4n_xaxTHh3JVO_UWZVZG-5e5-9Xg_YPqw/s400/Figure+2-14.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;The chemiosmotic theory of mitochondrial energy transduction.  &lt;b&gt;Middle:&lt;/b&gt; The flux of protons is directed from the matrix to the  intermembranous space promoted at the expense of energy derived from the  electron transport system in the inner membrane. &lt;b&gt;Left:&lt;/b&gt; Half the energy  derived from proton reflux produces ATP; the remaining energy produces heat.  &lt;b&gt;Right:&lt;/b&gt; The protein thermogenin, present in multilocular adipose tissue,  forms a shunt for reflux of protons. This reflux, which dissipates energy as  heat, does not produce ATP (see Chapter 6: Adipose Tissue).&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;div class="contentBody"&gt;The number of mitochondria and the number of cristae in  each mitochondrion are related to the energetic activity of the cells in which  they reside. Thus, cells with a high-energy metabolism (eg, cardiac muscle,  cells of some kidney tubules) have abundant mitochondria with a large number of  closely packed cristae, whereas cells with a low-energy metabolism have few  mitochondria with short cristae.&lt;/div&gt;&lt;a href="" name="711804"&gt;&lt;/a&gt; &lt;div class="contentBody"&gt;Between the cristae is an amorphous &lt;b&gt;matrix,&lt;/b&gt; rich in  protein and containing circular molecules of DNA and the three varieties of RNA.  In a great number of cell types, the mitochondrial matrix also exhibits rounded  electron-dense granules rich in Ca&lt;sup&gt;2+&lt;/sup&gt;. Although the function of this  cation in mitochondria is not completely understood, it may be important in  regulating the activity of some mitochondrial enzymes; another functional role  is related to the necessity of keeping the cytosolic concentration of  Ca&lt;sup&gt;2+&lt;/sup&gt; low. Mitochondria will pump in Ca&lt;sup&gt;2+&lt;/sup&gt; when its  concentration in the cytosol is high. Enzymes for the citric acid (Krebs) cycle  and fatty acid &lt;img border="0" src="2.%20The%20Cytoplasm_files/betalower.gif" /&gt;-oxidation are found to reside within the matrix space.&lt;/div&gt;&lt;a href="" name="711805"&gt;&lt;/a&gt; &lt;div class="contentBody"&gt;The DNA isolated from the mitochondrial matrix is double  stranded and has a circular structure, very similar to that of bacterial  chromosomes. These strands are synthesized within the mitochondrion; their  duplication is independent of nuclear DNA replication. Mitochondria contain the  three types of RNA: ribosomal RNA (rRNA), messenger RNA (mRNA), and transfer RNA  (tRNA). Mitochondrial ribosomes are smaller than cytosolic ribosomes and are  comparable to bacterial ribosomes. Protein synthesis occurs in mitochondria, but  because of the reduced amount of mitochondrial DNA, only a small proportion of  the mitochondrial proteins is produced locally. Most are encoded by nuclear DNA  and synthesized in polyribosomes located in the cytosol. These proteins have a  small amino acid sequence that is a signal for their mitochondrial destination,  and they are transported into mitochondria by an energy-requiring  mechanism.&lt;/div&gt;&lt;a href="" name="711806"&gt;&lt;/a&gt; &lt;div class="contentBody"&gt;The initial degradation of carbohydrates and fats is  carried out in the cytoplasmic matrix. The metabolic end product of these  extramitochondrial metabolic pathways is acetyl coenzyme A, which then enters  mitochondria. Within mitochondria, acetyl coenzyme A combines with oxaloacetate  to form citric acid. Within the citric acid cycle, several reactions of  decarboxylation produce CO&lt;sub&gt;2&lt;/sub&gt;, and specific reactions catalyzed by  dehydrogenase result in the removal of four pairs of H&lt;sup&gt;+&lt;/sup&gt; ions. The  H&lt;sup&gt;+&lt;/sup&gt; ions ultimately react with oxygen to form H&lt;sub&gt;2&lt;/sub&gt;O. Through  the action of cytochromes &lt;i&gt;a&lt;/i&gt;, &lt;i&gt;b&lt;/i&gt;, and &lt;i&gt;c&lt;/i&gt;, coenzyme Q, and  cytochrome oxidase, the &lt;b&gt;electron transport system,&lt;/b&gt; located in the inner  mitochondrial membrane, releases energy that is captured at three points of this  system through the formation of ATP from ADP and inorganic phosphate. Under  aerobic conditions, the combined activity of extramitochondrial glycolysis and  the citric acid cycle as well as the electron transport system gives rise to 36  molecules of ATP per molecule of glucose. This is 18 times the energy obtainable  under anaerobic circumstances, when only the glycolytic pathway can be  used.&lt;/div&gt;&lt;a href="" name="711807"&gt;&lt;/a&gt; &lt;div class="contentBody"&gt;In the process of mitosis, each daughter cell receives  approximately half the mitochondria originally present in the parent cell. New  mitochondria originate from preexisting mitochondria by growth and subsequent  division (fission) of the organelle itself.&lt;/div&gt;&lt;a href="" name="711808"&gt;&lt;/a&gt; &lt;div class="contentBody"&gt;The fact that mitochondria have some characteristics in  common with bacteria has led to the hypothesis that mitochondria originated from  an ancestral aerobic prokaryote that adapted to an endosymbiotic (intracellular  symbiosis) life within a eukaryotic host cell.&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;i&gt;&lt;span style="color: red;"&gt;&lt;b&gt;Medical Application&lt;/b&gt;&lt;/span&gt;&lt;/i&gt;&lt;a href="" name="711810"&gt;&lt;/a&gt; &lt;/div&gt;&lt;div class="contentBodyWithMargin"&gt;Several diseases of mitochondrial deficiency have  been described, and most of them are characterized by muscular dysfunction.  Because of their high-energy metabolism, skeletal muscle fibers are very  sensitive to mitochondrial defects. DNA mutations or defects that can occur in  the mitochondria or the cell nucleus cause mitocondria diseases. Mitochondrial  inheritance is maternal, because few, if any, mitochondria from the sperm  nucleus remain in the cytoplasm of the zygote. In the case of nuclear DNA  defects, inheritance may be from either parent or both parents. Generally, in  these diseases the mitochondria show morphological changes (Figure 2–13B).&lt;/div&gt;&lt;div class="contentBodyWithMargin"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Becker WM et al: &lt;i&gt;The World of the Cell&lt;/i&gt;,  4th ed. Benjamin/Cummings, 2000. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cooper GM: &lt;i&gt;The Cell: A Molecular  Approach&lt;/i&gt;. ASM Press/Sinauer Associates, Inc., 1997. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: &lt;i&gt;A Guided Tour of the Living  Cell&lt;/i&gt;. Freeman, 1984. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: Microbodies in the living cell. Sci  Am 1983;248:74. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Dustin P: &lt;i&gt;Microtubules&lt;/i&gt;, 2nd ed.  Springer-Verlag, 1984. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Farquhar MG: Progress in unraveling pathways of  Golgi traffic. Annu Rev Cell Biol 1985;1:447. [PMID: 3916320] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Fawcett D: &lt;i&gt;The Cell&lt;/i&gt;, 2nd ed. Saunders,  1981. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Krstíc RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Mitchison TJ, Cramer LP: Actin-based cell  motility and cell locomotion. Cell 1996;84:371. [PMID: 8608590] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Osborn M, Weber K: Intermediate filaments:  cell-type-specific markers in differentiation and pathology. Cell 1982;31:303.  [PMID: 6891619] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Pfeffer SR, Rothman JE: Biosynthetic protein  transport and sorting in the endoplasmic reticulum. Annu Rev Biochem  1987;56:829. [PMID: 3304148] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rothman J: The compartmental organization of  the Golgi apparatus. Sci Am 1985;253:74. [PMID: 3929377] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Simons K, Ikonen E: How cells handle  cholesterol. Science 2000;290:1721. [PMID: 11099405] &lt;br /&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Tzagoloff A: &lt;i&gt;Mitochondria&lt;/i&gt;. Plenum, 1982.  &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Weber K, Osborn M: The molecules of the cell  matrix. Sci Am 1985;253:110. [PMID: 4071030] &lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="contentBodyWithMargin"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/mitochondria.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEizqa_lFGi-Z07Y3TVZswfsjfl_q2UI-mdfff5VPK13u8vWkbKVwQGRpXb8mYoratnb-yZDC1E5oM4RJU4jKbKXvg_1uaUw-R_Mda19tU40yGwW4UnsPXa_hJAxwxv958hZcQ6ftRZaUkk/s72-c/Figure+2-11.bmp" width="72"/><thr:total>32</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-2172329731990059763</guid><pubDate>Fri, 17 Jun 2011 12:01:00 +0000</pubDate><atom:updated>2011-06-19T12:15:28.500+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">My Coursework</category><title>Placenta (Histology)</title><description>&lt;div style="text-align: justify;"&gt;&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Vertical section through a mature placenta. It consists of the &lt;b&gt;&lt;i&gt;chorionic plate (membrana chorii)&lt;/i&gt;&lt;/b&gt; &lt;b&gt;1&lt;/b&gt; , the branched microvilli and the basal plate (not shown here).&lt;b&gt;&lt;i&gt; The intervillous space&lt;/i&gt;&lt;/b&gt; &lt;b&gt;2&lt;/b&gt; with the maternal stream of blood is located between the villi. This micrograph shows the &lt;b&gt;&lt;i&gt;chorionic plate&lt;/i&gt; 1&lt;/b&gt; (upper part of the figure), which is covered by a single-layered cuboidal to &lt;b&gt;&lt;i&gt;columnar amnion epithelium&lt;/i&gt;&lt;/b&gt; &lt;b&gt;3&lt;/b&gt; (see Fig. 590). Syncytiotrophoblasts cover the chorionic plate at the intervillous space. Many termini of &lt;i&gt;&lt;b&gt;villi&lt;/b&gt;&lt;/i&gt; &lt;b&gt;4&lt;/b&gt; and branches of villi underneath the chorionic plate are sectioned. They are covered with syncytiotrophoblasts as well (see Fig.587). Fibrinoid (Langhans) is present between villi and subchorionic tissue. Fibroid material is acidophilic.&lt;/span&gt;&lt;/span&gt;&lt;br /&gt;
&lt;br /&gt;
&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;&lt;b&gt;Figure 585&lt;/b&gt; &lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhbjg2byvYAo-SL0_cXDElwwrIyOolyk46hJjK3r2y3Bw8O-hqL5IUPgOSGfwGZUHQK5MJdjVQBwRcyMfOrvKWIOYK3AYAGNycXZBip-k_F_lP5DkaIum7-Iav2ckyDRd-6QLpcu7gajd8/s1600/Placenta+1.JPG" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="201" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhbjg2byvYAo-SL0_cXDElwwrIyOolyk46hJjK3r2y3Bw8O-hqL5IUPgOSGfwGZUHQK5MJdjVQBwRcyMfOrvKWIOYK3AYAGNycXZBip-k_F_lP5DkaIum7-Iav2ckyDRd-6QLpcu7gajd8/s400/Placenta+1.JPG" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="short_text" id="result_box" lang="en"&gt;Info : &lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;b&gt;1. Chorionic plate, membrana chorii&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;b&gt;2. Intervillous space&lt;/b&gt;&lt;/span&gt;&lt;br /&gt;
&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;b&gt;3. Amnion epithelium, fetal side of the placenta&lt;/b&gt;&lt;/span&gt;&lt;br /&gt;
&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;b&gt;4. Placental villi&lt;/b&gt;&lt;/span&gt;&lt;br /&gt;
&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;b&gt;5. Subchorionic fibrinoid&lt;/b&gt;&lt;/span&gt;&lt;br /&gt;
&lt;div style="text-align: justify;"&gt;&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;span style="font-size: x-small;"&gt;&lt;i&gt;Stain: alum hematoxylin-eosin; magnification: × 40&lt;/i&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="short_text" id="result_box" lang="en"&gt;Detail of the labyrinth from a human placenta (39 weeks of gestation) with multiple villi (overview). With the exception of a fewsporadic cells, the cytotrophoblast layer has degenerated. Therefore, the &lt;b&gt;&lt;i&gt;villi&lt;/i&gt; 1&lt;/b&gt; are only surrounded by the syncytiotrophoblast. Darker proliferation nodes are seen in some places on the surface. The center part of the villi consists of loose chorionic mesodermal tissue and erythrocyte-filled capillaries. There are maternal blood cells in the &lt;b&gt;&lt;i&gt;intervillous space&lt;/i&gt;&lt;/b&gt; &lt;b&gt;2&lt;/b&gt; (&lt;i&gt;maternal milieu&lt;/i&gt;).&lt;/span&gt;&lt;br /&gt;
&lt;br /&gt;
&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;b&gt;Figure 586 &lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjVDXIrLmRRbqo8UmPrCdtM8Zhyphenhyphenj8_CPFLyHRDfIOGOaEIiNhKNvD2m5iza6XUNrSOFBg1LIwFbsBowN5OMG5thaZKOqqoRLsWVIwy4bKo5eQ-briiy4jxOG7usKBG9es-33OGfNiyzUAo/s1600/Placenta+2.JPG" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="218" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjVDXIrLmRRbqo8UmPrCdtM8Zhyphenhyphenj8_CPFLyHRDfIOGOaEIiNhKNvD2m5iza6XUNrSOFBg1LIwFbsBowN5OMG5thaZKOqqoRLsWVIwy4bKo5eQ-briiy4jxOG7usKBG9es-33OGfNiyzUAo/s400/Placenta+2.JPG" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="short_text" id="result_box" lang="en"&gt;Info : &lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;i&gt; &lt;/i&gt;&lt;b&gt;1. Placental villi&lt;br /&gt;
2. Intervillous space&lt;/b&gt;&lt;i&gt;&lt;br /&gt;
&lt;span style="font-size: x-small;"&gt;Stain: Masson-Goldner trichrome; magnification: × 65&lt;/span&gt;&lt;/i&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="short_text" id="result_box" lang="en" style="font-size: small;"&gt;Cross-section of the chorionic villi from a human placenta in the 4th gestational month. The chorionic villi consist of loosely structured &lt;i&gt;&lt;b&gt;chorionic mesoderm&lt;/b&gt;&lt;/i&gt; &lt;b&gt;1&lt;/b&gt; and a cover of ectodermal trophoblasts. &lt;i&gt;&lt;b&gt;Capillaries&lt;/b&gt;&lt;/i&gt; &lt;b&gt;2&lt;/b&gt; and rounded, eosinophilic cells with granules or vacuoles (Hofbauer cells) are found in the chorionic mesoderm.Up to the end of the 4th gestational month, the trophoblast covering is two-layered. The inner epithelium with &lt;i&gt;&lt;b&gt;cytotrophoblasts&lt;/b&gt;&lt;/i&gt; (&lt;i&gt;Langhans layer&lt;/i&gt;) &lt;b&gt;3&lt;/b&gt; clearly shows the borders of the cuboidal cells. The outer layer consists of polynucleated cells with undefined borders. The intervillous space contains sporadic maternal blood cells and fibrin clots (cf. Figs. 585, 586, 588).&lt;/span&gt;&lt;br /&gt;
&lt;br /&gt;
&lt;span class="short_text" id="result_box" lang="en" style="font-size: small;"&gt;&lt;b&gt;Figure 587 &lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhkLVWzr3k_jPTva_frxRDZMpD9N4fpgv43XPs3YguNgBBWJDfnqGBPtKRavJD89Ba51tm22sf98Lp4qmO-1sfRneSZCyIctsxMB1rIdePsYRTpNYULWkT-4KxA27-BlF00Zmb6yAq5K0Q/s1600/Placenta+3.JPG" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="221" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhkLVWzr3k_jPTva_frxRDZMpD9N4fpgv43XPs3YguNgBBWJDfnqGBPtKRavJD89Ba51tm22sf98Lp4qmO-1sfRneSZCyIctsxMB1rIdePsYRTpNYULWkT-4KxA27-BlF00Zmb6yAq5K0Q/s400/Placenta+3.JPG" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="short_text" id="result_box" lang="en" style="font-size: small;"&gt; Info :&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="short_text" id="result_box" lang="en" style="font-size: small;"&gt;&lt;b&gt;1. Mesenchymal villi stroma&lt;br /&gt;
2. Capillaries&lt;br /&gt;
3. Cytotrophoblast&lt;br /&gt;
4. Syncytiotrophoblast&lt;/b&gt;&lt;br /&gt;
&lt;span style="font-size: x-small;"&gt;&lt;i&gt;Stain: azan; magnification: × 210&lt;/i&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;&lt;span class="short_text" id="result_box" lang="en" style="font-size: small;"&gt;Reference :&lt;/span&gt;&lt;/b&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="short_text" id="result_box" lang="en" style="font-size: small;"&gt;Kuehnel, &lt;i&gt;Color Atlas of Cytology, Histology, and Microscopic Anatomy&lt;/i&gt;, 4th ed. 2003.&lt;/span&gt;&lt;br /&gt;
&lt;br /&gt;
&lt;div style="color: blue;"&gt;&lt;u&gt;&lt;b&gt;&lt;i&gt;&lt;b&gt;&lt;i&gt;&lt;span class="short_text" id="result_box" lang="en"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Continued...&lt;/span&gt;&lt;/span&gt;&lt;/i&gt;&lt;/b&gt;&lt;/i&gt;&lt;/b&gt;&lt;/u&gt;&lt;/div&gt;&lt;/div&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/placenta.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhbjg2byvYAo-SL0_cXDElwwrIyOolyk46hJjK3r2y3Bw8O-hqL5IUPgOSGfwGZUHQK5MJdjVQBwRcyMfOrvKWIOYK3AYAGNycXZBip-k_F_lP5DkaIum7-Iav2ckyDRd-6QLpcu7gajd8/s72-c/Placenta+1.JPG" width="72"/><thr:total>13</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-5029092336507789028</guid><pubDate>Thu, 16 Jun 2011 14:22:00 +0000</pubDate><atom:updated>2011-06-16T21:22:08.896+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">Histology And Its Methods of Study</category><title>Detection Methods Using High-Affinity Interactions Between Molecules</title><description>&lt;div class="contentBody" style="text-align: justify;"&gt;A molecule present in a tissue section may be identified by  using compounds that specifically interact with the molecule. The compounds that  will interact with the molecule must be tagged with a label that can be detected  under the light or electron microscope (Figure 1–20). The most commonly used  labels are fluorescent compounds (which can be seen with a fluorescence or laser  microscope), radioactive atoms (which can be detected with autoradiography),  molecules of peroxidase (which can be detected after demonstration of the enzyme  with hydrogen peroxide and 3,3&lt;i&gt;'&lt;/i&gt;-diaminoazobenzidine) or other enzymes  (which can be detected with their respective substrates), and metal (usually  gold) particles that can be observed with light and electron microscopy. These  methods are mainly used for detecting sugars, proteins, and nucleic acids.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 1-20&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiksTozxzc4Ijx3rJ0OZLlZh055yoUR07hroT1-hzv_oBCzxmrTn3_uMbN79lq5pvUZn0DFG6kJwQmRpgMpb3cS5HxKPKWLQOxbLO5MVQlDuFApIfGP4xioUO_rqXSVWVuPix1bY8COopw/s1600/Figure+1-20.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiksTozxzc4Ijx3rJ0OZLlZh055yoUR07hroT1-hzv_oBCzxmrTn3_uMbN79lq5pvUZn0DFG6kJwQmRpgMpb3cS5HxKPKWLQOxbLO5MVQlDuFApIfGP4xioUO_rqXSVWVuPix1bY8COopw/s400/Figure+1-20.bmp" width="287" /&gt;&lt;/a&gt;Compounds that have affinity toward another molecule can be  tagged with a label and used to identify that molecule. (&lt;b&gt;1&lt;/b&gt;) Molecule A  has a high and specific affinity toward a portion of molecule B. (&lt;b&gt;2&lt;/b&gt;) When  A and B are mixed, A binds to the portion of B it recognizes. (&lt;b&gt;3&lt;/b&gt;)  Molecule A may be tagged with a label that can be visualized with a light or  electron microscope. The label can be a fluorescent compound, an enzyme such as  peroxidase, a gold particle, or a radioactive atom. (&lt;b&gt;4&lt;/b&gt;) If molecule B is  present in a cell or extracellular matrix that is incubated with labeled  molecule A, molecule B can be detected.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Phalloidin, protein A, lectins, and antibodies are examples  of compounds that interact specifically with other molecules.&lt;/div&gt;&lt;a href="" name="710091"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Phalloidin,&lt;/b&gt; which is extracted from a mushroom  (&lt;i&gt;Amanita phalloides&lt;/i&gt;), interacts strongly with actin and is usually  labeled with fluorescent dyes to demonstrate actin filaments.&lt;/div&gt;&lt;a href="" name="710092"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Protein A&lt;/b&gt; is a protein obtained from  &lt;i&gt;Staphylococcus aureus&lt;/i&gt; that binds to the Fc region of immunoglobulin  (antibody) molecules. When protein A is tagged with a label, immunoglobulins can  be detected.&lt;/div&gt;&lt;a href="" name="710093"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Lectins&lt;/b&gt; are proteins or glycoproteins that are  derived mainly from plant seeds and that bind with high affinity and specificity  to carbohydrates. Different lectins bind to specific sequences of sugar  molecules. They may bind to glycoproteins, proteoglycans, and glycolipids and  are widely used to characterize membrane molecules containing defined sequences  of sugars.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead5" style="text-align: justify;"&gt;&lt;i&gt;&lt;b&gt;Immunocytochemistry&lt;/b&gt;&lt;/i&gt;&lt;/div&gt;&lt;a href="" name="710095"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;A highly specific interaction between molecules is that  between an antigen and its antibody. For this reason, methods using labeled  antibodies have proved most useful in identifying and localizing specific  proteins and glycoproteins.&lt;/div&gt;&lt;a href="" name="710096"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;The body has cells that are able to distinguish its own  molecules (self) from foreign ones. When exposed to foreign molecules—called  &lt;b&gt;antigens&lt;/b&gt;—the body may respond by producing  proteins—&lt;b&gt;antibodies&lt;/b&gt;—that react specifically and bind to the antigen, thus  helping to eliminate the foreign substance. Antibodies are proteins of a large  family, the &lt;b&gt;immunoglobulin&lt;/b&gt; family.&lt;/div&gt;&lt;a href="" name="710097"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;In immunocytochemistry, a tissue section (or cells in  culture) that may contain a certain protein is incubated in a solution  containing an antibody to this protein. The antibody binds specifically to the  protein, whose location can then be seen with either the light or electron  microscope, depending on the type of compound used to label the antibody.&lt;/div&gt;&lt;a href="" name="710098"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;One of the most important requirements for  immunocytochemistry is the availability of an antibody against the protein that  is to be detected. This means that the protein must have been previously  purified and isolated so that antibodies can be produced. Some methods for  protein isolation can be seen in Figures 1–21 and 1–22.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;b&gt;Figure 1-21&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhg6lGq2tEkE9gb0gJCiIZ8tUIfAvaovMPJe5nrgwH6tjqxYTYVyd-ShE-7r-9p31kiMSxGN7mWptZmIo6NruDLjHCHJJE39tOpVGl_pajsIXAA4Ukl9CyPetzQVepTbQKNm78gMoNuHFc/s1600/Figure+1-21.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="640" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhg6lGq2tEkE9gb0gJCiIZ8tUIfAvaovMPJe5nrgwH6tjqxYTYVyd-ShE-7r-9p31kiMSxGN7mWptZmIo6NruDLjHCHJJE39tOpVGl_pajsIXAA4Ukl9CyPetzQVepTbQKNm78gMoNuHFc/s640/Figure+1-21.bmp" width="200" /&gt;&lt;/a&gt;&lt;span class="font11"&gt;Ultracentrifugation (&lt;b&gt;A&lt;/b&gt;) and  chromatography (&lt;b&gt;B&lt;/b&gt;): methods of protein isolation. &lt;b&gt;A:&lt;/b&gt; A mixture of  proteins obtained from homogenized cells or tissues is submitted to  centrifugation at high speed for several hours. The proteins separate into  several bands, depending on the size and density of the protein molecules. The  ultracentrifugation medium is drained and collected in several fractions that  contain different proteins, which can be analyzed further. &lt;b&gt;B:&lt;/b&gt; A solution  containing a mixture of proteins obtained from homogenized cells or tissues is  added to a column filled with beads that have different chemical properties. For  instance, the beads may have different electrostatic charges (attracting  proteins according to their charge) or different sizes of pores (acting as  sieves for different-sized molecules). As the proteins migrate through the  column, their movement is slowed according to their interaction with the  particles. When the effluent is recovered, the different groups of proteins may  be collected separately.&lt;/span&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;span class="font11"&gt;&lt;b&gt;Figure 1-22&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhFSdxHu0bGJCVW6h7PyLMjjXR0U9nMzMwrp-sIt-j_9a0KXlbx1zdrbTt2tenYlyC9M950LU-521Y0hyphenhyphen-hcS3Mibr2W2DB7VIIrgy7LcXXStp6UheKEy4lv6fEk_llDlWRBBNhnZkDd3w/s1600/Figure+1-22.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="640" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhFSdxHu0bGJCVW6h7PyLMjjXR0U9nMzMwrp-sIt-j_9a0KXlbx1zdrbTt2tenYlyC9M950LU-521Y0hyphenhyphen-hcS3Mibr2W2DB7VIIrgy7LcXXStp6UheKEy4lv6fEk_llDlWRBBNhnZkDd3w/s640/Figure+1-22.bmp" width="257" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Gel electrophoresis: a method of protein isolation. &lt;b&gt;A:&lt;/b&gt;  Isolation of proteins. (&lt;b&gt;1&lt;/b&gt;) Mixtures of proteins are obtained from  homogenized cells or tissues. They are usually treated with a strong detergent  (sodium dodecyl sulfate) and with mercaptoethanol to unfold and separate the  protein subunits. (&lt;b&gt;2&lt;/b&gt;) The samples are put on top of a slab of  polyacrylamide gel, which is submitted to an electrical field. The proteins  migrate along the gel according to their size and shape. (&lt;b&gt;3&lt;/b&gt;) A mixture of  proteins of known molecular mass is added to the gel as a reference to identify  the molecular mass of the other proteins. &lt;b&gt;B:&lt;/b&gt; Detection and identification  of the proteins. (&lt;b&gt;1&lt;/b&gt;) Staining. All proteins will stain the same color.  The color intensity is proportional to the protein concentration. (&lt;b&gt;2&lt;/b&gt;)  Autoradiography. Radioactive proteins can be detected by autoradiography. An  x-ray film is apposed to the gel for a certain time and then developed.  Radioactive proteins will appear as dark bands in the film. (&lt;b&gt;3&lt;/b&gt;)  Immunoblotting. The proteins can be transferred from the gel to a nitrocellulose  membrane. The membrane is incubated with a labeled antibody made against  proteins that may be present in the sample.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="contentHead8"&gt;&lt;i&gt;&lt;b&gt;Polyclonal and Monoclonal Antibodies&lt;/b&gt;&lt;/i&gt;&lt;/div&gt;&lt;a href="" name="710100"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Let us suppose that our objective is to produce antibodies  against protein &lt;i&gt;x&lt;/i&gt; of a certain animal species (eg, a rat or a human). If  protein &lt;i&gt;x&lt;/i&gt; is already isolated, it is injected into an animal of another  species (eg, a rabbit or a goat). If the protein is sufficiently different for  this animal to recognize it as foreign—that is, as an antigen—the animal will  produce antibodies against the protein (eg, rabbit antibody against rat &lt;i&gt;x&lt;/i&gt;  or goat antibody against human &lt;i&gt;x&lt;/i&gt;). These antibodies are collected from  the animal's plasma and used for immunocytochemistry.&lt;/div&gt;&lt;a href="" name="710101"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Several groups (clones) of lymphocytes of the animal that  was injected with protein &lt;i&gt;x&lt;/i&gt; may recognize different parts of protein  &lt;i&gt;x&lt;/i&gt; and each group produces an antibody against each part. These antibodies  constitute a mixture of &lt;b&gt;polyclonal antibodies.&lt;/b&gt;&lt;/div&gt;&lt;a href="" name="710102"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;It is possible, however, to furnish protein &lt;i&gt;x&lt;/i&gt; for  lymphocytes maintained in cell culture (actually, lymphocytes fused with tumor  cells). The different clones of lymphocytes will produce different antibodies  against the several parts of protein &lt;i&gt;x&lt;/i&gt;. Each clone can be isolated and  cultured separately so that the different antibodies against protein &lt;i&gt;x&lt;/i&gt;  can be collected separately. Each of these antibodies is a &lt;b&gt;monoclonal  antibody.&lt;/b&gt; There are several advantages to using a monoclonal antibody rather  than a polyclonal antibody: for instance, a monoclonal antibody can be selected  to be highly specific and to bind strongly to the protein to be detected.  Therefore, there will be less nonspecific binding to other proteins similar to  the one being looked for. &lt;/div&gt;&lt;a href="" name="710103"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;In the &lt;b&gt;direct method of immunocytochemistry,&lt;/b&gt; the  antibody (either monoclonal or polyclonal) must be tagged with an appropriate  label. A tissue section is incubated with the antibody for some time so that the  antibody interacts with and binds to protein &lt;i&gt;x&lt;/i&gt;. The section is then  washed to remove the unbound antibody (Figure 1–23). Depending on the label that  was used (fluorescent compound, enzyme, gold particles), the section can be  observed with a light or electron microscope. If peroxidase or another enzyme  was used as a label, the enzyme must be detected before the tissue section is  observed in the microscope (see Histochemistry &amp;amp; Cytochemistry). The areas  of the tissue section that contain protein &lt;i&gt;x&lt;/i&gt; will become fluorescent or  will be covered by gold particles or by a dark precipitate if an enzyme was used  as a marker.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 1-23&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEit9S7ocFNUfashEjdGmWO7cDPeD63BxH6nvXczsT3M6zXpfyOUfTe8jA2CfE4k2zIjeLzqy0YM466yvXD7Ekysgf8uRzvYCYNtc2m_IAnGaklnC_MTclxihgeIYfh66E2yXzw_4FONXBc/s1600/Figure+1-23.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="141" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEit9S7ocFNUfashEjdGmWO7cDPeD63BxH6nvXczsT3M6zXpfyOUfTe8jA2CfE4k2zIjeLzqy0YM466yvXD7Ekysgf8uRzvYCYNtc2m_IAnGaklnC_MTclxihgeIYfh66E2yXzw_4FONXBc/s400/Figure+1-23.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;span class="font11"&gt;Direct method of immunocytochemistry.  (&lt;b&gt;1&lt;/b&gt;) Immunoglobulin molecule (Ig). (&lt;b&gt;2&lt;/b&gt;) Production of a polyclonal  antibody. Protein &lt;i&gt;x&lt;/i&gt; from a rat is injected into a rabbit. Several rabbit  Igs are produced against protein &lt;i&gt;x&lt;/i&gt;. (&lt;b&gt;3&lt;/b&gt;) Labeling the antibody. The  rabbit Igs are tagged with a label. (&lt;b&gt;4&lt;/b&gt;) Immunocytochemical reaction. The  rabbit Igs recognize and bind to different parts of protein &lt;i&gt;x&lt;/i&gt;.&lt;/span&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;The &lt;b&gt;indirect method of immunocytochemistry&lt;/b&gt; is more  sensitive but requires more steps. Let us suppose that our objective is to  detect protein &lt;i&gt;x&lt;/i&gt;, present in rats. Before proceeding to the  immunochemical reaction, two procedures are needed: (1) antibodies (polyclonal  or monoclonal) to rat protein &lt;i&gt;x&lt;/i&gt; must first be produced in an animal of  another species (eg, a rabbit); (2) in a parallel procedure, immunoglobulin from  a normal (noninjected) rabbit must be injected into an animal of a third species  (eg, a goat). Rabbit immunoglobulins are considered foreign by a goat and are  thus capable of inducing the production of an antibody (an antiantibody or  antiimmunoglobulin) in that animal.&lt;/div&gt;&lt;a href="" name="710105"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Indirect immunocytochemical detection is performed by  initially incubating a section of a rat tissue believed to contain protein  &lt;i&gt;x&lt;/i&gt; with rabbit anti-&lt;i&gt;x&lt;/i&gt; antibody. After washing, the tissue sections  are incubated with labeled goat antibody against rabbit antibodies. The  antiantibodies will bind to the rabbit antibody that had previously recognized  protein &lt;i&gt;x&lt;/i&gt; (Figure 1–24). Protein &lt;i&gt;x&lt;/i&gt; can then be detected by using a  microscopic technique appropriate for the label used in the secondary antibody.  There are other indirect methods that involve the use of other intermediate  molecules, such as the biotin-avidin technique.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;b&gt;Figure 1-24&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhTY9vC6FwhJOzhbs2w8PxKWeEEv9pfMkDaAUNexif8AyV1D9dyP84sukLeAxzZCiUiGnOtQtiPg93ls6lf3aKrgcQKhkZz8_E5eoHE-dFEh7I4057zCVqCtaMxtGtyZEnv9CEhXjV0Bu4/s1600/Figure+1-24.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="141" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhTY9vC6FwhJOzhbs2w8PxKWeEEv9pfMkDaAUNexif8AyV1D9dyP84sukLeAxzZCiUiGnOtQtiPg93ls6lf3aKrgcQKhkZz8_E5eoHE-dFEh7I4057zCVqCtaMxtGtyZEnv9CEhXjV0Bu4/s400/Figure+1-24.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;span class="font11"&gt;Indirect method of immunocytochemistry.  (&lt;b&gt;1&lt;/b&gt;) Production of a primary polyclonal antibody. Protein &lt;i&gt;x&lt;/i&gt; from a  rat is injected into a rabbit. Several rabbit immunoglobulins (Ig) are produced  against protein &lt;i&gt;x&lt;/i&gt;. (&lt;b&gt;2&lt;/b&gt;) Production of secondary antibody. Ig from a  nonimmune (normal) rabbit is injected into a goat. Goat Igs against rabbit Ig  are produced. The goat Igs are then isolated and tagged with a label. (&lt;b&gt;3&lt;/b&gt;)  First step of the immunocytochemical reaction. The rabbit Igs recognize and bind  to different parts of protein &lt;i&gt;x&lt;/i&gt;. (&lt;b&gt;4&lt;/b&gt;) Second step of the  immunocytochemical reaction. Labeled goat Igs recognize and bind to different  parts of rabbit immunoglobulin molecules, therefore labeling protein  &lt;i&gt;x&lt;/i&gt;.&lt;/span&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt; &lt;/div&gt;&lt;div class="contentBody"&gt;&lt;span style="color: red;"&gt;&lt;b&gt;&lt;i&gt;Medical Application&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;a href="" name="710107"&gt;&lt;/a&gt; &lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;Immunocytochemistry has contributed significantly  to research in cell biology and to the improvement of medical diagnostic  procedures. Figures 1–25, 1–26, 1–27, and 1–28 show examples of  immunocytochemical detection of molecules. Table 1–1 shows some of the routine  applications of immunocytochemical procedures in clinical practice.&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;table bgcolor="#ffffff" border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#cccccc" style="border-left: rgb(102,102,102) 1px solid; border-right: rgb(102,102,102) 1px solid; border-top: rgb(102,102,102) 1px solid;"&gt;&lt;table border="0" cellpadding="3" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td&gt; &lt;div class="tableTitle"&gt;Table 1–1. Commonly Used Proteins (Antigens) Important for  Immunocytochemical Diagnosis and Treatment of Disease.&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td&gt; &lt;table bgcolor="#666666" border="0" cellpadding="3" cellspacing="1"&gt;&lt;colgroup span="2"&gt;&lt;/colgroup&gt; &lt;thead&gt;
&lt;tr class="font12"&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Antigens&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Diagnosis&lt;/th&gt;&lt;/tr&gt;
&lt;/thead&gt; &lt;tbody&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" colspan="2" valign="top"&gt;&lt;b&gt;Intermediate  filament proteins&lt;/b&gt;&amp;nbsp;&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Cytokeratins&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Tumors of epithelial  origin&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Glial fibrillary acid  protein&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Tumors of some glial  cells&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Vimentin&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Tumors of connective  tissue&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Desmin&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Tumors of  muscle&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" colspan="2" valign="top"&gt;&lt;b&gt;Other  proteins&lt;/b&gt;&amp;nbsp;&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Protein and polypeptide  hormones&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Protein or polypeptide  hormone–producing tumors&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Carcinoembryonic antigen  (CEA)&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Glandular tumors, mainly  of the digestive tract and breast&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Steroid hormone  receptors&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Breast duct cell  tumors&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Antigens produced by  viruses&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Specific virus infections&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
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&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;b&gt;Figure 1-25&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEghWlObF9w0e4C-DzXweBGXpWZSEAFHHo92k2HgGThMwZCVWdcFJ-pQ9OhkALysdE9rJj040qtCAJcrRl-xX5yp9iLNoVZl-uu718ZcU1Tz-3MOh_MjCo7YlBWkRU18W38vSGzmtlP7g8k/s1600/Figure+1-25.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="288" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEghWlObF9w0e4C-DzXweBGXpWZSEAFHHo92k2HgGThMwZCVWdcFJ-pQ9OhkALysdE9rJj040qtCAJcrRl-xX5yp9iLNoVZl-uu718ZcU1Tz-3MOh_MjCo7YlBWkRU18W38vSGzmtlP7g8k/s400/Figure+1-25.bmp" width="400" /&gt;&lt;/a&gt;Photomicrograph of a mouse decidual cell grown in vitro. The  protein desmin, which forms intermediate filaments, was detected with an  indirect immunofluorescence technique. A mesh of fluorescent intermediate  filaments occupies most of the cytoplasm. The nucleus (N) is stained blue. High  magnification. (Courtesy of FG Costa.)&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;b&gt;&amp;nbsp;&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;b&gt;Figure 1-26&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgDjN5gJ5H8u8_UJs_abVM_T32IGnedOnwWfnFsngWR4Jz7ScmpHp75gMkkL-mXedslwLbQ5F90vM3zCrMcQSqv6QAWtBl17xYhWZjjle9bUTRWfYlkK3j6iuMeZ8DVa7fZGmmcg9344Kg/s1600/Figure+1-26.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgDjN5gJ5H8u8_UJs_abVM_T32IGnedOnwWfnFsngWR4Jz7ScmpHp75gMkkL-mXedslwLbQ5F90vM3zCrMcQSqv6QAWtBl17xYhWZjjle9bUTRWfYlkK3j6iuMeZ8DVa7fZGmmcg9344Kg/s400/Figure+1-26.bmp" width="321" /&gt;&lt;/a&gt;&lt;span class="font11"&gt;Photomicrograph of a section of small  intestine in which an antibody against the enzyme lysozyme was applied to  demonstrate lysosomes in macrophages and Paneth cells. The brown color,  indicating the presence of lysozyme, results from the reaction done to show  peroxidase, which was linked to the secondary antibody. Nuclei were  counterstained with hematoxylin. Medium magnification.&lt;/span&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;span class="font11"&gt;&lt;b&gt;Figure 1-27&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjgI7Ie5PntU4FbXSKWQRqD3aFNbd5WZZCUM0E32Dv8z3_vwUPgnARxvVcCrGrF_CZHZdLYzox-TeklqJQxlQil4Ar9hA89CEgsrVsoMS1AdvhWsOLstmMC8vfVDxbQvwqEmRRmjHlfBA4/s1600/Figure+1-27.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjgI7Ie5PntU4FbXSKWQRqD3aFNbd5WZZCUM0E32Dv8z3_vwUPgnARxvVcCrGrF_CZHZdLYzox-TeklqJQxlQil4Ar9hA89CEgsrVsoMS1AdvhWsOLstmMC8vfVDxbQvwqEmRRmjHlfBA4/s400/Figure+1-27.bmp" width="255" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Carcinoembryonic antigen is a protein present in several  malignant tumors mainly of the breast and intestines. This photomicrograph is an  immunocytochemical demonstration of carcinoembryonic antigen in a section of  large intestine adenocarcinoma. The antibody was labeled with peroxidase and the  brown precipitate indicates tumor cells. The counterstain was hematoxylin.  Medium magnification.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;span class="font11"&gt;&lt;br /&gt;
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&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;b&gt;Figure 1–28&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhiOlO9_8I-XYPop0h4119zVFRaHITbPAi49fipd5XFZX1U4Lsm7nIY3vD8p12CCCkCjE2gYEx_AvY8iHHUh7AYax7psReODT4Tdmz6aaraWu6XnAOFH-8wMXiyRD4zggCpRY0r95xvnJM/s1600/Figure+1-28.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="228" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhiOlO9_8I-XYPop0h4119zVFRaHITbPAi49fipd5XFZX1U4Lsm7nIY3vD8p12CCCkCjE2gYEx_AvY8iHHUh7AYax7psReODT4Tdmz6aaraWu6XnAOFH-8wMXiyRD4zggCpRY0r95xvnJM/s320/Figure+1-28.bmp" width="320" /&gt;&lt;/a&gt;Electron micrograph showing a section of a pancreatic acinar  cell that was incubated with antiamylase antibody and stained by protein A  coupled with gold particles. Protein A has high affinity toward antibody  molecules. The gold particles appear as very small black dots over the secretory  granules. (Courtesy of M Bendayan.)&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="contentHead5" style="text-align: justify;"&gt;&lt;b&gt;Hybridization Techniques&lt;/b&gt;&lt;/div&gt;&lt;a href="" name="710109"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;The central challenge in modern cell biology is to  understand the workings of the cell in molecular detail. This goal requires  techniques that permit analysis of the molecules involved in the process of  information flow from DNA to protein. Many techniques are based on  &lt;b&gt;hybridization.&lt;/b&gt; Hybridization is the binding between two single strands of  nucleic acids (DNA with DNA, RNA with RNA, or RNA with DNA) that recognize each  other if the strands are complementary. The greater the similarities of the  sequences, the more readily complementary strands form "hybrid" double-stranded  molecules. Hybridization thus allows the specific identification of sequences of  DNA or RNA.&lt;/div&gt;&lt;a href="" name="710110"&gt;&lt;/a&gt; &lt;div class="contentHead8" style="text-align: justify;"&gt;&lt;b&gt;&lt;i&gt;In Situ&lt;/i&gt; Hybridization&lt;/b&gt;&lt;/div&gt;&lt;a href="" name="710111"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;When applied directly to cells and tissue sections, smears,  or chromosomes of squashed mitotic cells, the technique is called &lt;i&gt;in situ  hybridization.&lt;/i&gt; This technique is ideal for determining if a cell has a  specific sequence of DNA (such as a gene or part of a gene), for identifying the  cells in which a specific gene is being transcribed, or for determining the  localization of a gene in a specific chromosome. The DNA inside the cell must be  initially denatured by heat or by denaturing agents so that both strands of the  DNA separate. They are then ready to be hybridized with a segment of  single-stranded DNA or RNA that is complementary to the sequence to be detected.  This sequence is called a &lt;b&gt;probe.&lt;/b&gt; The probe may be obtained by cloning, by  polymerase chain reaction (PCR) amplification of the target sequence, or by  synthesis if the desired sequence is short. The probe must be tagged with a  label, usually a radioactive isotope (which can be localized by autoradiography)  or a modified nucleotide (digoxygenin), which can be identified by  immunocytochemistry.&lt;/div&gt;&lt;a href="" name="710112"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;In &lt;i&gt;in situ&lt;/i&gt; hybridization, the tissue section,  cultured cells, smears, or chromosomes of squashed mitotic cells must first be  heated to separate the double strands of their DNA. A solution containing the  probe is then placed over the specimen for a period of time necessary for  hybridization. After washing off the excess probe, the localization of the bound  probe is revealed through its label (Figure 1–29).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 1-29&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjSPLSxk3pnLTNF32KJSg72YrVAHkmuzfUcKDznIngv2rOQKNmYjbV01MHigDACK59FQk_YnGM4F_YLwvPkTOQbkkzGcNtI2dHlcK7vrwiu5pZiGPm6HT33Oa_irlXXGBC2_FSg66Mavw4/s1600/Figure+1-29.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjSPLSxk3pnLTNF32KJSg72YrVAHkmuzfUcKDznIngv2rOQKNmYjbV01MHigDACK59FQk_YnGM4F_YLwvPkTOQbkkzGcNtI2dHlcK7vrwiu5pZiGPm6HT33Oa_irlXXGBC2_FSg66Mavw4/s320/Figure+1-29.bmp" width="264" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Tissue section of a benign epithelial tumor (condyloma)  submitted to &lt;i&gt;in situ&lt;/i&gt; hybridization. The brown areas are places where DNA  of human papillomavirus type 2 is present. The counterstain was hematoxylin.  Medium magnification. (Courtesy of JE Levi.)&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Hybridization can also be performed with purified DNA or  RNA in solid supports. Mixtures of DNA or RNA are separated by electrophoresis  in an agarose gel or a polyacrylamide gel. After electrophoresis, the fragments  of nucleic acids are transferred to a nylon or nitrocellulose sheet by solvent  drag: a buffer flows through the gel and membrane by capillarity, carrying the  nucleic acid molecules that bind strongly to the nylon or nitrocellulose sheet,  where the nucleic acids can be further analyzed. This technique of DNA  identification is called Southern blotting. When electrophoresis of RNA is  performed, the technique is called Northern blotting.&lt;/div&gt;&lt;a href="" name="710114"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Hybridization techniques are highly specific and are  routinely used in research, clinical diagnosis, and forensic medicine.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Alberts B et al: &lt;i&gt;Molecular Biology of the  Cell,&lt;/i&gt; 3rd ed. Garland, 1994. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Bancroft JD, Stevens A: &lt;i&gt;Theory and Practice  of Histological Techniques,&lt;/i&gt; 2nd ed. Churchill Livingstone, 1990. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cuello ACC: &lt;i&gt;Immunocytochemistry&lt;/i&gt;. Wiley,  1983. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Darnell J, Lodish H, Baltimore D: &lt;i&gt;Molecular  Cell Biology,&lt;/i&gt; 2nd ed. Scientific American Books, 1990. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Hayat MA: &lt;i&gt;Stains and Cytochemical  Methods&lt;/i&gt;. Plenum, 1993. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;James J: &lt;i&gt;Light Microscopic Techniques in  Biology and Medicine&lt;/i&gt;. Martinus Nijhoff, 1976. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Junqueira LCU et al: Differential staining of  collagen types I, II and III by Sirius Red and polarization microscopy. Arch  Histol Jpn 1978;41:267. [PMID: 82432] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Meek GA: &lt;i&gt;Practical Electron Microscopy for  Biologists&lt;/i&gt;. Wiley, 1976. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Pease AGE: &lt;i&gt;Histochemistry: Theoretical and  Applied,&lt;/i&gt; 4th ed. Churchill Livingstone, 1980. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rochow TG, Tucker PA: &lt;i&gt;Introduction to  Microscopy by Means of Light, Electrons, X Rays, or Acoustics&lt;/i&gt;. Plenum, 1994.  &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rogers AW: &lt;i&gt;Techniques of  Autoradiography,&lt;/i&gt; 3rd ed. Elsevier, 1979. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rubbi CP: &lt;i&gt;Light Microscopy. Essential  Data&lt;/i&gt;. Wiley, 1994. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Spencer M: &lt;i&gt;Fundamentals of Light  Microscopy&lt;/i&gt;. Cambridge University Press, 1982. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Stoward PJ, Polak JM (editors):  &lt;i&gt;Histochemistry: The Widening Horizons of Its Applications in Biological  Sciences&lt;/i&gt;. Wiley, 1981. &lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;&amp;nbsp;&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt; &lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/detection-methods-using-high-affinity.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiksTozxzc4Ijx3rJ0OZLlZh055yoUR07hroT1-hzv_oBCzxmrTn3_uMbN79lq5pvUZn0DFG6kJwQmRpgMpb3cS5HxKPKWLQOxbLO5MVQlDuFApIfGP4xioUO_rqXSVWVuPix1bY8COopw/s72-c/Figure+1-20.bmp" width="72"/><thr:total>29</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-6295843705011561989</guid><pubDate>Thu, 16 Jun 2011 13:56:00 +0000</pubDate><atom:updated>2011-06-16T20:56:36.275+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">Histology And Its Methods of Study</category><title>Histochemistry &amp; Cytochemistry</title><description>&lt;div class="contentBody" style="text-align: justify;"&gt;The terms &lt;b&gt;histochemistry&lt;/b&gt; and &lt;b&gt;cytochemistry&lt;/b&gt;  are used to indicate methods for localizing substances in tissue sections.  Several procedures are used to obtain this type of information, most of them  based on specific chemical reactions or on high-affinity interactions between  macromolecules. These methods usually produce insoluble colored or  electron-dense compounds that enable the localization of specific substances by  means of light or electron microscopy.&lt;/div&gt;&lt;a href="" name="710066"&gt;&lt;/a&gt; &lt;div class="contentHead5" style="text-align: justify;"&gt;Ions&lt;/div&gt;&lt;a href="" name="710067"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Several ions (eg, calcium, iron, phosphate) have been  localized in tissues with these methods, using chemical reactions that produce a  dark insoluble product (Figure 1–16).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 1-16&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiuKSkkzFAKqnFxQP_tsnuHLh5pfGVFHbEKtd3WWfkuPldiyrN55BWrV25RGoX5azUPpsFb66fr_7NZsMtpWRquQnOQJ1tC5cbuoCvcUh5cIZQvdw6_jbCnMdzUCtqB3FtWvEHM7Cq__KI/s1600/Figure+1-16.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiuKSkkzFAKqnFxQP_tsnuHLh5pfGVFHbEKtd3WWfkuPldiyrN55BWrV25RGoX5azUPpsFb66fr_7NZsMtpWRquQnOQJ1tC5cbuoCvcUh5cIZQvdw6_jbCnMdzUCtqB3FtWvEHM7Cq__KI/s400/Figure+1-16.bmp" width="280" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Photomicrograph of a bone section treated with a histochemical  technique to demonstrate calcium ions. The dark precipitate indicates the  presence of calcium phosphate in calcified bone and cartilage. Noncalcified  cartilage tissue (stained in pink) is in the upper portion of the figure. Medium  magnification. (Courtesy of PA Abrahamsohn.)&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead5"&gt;&lt;span style="font-size: small;"&gt;&lt;b&gt;Nucleic Acids &lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;a href="" name="710069"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;DNA can be identified and quantified in cell nuclei using  the Feulgen reaction, which produces a red color in DNA. DNA and RNA can also be  analyzed by staining cells or tissue sections with a basic stain.&amp;nbsp;&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;a href="" name="710070"&gt;&lt;/a&gt; &lt;div class="contentHead5" style="text-align: justify;"&gt;&lt;i&gt;&lt;b&gt;Proteins&lt;/b&gt;&lt;/i&gt;&lt;/div&gt;&lt;a href="" name="710071"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Although there are general methods to detect proteins in  tissue sections, the histochemical methods usually do not permit identification  of specific proteins in cells and tissues. &lt;b&gt;Immunocytochemistry,&lt;/b&gt; presented  later in this chapter, can do so.&lt;/div&gt;&lt;a href="" name="710072"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Several histochemical methods, however, can be used to  reveal, more or less specifically, a large group of proteins, the  &lt;b&gt;enzymes.&lt;/b&gt; These methods usually make use of the capacity of the enzymes to  react with specific chemical bonds. Most histoenzymatic methods work in the  following way: (1) tissue sections are immersed in a solution that contains the  substrate of the enzyme intended for study; (2) the enzyme is allowed to act on  its substrate; (3) at this stage or at a later stage in the method, the section  is put in contact with a marker compound; (4) this compound reacts with a  molecule that results from the degradation or transformation of the substrate;  (5) the final reaction product, which must be insoluble and visible by light or  electron microscopy, precipitates over the sites that contain the enzyme. When  examining such a section in the microscope, it is possible to see the cells (or  organelles) covered with a colored or electron-dense material.&lt;/div&gt;&lt;a href="" name="710073"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Examples of enzymes that can be detected include the  following:&lt;/div&gt;&lt;a href="" name="710074"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Phosphatases&lt;/b&gt; are enzymes widely found in the body.  They split the bond between a phosphate group and an alcohol residue of  phosphorylated molecules. The colored insoluble reaction product of phosphatases  is usually lead phosphate or lead sulfide. Alkaline phosphatases, which have  their maximum activity at an alkaline pH, can be detected (Figure 1–17). Acid  phosphatases are frequently used to demonstrate &lt;b&gt;lysosomes,&lt;/b&gt; cytoplasmic  organelles that contain acid phosphatase (Figure 1–18).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 1-17&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgHEOawzfmHqhanzC0__BrF3ztU2t1bZ1dTgG8ihiImY5lqg86UClKTVMNlF85KAlhqBlf3-7JhjCZC7SOmi2wRewue-bcFpDqvv253YxeXbStjJXUueAzW7A2Sk6416rHvfUNn5rVCxjw/s1600/Figure+1-17.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgHEOawzfmHqhanzC0__BrF3ztU2t1bZ1dTgG8ihiImY5lqg86UClKTVMNlF85KAlhqBlf3-7JhjCZC7SOmi2wRewue-bcFpDqvv253YxeXbStjJXUueAzW7A2Sk6416rHvfUNn5rVCxjw/s400/Figure+1-17.bmp" width="330" /&gt;&lt;/a&gt;Photomicrograph of a rat kidney section treated by the Gomori  method to demonstrate the enzyme alkaline phosphatase. The sites where this  enzyme is present are covered by a black precipitate (arrows). Medium  magnification.&lt;/div&gt;&lt;div class="font11"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="font11"&gt;&lt;b&gt;Figure 1-18&lt;/b&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEj7wHsCOEUFgPe4OwNbcJfbHJgcyI4c2q0UMXm91RAVQZmRBbXTbf87pgH5pw-2cqqDeXCvU2mD2DiJy4PwpZZ_ZcLT9MAWbYQFRw0dZIr6K1tzHPWsvuacRXJ0UJIExoEg7G7qrOewiqI/s1600/Figure+1-18.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEj7wHsCOEUFgPe4OwNbcJfbHJgcyI4c2q0UMXm91RAVQZmRBbXTbf87pgH5pw-2cqqDeXCvU2mD2DiJy4PwpZZ_ZcLT9MAWbYQFRw0dZIr6K1tzHPWsvuacRXJ0UJIExoEg7G7qrOewiqI/s400/Figure+1-18.bmp" width="400" /&gt;&lt;/a&gt;Detection of acid phosphatase. Electron micrograph of a rat  kidney cell showing three lysosomes (ly) close to the nucleus (N). The dark  material on the lysosomes is lead phosphate that precipitated on places where  acid phosphatase was present. (Courtesy of E Katchburian.)&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Dehydrogenases&lt;/b&gt; remove hydrogen from one substrate  and transfer it to another. There are many dehydrogenases in the body, and they  play an important role in several metabolic processes. Dehydrogenases are  detected histochemically by incubating nonfixed tissue sections in a substrate  solution containing a molecule that receives hydrogen and precipitates as an  insoluble colored compound. By this method, succinate dehydrogenase—a key enzyme  in the citric acid (Krebs) cycle—can be localized in mitochondria.&lt;/div&gt;&lt;a href="" name="710076"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Peroxidase&lt;/b&gt;, which is present in several types of  cells, is an enzyme that promotes the oxidation of certain substrates with the  transfer of hydrogen ions to hydrogen peroxide, forming molecules of  water.&lt;/div&gt;&lt;a href="" name="710077"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;In this method, sections of adequately fixed tissue are  incubated in a solution containing hydrogen peroxide and  3,3&lt;i&gt;'&lt;/i&gt;-diaminoazobenzidine. The latter compound is oxidized in the presence  of peroxidase, resulting in an insoluble, brown, electron-dense precipitate that  permits the localization of peroxidase activity by light and electron  microscopy. Peroxidase activity in blood cells, which is important in the  diagnosis of leukemias, can be detected by this method.&lt;/div&gt;&lt;a href="" name="710078"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Because peroxidase is extremely active and produces an  appreciable amount of insoluble precipitate in a short time, it has also been  used for an important practical application: tagging other compounds. Molecules  of peroxidase can be purified, isolated, and coupled with another molecule.  Later in this chapter, applications of tagging molecules with peroxidase are  presented.&lt;/div&gt;&lt;a href="" name="710079"&gt;&lt;/a&gt; &lt;div class="contentHead5" style="text-align: justify;"&gt;Polysaccharides &amp;amp; Oligosaccharides&lt;/div&gt;&lt;a href="" name="710080"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Polysaccharides in the body occur either in a free state or  combined with proteins and lipids. In the combined state, they constitute an  extremely complex heterogeneous group. Polysaccharides can be demonstrated by  the periodic acid–Schiff (PAS) reaction, which is based on the transformation  into aldehyde of 1,2-glycol groups present in the sugar molecules. These  aldehydes are then revealed by Schiff's reagent, which produces a purple or  magenta color in areas of the section with an accumulation of  polysaccharides.&lt;/div&gt;&lt;a href="" name="710081"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;A ubiquitous free polysaccharide in the body is  &lt;b&gt;glycogen,&lt;/b&gt; which can be demonstrated by the PAS reaction in liver,  striated muscle, and other tissues where it accumulates.&lt;/div&gt;&lt;a href="" name="710082"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Glycoproteins&lt;/b&gt; are protein molecules associated with  small, branched chains of sugars (oligosaccharides). The protein chain  predominates in weight and volume over the oligosaccharide chain. Because both  glycogen and neutral glycoproteins are PAS positive, the specificity of the PAS  reaction can be improved by comparing the staining of regular sections with that  of sections pretreated with an enzyme that breaks glycogen (eg, amylase present  in the saliva). Structures that stain intensely with the PAS reaction but do not  stain after treatment with amylase contain glycogen. Figure 1–19 shows examples  of structures stained by the PAS reaction.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 1-19&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgZ95A-uxFvN96zlEt70Tep70RhuOz77f2_YAETm7xfDeoHJORSNi_NIpcLEaMuTrUzE9xa961pC0C2TdUvX2uFPfDQyjC05vxldjBIGctSGrT-aWpT0Psf13sjYf17uJbvXM9Y7wvFdsU/s1600/Figure+1-19.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="391" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgZ95A-uxFvN96zlEt70Tep70RhuOz77f2_YAETm7xfDeoHJORSNi_NIpcLEaMuTrUzE9xa961pC0C2TdUvX2uFPfDQyjC05vxldjBIGctSGrT-aWpT0Psf13sjYf17uJbvXM9Y7wvFdsU/s400/Figure+1-19.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Photomicrograph of an intestinal villus stained by PAS. Staining  is intense in the cell surface brush border (arrows) and in the secretory  product of goblet cells (G) because of their high content of polysaccharides.  The counterstain was hematoxylin. High magnification.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Glycosaminoglycans&lt;/b&gt; are strongly anionic, unbranched  long-chain polysaccharides containing aminated monosaccharides (amino sugars).  The complex molecules formed by the attachment of glycosaminoglycan chains to a  protein core constitute the &lt;b&gt;proteoglycans.&lt;/b&gt; Some of the significant  constituents of connective tissue matrices are proteoglycans (see Chapter 5:  Connective Tissue and Chapter 7: Cartilage). Unlike the glycoproteins, the  carbohydrate chains in proteoglycans constitute the major component of the  molecule. Glycosaminoglycans and acidic glycoproteins are strongly anionic  because of their high content of carboxyl and sulfate groups. For this reason,  they react strongly with the alcian blue dye.&lt;/div&gt;&lt;a href="" name="710084"&gt;&lt;/a&gt; &lt;div class="contentHead5" style="text-align: justify;"&gt;Lipids&lt;/div&gt;&lt;a href="" name="710085"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Lipids are best revealed with dyes that are soluble in  lipids. Frozen sections are immersed in alcohol solutions saturated with the  dye. Sudan IV and Sudan black are the most commonly used dyes. The dye dissolves  in the cellular lipid droplets, which become stained in red or black. Additional  methods used for the localization of cholesterol and its esters, phospholipids,  and glycolipids are useful in diagnosing metabolic diseases in which there are  intracellular accumulations of different kinds of lipids.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt; &lt;/div&gt;&lt;div class="contentBody"&gt;&lt;span style="color: red;"&gt;&lt;b&gt;&lt;i&gt;Medical Application&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;a href="" name="710087"&gt;&lt;/a&gt; &lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;Several histochemical procedures are frequently  used in laboratory diagnosis of diseases that result in the storage of iron,  glycogen, glycosaminoglycans, and other substances. Examples are Perls' reaction  for iron (eg, hemochromatosis, hemosiderosis), the PAS-amylase reaction for  glycogen (glycogenosis), alcian blue staining for glycosaminoglycans  (mucopolysaccharidosis), and lipid staining (sphingolipidosis).&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Alberts B et al: &lt;i&gt;Molecular Biology of the  Cell,&lt;/i&gt; 3rd ed. Garland, 1994. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Bancroft JD, Stevens A: &lt;i&gt;Theory and Practice  of Histological Techniques,&lt;/i&gt; 2nd ed. Churchill Livingstone, 1990. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cuello ACC: &lt;i&gt;Immunocytochemistry&lt;/i&gt;. Wiley,  1983. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Darnell J, Lodish H, Baltimore D: &lt;i&gt;Molecular  Cell Biology,&lt;/i&gt; 2nd ed. Scientific American Books, 1990. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Hayat MA: &lt;i&gt;Stains and Cytochemical  Methods&lt;/i&gt;. Plenum, 1993. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;James J: &lt;i&gt;Light Microscopic Techniques in  Biology and Medicine&lt;/i&gt;. Martinus Nijhoff, 1976. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Junqueira LCU et al: Differential staining of  collagen types I, II and III by Sirius Red and polarization microscopy. Arch  Histol Jpn 1978;41:267. [PMID: 82432] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Meek GA: &lt;i&gt;Practical Electron Microscopy for  Biologists&lt;/i&gt;. Wiley, 1976. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Pease AGE: &lt;i&gt;Histochemistry: Theoretical and  Applied,&lt;/i&gt; 4th ed. Churchill Livingstone, 1980. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rochow TG, Tucker PA: &lt;i&gt;Introduction to  Microscopy by Means of Light, Electrons, X Rays, or Acoustics&lt;/i&gt;. Plenum, 1994.  &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rogers AW: &lt;i&gt;Techniques of  Autoradiography,&lt;/i&gt; 3rd ed. Elsevier, 1979. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rubbi CP: &lt;i&gt;Light Microscopy. Essential  Data&lt;/i&gt;. Wiley, 1994. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Spencer M: &lt;i&gt;Fundamentals of Light  Microscopy&lt;/i&gt;. Cambridge University Press, 1982. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Stoward PJ, Polak JM (editors):  &lt;i&gt;Histochemistry: The Widening Horizons of Its Applications in Biological  Sciences&lt;/i&gt;. Wiley, 1981. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/histochemistry-cytochemistry.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiuKSkkzFAKqnFxQP_tsnuHLh5pfGVFHbEKtd3WWfkuPldiyrN55BWrV25RGoX5azUPpsFb66fr_7NZsMtpWRquQnOQJ1tC5cbuoCvcUh5cIZQvdw6_jbCnMdzUCtqB3FtWvEHM7Cq__KI/s72-c/Figure+1-16.bmp" width="72"/><thr:total>3</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-5555289544109225071</guid><pubDate>Wed, 15 Jun 2011 08:31:00 +0000</pubDate><atom:updated>2011-06-15T21:25:50.307+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">Medical Jokes</category><title>Asking for Help</title><description>&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhfT8c0ZtE1sT93pjrx91ykY-qxWAREyesMrtdNbJz-2WRyAen5KoMYCLvymuKrVgTsnXqREQndoctGAWoHYGSTGdG6vTEe8c0RAxclzeajyXPjrBeU6fSzkZBnTOgd3jIQcGDI41sPz6s/s1600/Crazy+Doctor.gif" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="212" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhfT8c0ZtE1sT93pjrx91ykY-qxWAREyesMrtdNbJz-2WRyAen5KoMYCLvymuKrVgTsnXqREQndoctGAWoHYGSTGdG6vTEe8c0RAxclzeajyXPjrBeU6fSzkZBnTOgd3jIQcGDI41sPz6s/s320/Crazy+Doctor.gif" width="320" /&gt;&lt;/a&gt;&lt;/div&gt;Somewhere in doctor's practice room, came a man ± 60 years old, a woman ± 25 years old and a child ± 2 years old. &lt;br /&gt;
&lt;br /&gt;
After seated, there was a question and answer between doctor with these patients.&lt;br /&gt;
&lt;br /&gt;
&lt;b&gt;The Doctor&lt;/b&gt; : Who is sick ?&lt;br /&gt;
&lt;b&gt;The Woman&lt;/b&gt; (who answered): That's Mr. Doctor, my husband can not move their weapons. (That's impotent).&lt;br /&gt;
&lt;b&gt;The Doctor&lt;/b&gt; (half-surprised, because he thinks he's did her parents): "How long has the pain sir?"&lt;br /&gt;
&lt;b&gt;The Man &lt;/b&gt;: It's been about 5 years ago doctor...&lt;br /&gt;
&lt;b&gt;The Doctor&lt;/b&gt; : But your child&amp;nbsp; was ± 2 years old, that's impossible...&lt;br /&gt;
&lt;br /&gt;
The Woman heard the question doctor did smile a little smile. The Man with a coy answer :&lt;br /&gt;
&lt;br /&gt;
&lt;b&gt;The Man&lt;/b&gt; : Yes, Doctor, that child is a child of my wife, but he's not my child. &lt;br /&gt;
&lt;b&gt;The Doctor&lt;/b&gt; : Does your wife have time to marry when you're widowed?&lt;br /&gt;
&lt;b&gt;The Man&lt;/b&gt; : No doctor, he was still a virgin.&lt;br /&gt;
&lt;b&gt;The Doctor&lt;/b&gt; : So...!!?&lt;br /&gt;
&lt;b&gt;The Man&lt;/b&gt; : That time... I asked for help to my neighbor because I want to have a child...&lt;br /&gt;
&lt;br /&gt;
Hearing the unexpected answer before the doctor said :&lt;br /&gt;
&lt;br /&gt;
&lt;b&gt;The Doctor&lt;/b&gt; : Why didn't you ask me to do it ?&lt;br /&gt;
&lt;br /&gt;
The woman heard the words of Doctor said, looking small smile full of meaning. Doctors soon realized, and correct it.&lt;b&gt;&lt;br /&gt;
&lt;br /&gt;
The Doctor&lt;/b&gt; : No...I mean...why didn't you seek treatment before !... XD</description><link>http://dehistology.blogspot.com/2011/06/asking-for-help.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEhfT8c0ZtE1sT93pjrx91ykY-qxWAREyesMrtdNbJz-2WRyAen5KoMYCLvymuKrVgTsnXqREQndoctGAWoHYGSTGdG6vTEe8c0RAxclzeajyXPjrBeU6fSzkZBnTOgd3jIQcGDI41sPz6s/s72-c/Crazy+Doctor.gif" width="72"/><thr:total>6</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-1102278025554210239</guid><pubDate>Tue, 14 Jun 2011 13:46:00 +0000</pubDate><atom:updated>2011-06-14T20:46:46.533+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cell Nucleus</category><title>Apoptosis</title><description>&lt;div class="contentBody" style="text-align: justify;"&gt;Cell proliferation for renewal and growth is a process of  self-evident physiological significance. Less evident, but no less important for  body functions and health, is the process of programmed cell death called  &lt;b&gt;apoptosis&lt;/b&gt;. A few examples of apoptosis will illustrate its  significance.&lt;/div&gt;&lt;a href="" name="712726"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;Most T lymphocytes originating in the thymus have the  ability to attack and destroy body components and would cause serious damage if  they entered the blood circulation. Inside the thymus, these T lymphocytes  receive signals that activate the apoptotic program encoded in their  chromosomes. They are destroyed by apoptosis before leaving the thymus (see  Chapter 14: Lymphoid Organs).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt; &lt;/div&gt;&lt;div class="contentBody"&gt;&lt;span style="color: red;"&gt;&lt;b&gt;&lt;i&gt;Medical Application&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;a href="" name="712728"&gt;&lt;/a&gt; &lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;Most cells of the body can activate their  apoptotic program when major changes occur in their DNA for example, just  before a tumor appears, when a number of mutations have already accumulated in  the DNA. In this way, apoptosis prevents the proliferation of malignant cells  that develop as a result of accumulated mutations in the DNA. To form a clone  and develop into a tumor, the malignant cell needs to deactivate the genes that  control the apoptotic process.&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Apoptosis was first discovered in developing embryos, where  programmed cell death is an essential process for shaping the embryo  (morphogenesis). Later investigators observed that apoptosis is also a common  event in the tissues of normal adults.&lt;/div&gt;&lt;a href="" name="712730"&gt;&lt;/a&gt; &lt;div class="contentBody" style="text-align: justify;"&gt;In apoptosis, the cell and its nucleus become compact,  decreasing in size. At this stage the apoptotic cell shows a dark-stained  nucleus (pyknotic nucleus), easily identified with the light microscope (Figure  3-24). Next, the chromatin is cut into pieces by DNA endonucleases. During  apoptosis the cell shows cytoplasmic large vesicles (blebs) that detach from the  cell surface (Figure 3-25). These detached fragments are contained within the  plasma membrane, which is changed in such a way that all cell remnants are  readily engulfed, or phagocytosed, mainly by macrophages. However, in  macrophages the apoptotic fragments do not elicit the synthesis of the molecules  that triggers the inflammatory process (see below).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 3-24&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEj6uU2dUbDf_VthhrV7RLF7mktXuMayknedcWhFKhV5w-OjLoY-bnM9L2j6gYjYUbyd4eAxHwyk8c_8mEJc9q5ufOTZ06KdoSr5YKeJa6cti9zUZmyCDziQRdTevxRTxcd2gPLTlOl1ssI/s1600/Figure+3-24.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="283" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEj6uU2dUbDf_VthhrV7RLF7mktXuMayknedcWhFKhV5w-OjLoY-bnM9L2j6gYjYUbyd4eAxHwyk8c_8mEJc9q5ufOTZ06KdoSr5YKeJa6cti9zUZmyCDziQRdTevxRTxcd2gPLTlOl1ssI/s400/Figure+3-24.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Section of a mammary gland from an animal whose lactation was  interrupted for 5 days. Note atrophy of the epithelial cells and dilation of the  alveolar lumen, which contains several detached cells in the process of  apoptosis, as seen from the nuclear alterations. PT stain. Medium  magnification.&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;b&gt;Figure 3-25&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEi0E78dmSQ1KhTGyj4xijFSpZZkN7IQEa7ORTtoyE145QcVRa3VgSILIYPrkXR6aIYGoJLVuyZh3sXG5Luwhrt2sESYe2tXV_YKucQID8XYEHU_y3_sYvKAL3c4OLjTijvx9PZMls7s2Yk/s1600/Figure+3-25.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="348" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEi0E78dmSQ1KhTGyj4xijFSpZZkN7IQEa7ORTtoyE145QcVRa3VgSILIYPrkXR6aIYGoJLVuyZh3sXG5Luwhrt2sESYe2tXV_YKucQID8XYEHU_y3_sYvKAL3c4OLjTijvx9PZMls7s2Yk/s400/Figure+3-25.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Electron micrograph of a cell in apoptosis showing that its  cytoplasm is undergoing a process of fragmentation in blebs that preserve their  plasma membranes. These blebs are phagocytosed by macrophages without eliciting  an inflammatory reaction. No cytoplasmic substances are released into the  extracellular space.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt; &lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0" style="margin-left: 0px; margin-right: 0px; text-align: left;"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff" valign="top"&gt; &lt;div class="contentBody"&gt;&lt;span style="color: red;"&gt;&lt;b&gt;&lt;i&gt;Medical Application&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;a href="" name="712732"&gt;&lt;/a&gt; &lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;The accidental death of cells, a pathological  process, is called &lt;b&gt;necrosis.&lt;/b&gt; Necrosis can be caused by microorganisms,  viruses, chemicals, and other harmful agents. Necrotic cells swell; their  organelles increase in volume; and finally they burst, releasing their contents  into the extracellular space. Macrophages engulf the debris of necrotic cells by  phagocytosis and then secrete molecules that activate other immunodefensive  cells to promote inflammation.&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;a href="" name="712733"&gt;&lt;/a&gt; &lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff" valign="top"&gt; &lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cooper GM: &lt;i&gt;The Cell: A Molecular  Approach&lt;/i&gt;. ASM Press/Sinauer Associates, Inc., 1997. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Doye V, Hurt E: From nucleoporins to nuclear  pore complexes. Curr Opin Cell Biol 1997;9:401. [PMID: 9159086] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Duke RC et al: Cell suicide in health and  disease. Sci Am 1996;275(6):48. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Fawcett D: &lt;i&gt;The Cell,&lt;/i&gt; 2nd ed. Saunders,  1981. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Goodman SR: &lt;i&gt;Medical Cell Biology&lt;/i&gt;.  Lippincott, 1994. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Jordan EG, Cullis CA (editors): &lt;i&gt;The  Nucleolus&lt;/i&gt;. Cambridge University Press, 1982. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Kornberg RD, Klug A: The nucleosome. Sci Am  1981;244:52. [PMID: 7209486] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;KrstÃ­c RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Lloyd D et al: &lt;i&gt;The Cell Division Cycle&lt;/i&gt;.  Academic Press, 1982. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;MÃ©lÃ¨se T, Xue Z: The nucleolus: an organelle  formed by the act of building a ribosome. Curr Opin Cell Biol 1995;7:319. [PMID:  15900607] &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Trent RJ: &lt;i&gt;Molecular Medicine. An  Introductory Text for Students&lt;/i&gt;. Churchill Livingstone, 1993. &lt;br /&gt;
&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Watson JD et al: &lt;i&gt;Recombinant DNA,&lt;/i&gt; 2nd  ed. Scientific American Books, 1992.&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="contentHead3"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead3"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt; &lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/apoptosis.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEj6uU2dUbDf_VthhrV7RLF7mktXuMayknedcWhFKhV5w-OjLoY-bnM9L2j6gYjYUbyd4eAxHwyk8c_8mEJc9q5ufOTZ06KdoSr5YKeJa6cti9zUZmyCDziQRdTevxRTxcd2gPLTlOl1ssI/s72-c/Figure+3-24.bmp" width="72"/><thr:total>0</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-2948933428515269744</guid><pubDate>Tue, 14 Jun 2011 13:24:00 +0000</pubDate><atom:updated>2011-06-17T15:54:08.964+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">Java Application for Medical</category><title>First Aid 3.0 (Java Software)</title><description>&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiYO_ADXh4Gx0VQDv8XSkag_Z-Hyv1hYKIoK1FvX2s_CMsAIUuhI9QsASdxjjwNi0AraxC15uE8uWrQpRO89gZZdZ6kzEJQEkBP6WUmb7-6S7S9V7uBjTonb6M-s13oiVhXhIAKK3JewFs/s1600/First+Aid+v3.0.jpg" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiYO_ADXh4Gx0VQDv8XSkag_Z-Hyv1hYKIoK1FvX2s_CMsAIUuhI9QsASdxjjwNi0AraxC15uE8uWrQpRO89gZZdZ6kzEJQEkBP6WUmb7-6S7S9V7uBjTonb6M-s13oiVhXhIAKK3JewFs/s1600/First+Aid+v3.0.jpg" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Handling an accident or an emergency situation is something we all  hope we never have to face. Even so, it's something we should all be  prepared for. &lt;b&gt;First Aid&lt;/b&gt; includes step-by-step instructions for 50  different first aid procedures. The conditions/injuries are listed in a  simple alphabetically-ordered on the main screen, and these can be  scrolled down very quickly.&lt;/div&gt;&lt;div&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Each procedure in &lt;b&gt;First Aid&lt;/b&gt; is explained in a clear and concise  manner, meaning you don't have to read through pages and pages of text  while the victim is laying in agony. Colorful illustrations are used to  provide an at-a-glance guide to some of the rescue maneuvers, which  include cardiopulmonary resuscitation and cuts and scrapes first aid.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Besides offering these 50 overviews, &lt;b&gt;First Aid&lt;/b&gt; also provides  information on emergency service phone numbers for any country, details  of general conduct, and a one-click call button to the emergency  services.&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;It's worth noting that &lt;b&gt;First Aid&lt;/b&gt; merely offers information on  emergency procedures and, as its disclaimer says, it doesn't represent a  substitute to a first aid course.&lt;br /&gt;
&lt;br /&gt;
reviewed by &lt;a class="url track-me track-tracking_place-ProgramPage track-action-ClickRedactor track-parameter-myVal-James_Thornton" href="http://en.softonic.com/software-reviewer/james-thornton" rel="nofollow" style="color: blue;" title="Read this author's latest reviews"&gt;&lt;i class="fn reviewer"&gt;James Thornton&lt;/i&gt;&lt;/a&gt; &lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;b&gt;Download &lt;/b&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: large;"&gt;&lt;a href="http://www.mediafire.com/?4rnvyjwfxr95ubl"&gt;&lt;b&gt;First Aid 3.0.jar &lt;/b&gt;&lt;/a&gt;&lt;/span&gt;&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/first-aid-30.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiYO_ADXh4Gx0VQDv8XSkag_Z-Hyv1hYKIoK1FvX2s_CMsAIUuhI9QsASdxjjwNi0AraxC15uE8uWrQpRO89gZZdZ6kzEJQEkBP6WUmb7-6S7S9V7uBjTonb6M-s13oiVhXhIAKK3JewFs/s72-c/First+Aid+v3.0.jpg" width="72"/><thr:total>3</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-8650126654482315792</guid><pubDate>Mon, 13 Jun 2011 13:06:00 +0000</pubDate><atom:updated>2011-06-14T20:47:17.396+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cell Nucleus</category><title>The Cell Cycle</title><description>&lt;div class="contentBody" style="text-align: justify;"&gt;Mitosis is the visible manifestation of cell division, but  other processes, not so easily observed with the light microscope, play a  fundamental role in cell multiplication. Principal among these is the phase in  which DNA replicates. This process can be analyzed by introducing labeled  radioactive DNA precursors (eg, [&lt;sup&gt;3&lt;/sup&gt;H]thymidine) into the cell and  tracing them by means of biochemical and autoradiographic methods. DNA  replication has been shown to occur during &lt;b&gt;interphase,&lt;/b&gt; when no visible  phenomena of cell division can be seen with the microscope. This alternation  between mitosis and interphase, known as the &lt;b&gt;cell cycle,&lt;/b&gt; occurs in all  tissues with cell turnover. A careful study of the cell cycle reveals that it  can be divided into two stages: mitosis, consisting of the four phases already  described (prophase, metaphase, anaphase, and telophase), and interphase  (Figures 3-20 and 3-21).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="tableTitle"&gt;&lt;b&gt;Figure 3-20&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg58JDVpO7ZjKSrhNxHC0rXKEgv6bbnUPcROozGrjjl5Wj2uA6OozJQweEQRUaoDOcxHPOa_wjRa8k7ItfD6wZreh_Sr0s7kZitRxpy9y2IsvmqjnCXkul7f4TAus4-It9-alcoH9OXioc/s1600/Figure+3-20.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="271" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg58JDVpO7ZjKSrhNxHC0rXKEgv6bbnUPcROozGrjjl5Wj2uA6OozJQweEQRUaoDOcxHPOa_wjRa8k7ItfD6wZreh_Sr0s7kZitRxpy9y2IsvmqjnCXkul7f4TAus4-It9-alcoH9OXioc/s400/Figure+3-20.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Phases of the cell cycle in bone tissue. The G&lt;sub&gt;1&lt;/sub&gt; phase  (presynthesis) varies in duration, which depends on many factors, including the  rate of cell division in the tissue. In bone tissue, G&lt;sub&gt;1&lt;/sub&gt; lasts 25 h.  The S phase (DNA synthesis) lasts about 8 h. The G&lt;sub&gt;2&lt;/sub&gt;-plus-mitosis  phase lasts 2.5-3 h. (The times indicated are courtesy of RW Young.)&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 3-21&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEh2lvt_jtwFH5zhYnSMOfKgVpXMZGyhN45ZeXv9Otaizx3pIixNyp-BcjvhIVIbksTUcDd8IYz-YQJViZD3du6KVFqxF3ljn8NUep1Z5lHtWFJ4ojsmHjtk5g2DvBOKxuBs-UEGqCGHMQ8/s1600/Figure+3-21.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEh2lvt_jtwFH5zhYnSMOfKgVpXMZGyhN45ZeXv9Otaizx3pIixNyp-BcjvhIVIbksTUcDd8IYz-YQJViZD3du6KVFqxF3ljn8NUep1Z5lHtWFJ4ojsmHjtk5g2DvBOKxuBs-UEGqCGHMQ8/s320/Figure+3-21.bmp" width="251" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;The four phases of the cell cycle. In G&lt;sub&gt;1&lt;/sub&gt; the cell  either continues the cycle or enters a quiescent phase called G&lt;sub&gt;0&lt;/sub&gt;.  From this phase, most cells can return to the cycle, but some stay in  G&lt;sub&gt;0&lt;/sub&gt; for a long time or even for their entire lifetime. The checking or  restriction point (R) in G&lt;sub&gt;1&lt;/sub&gt; stops the cycle under conditions  unfavorable to the cell. When the cell passes this restriction point, it  continues the cycle through the synthetic phase (S) and the G&lt;sub&gt;2&lt;/sub&gt; phase,  originating two daughter cells in mitosis (M) except when interrupted by another  restriction point (not shown) in G&lt;sub&gt;2&lt;/sub&gt;.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Interphase is itself divided into three phases:  G&lt;sub&gt;1&lt;/sub&gt; (presynthesis), S (DNA synthesis), and G&lt;sub&gt;2&lt;/sub&gt; (post-DNA  duplication). The sequence of these phases and the approximate times involved  are illustrated in Figures 3-20 and 3-21. The S phase is characterized by  the synthesis of DNA and the beginning of the duplications of the centrosomes  with their centrioles. During the G&lt;sub&gt;1&lt;/sub&gt; phase, there is an intense  synthesis of RNA and proteins, including proteins that control the cell cycle,  and the cell volume, previously reduced to one-half by mitosis, is restored to  its normal size. In cells that are not continuously dividing, the activities of  the cell cycle may be temporarily or permanently suspended. Cells in such a  state (eg, muscle, nerve) are referred to as being in the G&lt;sub&gt;0&lt;/sub&gt;  phase.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8650126654482315792" name="712715"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;Regulation of the mammalian cell cycle is complex. It is  known that cultured cells deprived of serum stop proliferating and arrest in  G&lt;sub&gt;0&lt;/sub&gt;. The essential components provided by serum are highly specific  proteins called &lt;b&gt;growth factors,&lt;/b&gt; which are required only in very low  concentrations.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;/div&gt;&lt;div class="contentBody"&gt;&lt;i&gt;&lt;span style="color: red;"&gt;&lt;b&gt;Medical Application &lt;/b&gt;&lt;/span&gt;&lt;/i&gt;&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8650126654482315792" name="712717"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;Some growth factors are being used in medicine.  One example is erythropoietin, which stimulates proliferation, differentiation,  and survival of red blood cell precursors in the bone marrow.&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8650126654482315792" name="712718"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;The cell cycle is also regulated by a variety of signals  that inhibit progression through the cycle. DNA damage arrests the cell cycle  not only in G&lt;sub&gt;2&lt;/sub&gt; but also at a checkpoint in G&lt;sub&gt;1&lt;/sub&gt; (Figure  3-21). G&lt;sub&gt;1&lt;/sub&gt; arrest may permit the damage to be repaired before the  cell enters S phase, where the damaged DNA would be replicated. In mammalian  cells, arrest at the G1 checkpoint is mediated by the action of a protein known  as p53. The gene encoding p53 is often mutated in human cancers, thus reducing  the cell's ability to repair damaged DNA. Inheritance of damaged DNA by daughter  cells results in an increased frequency of mutations and general instability of  the genome, which may contribute to the development of cancer.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8650126654482315792" name="712719"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;Processes that occur during the G&lt;sub&gt;2&lt;/sub&gt; phase include  the accumulation of energy to be used during mitosis, the synthesis of tubulin  to be assembled in mitotic microtubules, and the synthesis of chromosomal  nonhistone proteins. In G&lt;sub&gt;2&lt;/sub&gt; there is also a checkpoint at which the  cell remains until all DNA synthesized with defects is corrected. In  G&lt;sub&gt;2&lt;/sub&gt; there is an accumulation of the protein complex maturation  promoting factor (&lt;b&gt;MPF&lt;/b&gt;) that induces the beginning of mitosis, the  condensation of the chromosomes, the rupture of the nuclear envelope, and other  events related to mitosis.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;i&gt;&lt;span style="color: red;"&gt;&lt;b&gt;Medical Application&lt;/b&gt;&lt;/span&gt;&lt;/i&gt; &lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;Rapidly growing tissues (eg, intestinal  epithelium) frequently contain cells in mitosis, whereas slowly growing tissues  do not. The increased number of mitotic figures and abnormal mitoses in tumors  is an important characteristic that distinguishes malignant from benign tumors.  The organism has elaborate regulatory systems that control cell reproduction by  either stimulating or inhibiting mitosis. Normal cell proliferation and  differentiation are controlled by a group of genes called &lt;b&gt;protooncogenes;&lt;/b&gt;  altering the structure or expression of these genes promotes the production of  tumors. Altered protooncogenes are present in tumor-producing viruses and are  probably derived from cells. Altered oncogene activity can be induced by a  change in the DNA sequence (mutation), an increase in the number of genes (gene  amplification), or gene rearrangement, in which genes are relocated near an  active promoter site. Altered oncogenes have been associated with several tumors  and hematological neoplasia. Proteins that stimulate mitotic activity in various  cell types include nerve growth factor, epithelial growth factor, fibroblast  growth factor, and precursors of erythrocyte growth factor (erythropoietin);  there is an extensive and rapidly growing list of these proteins (see Chapter  13: Hematopoiesis).&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8650126654482315792" name="712722"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;Cell proliferation is usually regulated by  precise mechanisms that can, when necessary, stimulate or retard mitosis  according to the needs of the organism. Several factors (eg, chemical  substances, certain types of radiation, viral infections) can induce DNA damage,  mutation, and abnormal cell proliferation that bypass normal regulatory  mechanisms for controlled growth and result in the formation of tumors.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=8650126654482315792" name="712723"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;The term &lt;b&gt;tumor,&lt;/b&gt; initially used to denote  any localized swelling in the body caused by inflammation or abnormal cell  proliferation, is now usually used as a synonym for &lt;b&gt;neoplasm&lt;/b&gt; (Gr.  &lt;i&gt;neos&lt;/i&gt;, new, + &lt;i&gt;plasma&lt;/i&gt;, thing formed). Neoplasm can be defined as an  abnormal mass of tissue formed by uncoordinated cell proliferation. Neoplasms  are either benign or malignant according to their characteristics of slow growth  and no invasiveness (benign) or rapid growth and great capacity to invade other  tissues and organs (malignant). &lt;b&gt;Cancer&lt;/b&gt; is the common term for all  malignant tumors (Figures 3-22 and 3-23).&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBodyWithMargin" style="text-align: justify;"&gt;&lt;b&gt;Figure 3-22&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiDA5c0O7LuSe8qm2oQr2tYUh2sSKzKDp3ycsoWRXkBs7Ces21s9SDPmkymmQJtEQm_m5JTA4XpVrMjCE_kPQJyouZfwFdVgeUjvu4XlWPrIXGNgOjsuyxsiVxVUXNquloPcKVqtfKpCs0/s1600/Figure+3-22.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="288" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiDA5c0O7LuSe8qm2oQr2tYUh2sSKzKDp3ycsoWRXkBs7Ces21s9SDPmkymmQJtEQm_m5JTA4XpVrMjCE_kPQJyouZfwFdVgeUjvu4XlWPrIXGNgOjsuyxsiVxVUXNquloPcKVqtfKpCs0/s400/Figure+3-22.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Section of a malignant epithelial skin tumor (squamous cell  carcinoma). An increase in the number of cells in mitosis and diversity of  nuclear morphology are signs of malignancy. PT stain. Medium magnification.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;b&gt;Figure 3-23&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg4qdLbau882zk5Y9Fus-2ow8ZTZwRJgYIu-dsZQ5NFaJuM0zlP6UYF4LHbEjsSTPk_NjMHyXIDdztgAJ3lnyY3dZI9sBt26cqN6EV0n_zsyvAoxq1I4yDAeqM2UlRKoqwn_28swzbqzZM/s1600/Figure+3-23.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="288" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg4qdLbau882zk5Y9Fus-2ow8ZTZwRJgYIu-dsZQ5NFaJuM0zlP6UYF4LHbEjsSTPk_NjMHyXIDdztgAJ3lnyY3dZI9sBt26cqN6EV0n_zsyvAoxq1I4yDAeqM2UlRKoqwn_28swzbqzZM/s400/Figure+3-23.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Section of a fast-growing malignant epithelial skin tumor  showing an increased number of cells in mitosis and great diversity of nuclear  morphology. H&amp;amp;E stain. Medium magnification.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;MÃ©lÃ¨se T, Xue Z: The nucleolus: an organelle  formed by the act of building a ribosome. Curr Opin Cell Biol 1995;7:319. [PMID:  15900607] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Trent RJ: &lt;i&gt;Molecular Medicine. An  Introductory Text for Students&lt;/i&gt;. Churchill Livingstone, 1993. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Watson JD et al: &lt;i&gt;Recombinant DNA,&lt;/i&gt; 2nd  ed. Scientific American Books, 1992. &lt;/td&gt;&lt;/tr&gt;
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&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/cell-cycle.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg58JDVpO7ZjKSrhNxHC0rXKEgv6bbnUPcROozGrjjl5Wj2uA6OozJQweEQRUaoDOcxHPOa_wjRa8k7ItfD6wZreh_Sr0s7kZitRxpy9y2IsvmqjnCXkul7f4TAus4-It9-alcoH9OXioc/s72-c/Figure+3-20.bmp" width="72"/><thr:total>49</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-3543638311031340170</guid><pubDate>Mon, 13 Jun 2011 11:51:00 +0000</pubDate><atom:updated>2011-06-13T18:52:57.052+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">News</category><title>Von Willebrand Disease</title><description>&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg6g8HYEhaUZcCoI3J4L6_C4J1t1f1TDGjKrPExfhsh7vAsgGvvaCN8-75kDv4zR1Gk3EbiSjyAv_x7BVKqfxfdMl-OA4zIEyI_FshIlVO2q6L1SN7JM8rZeMcZoDqvwpXY2TC5nyezckA/s1600/VWB.jpg" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="240" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg6g8HYEhaUZcCoI3J4L6_C4J1t1f1TDGjKrPExfhsh7vAsgGvvaCN8-75kDv4zR1Gk3EbiSjyAv_x7BVKqfxfdMl-OA4zIEyI_FshIlVO2q6L1SN7JM8rZeMcZoDqvwpXY2TC5nyezckA/s320/VWB.jpg" width="320" /&gt;&lt;/a&gt;&lt;b&gt;&lt;i&gt;&lt;span style="font-size: 11pt;"&gt; &lt;/span&gt;&lt;/i&gt;&lt;/b&gt;&lt;span class="" id="result_box" lang="en" style="font-size: small;"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;In Indonesia,&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;a lot&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;of people&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;are&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;surprised&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;by the&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;existence of&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;a disease&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;in which&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;a&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;patient&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;suffered&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;a bloody&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;sweating. &lt;/span&gt;&lt;/span&gt;&lt;span class="" id="result_box" lang="en" style="font-size: small;"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Until&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;now,&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;I&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;still don't&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;know&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;the exact&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;ins&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;and outs&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;of&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;this&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;disease. &lt;/span&gt;&lt;/span&gt;&lt;span class="" id="result_box" lang="en" style="font-size: small;"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;According to story, I&lt;/span&gt;'&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;ll&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;show the&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;following&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;information which i get&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;about&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;this&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;disease...&lt;/span&gt;&lt;/span&gt;&lt;br /&gt;
&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span class="" id="result_box" lang="en" style="font-size: small;"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;&amp;nbsp;&lt;/span&gt;&lt;/span&gt;&lt;span style="font-size: small;"&gt;&lt;b&gt;&lt;i&gt;&amp;nbsp;&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;br /&gt;
&lt;span style="font-size: small;"&gt;&lt;b&gt;&lt;i&gt;What is von Willebrand Disease?&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;Von Willebrand Disease is the most common of all inherited bleeding disorders.&amp;nbsp; A person can have a very mild form of the disease without many bleeding problems or the form of the disease can be more severe and cause more bleeding problems.&amp;nbsp; &lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&amp;nbsp;&amp;nbsp;&lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;b&gt;&lt;i&gt;What is von Willebrand Factor?&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;There are a lot of proteins in a person’s blood that help form a clot when needed to stop bleeding.&amp;nbsp; One of these proteins is called von Willebrand Factor.&amp;nbsp; Von Willebrand Factor is a glue-like, sticky protein that carries Factor 8 which is another protein in the blood that helps you clot. &amp;nbsp;It also helps platelets stick to the blood vessel wall when needed to “plug” up a hole that is causing bleeding.&amp;nbsp; When there is not enough von Willebrand Factor in the blood or when the von Willebrand Factor does not work well, a person has von Willebrand Disease. &lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;br /&gt;
&lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;b&gt;&lt;i&gt;What are the symptoms of von Willebrand Disease?&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&amp;nbsp;People with this disease often have more problems with gum bleeding after dental work or frequent nosebleeds. They can also have more bruising than the normal person or have heavy bleeding after surgery, dental work or a cut or other accident&lt;/span&gt;&lt;span style="color: black; font-family: &amp;quot;Arial&amp;quot;,&amp;quot;sans-serif&amp;quot;; font-size: small;"&gt;.&lt;/span&gt;&lt;span style="font-size: small;"&gt; &amp;nbsp;&amp;nbsp;If a woman has the disease, she can often have a heavy bleeding with her menstrual periods.&amp;nbsp; &lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;br /&gt;
&lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;b&gt;&lt;i&gt;How is von Willebrand Disease diagnosed?&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;If the diagnosis of von Willebrand Disease is suspected, a doctor will question that person to see if anyone else in the family has had bleeding problems because it is an inherited disorder.&amp;nbsp; Also some blood samples will be drawn to see how much von Willebrand Factor and Factor 8 are actually in the blood.&amp;nbsp; Sometimes these blood samples need to be repeated to get accurate results.&lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;br /&gt;
&lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;b&gt;&lt;i&gt;How is von Willebrand Disease treated?&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;Many medicines can be used to stop the bleeding related to von Willebrand Disease.&amp;nbsp; The type of treatment depends on how severe a person’s von Willebrand Disease is and where the bleeding is in the body.&amp;nbsp; These medications can be used before a surgery or dental procedures to help prevent bleeding or they can be used to help stop any bleeding that has occurred.&amp;nbsp; One of these medications actually has von Willebrand Factor in it and can be given in the vein to help stop bleeding. This is often needed for more severe forms of the disease. &amp;nbsp;Another medication called Stimate (DDAVP) is in the form of a nose spray and can help increase the amount of von Willebrand Factor in the blood for a long enough time to stop the bleeding. This often works for milder forms of the disease.&amp;nbsp; Birth control pills are often the best way to help control increased bleeding with menstrual periods.&amp;nbsp; A liquid medication called Amicar can be taken by mouth and is often helpful in stopping bleeding, especially in the mouth after dental work. &amp;nbsp;Your doctor will help decide which treatment is best for you.&lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;br /&gt;
&lt;/span&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="font-size: small;"&gt;&lt;b&gt;&lt;i&gt;Can von Willebrand Disease be cured?&lt;/i&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;/div&gt;&lt;div class="MsoNormal" style="text-align: justify;"&gt;&lt;span style="color: black; font-size: small;"&gt;VWD can't be cured, but it can be treated. With the right treatment, people who have VWD can lead normal, active lives &lt;/span&gt;&lt;b style="mso-bidi-font-weight: normal;"&gt;&lt;i style="mso-bidi-font-style: normal;"&gt;&lt;span style="font-size: 11pt;"&gt;&lt;/span&gt;&lt;/i&gt;&lt;/b&gt;&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/von-willebrand-disease.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg6g8HYEhaUZcCoI3J4L6_C4J1t1f1TDGjKrPExfhsh7vAsgGvvaCN8-75kDv4zR1Gk3EbiSjyAv_x7BVKqfxfdMl-OA4zIEyI_FshIlVO2q6L1SN7JM8rZeMcZoDqvwpXY2TC5nyezckA/s72-c/VWB.jpg" width="72"/><thr:total>6</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-9161781405051530840</guid><pubDate>Mon, 13 Jun 2011 11:35:00 +0000</pubDate><atom:updated>2011-06-17T16:44:20.859+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">Java Application for Medical</category><title>Oxford Concise Medical Dictionary (Java Software)</title><description>&lt;div style="text-align: justify;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiKutBVryUbPKE88fV2LROJHfEPxYw27IdruM3fbMB3AR_rLjmW3wFHm_qswT97OdTCywH0Ky-akPKp-_5Aecdj3LVVLD56gwRJdSzpuD5y3tEo0BpJG_mKZp3D4Pj0JZM8XzwsfHrtGiM/s1600/Medical+Dictionary+for+Mobile.jpg" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiKutBVryUbPKE88fV2LROJHfEPxYw27IdruM3fbMB3AR_rLjmW3wFHm_qswT97OdTCywH0Ky-akPKp-_5Aecdj3LVVLD56gwRJdSzpuD5y3tEo0BpJG_mKZp3D4Pj0JZM8XzwsfHrtGiM/s1600/Medical+Dictionary+for+Mobile.jpg" /&gt;&lt;/a&gt;&lt;span class="" id="result_box" lang="en"&gt;&lt;b&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Oxford&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Concise&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Medical&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Dictionary&lt;/span&gt;&lt;/b&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;is written&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;by&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;medical&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;specialists&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;and&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;panelists&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;,&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;this&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;dictionary&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;is intended&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;for&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;workers&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;in&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;the&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;sector&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;paramedic&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;,&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;as&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;such&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;were the&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;pharmacists&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;,&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;physiotherapy&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;,&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;speech therapy&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;,&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;and so&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;on&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;.&lt;/span&gt;&lt;br /&gt;
&lt;br /&gt;
&lt;b&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Oxford&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Concise&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Medical&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Dictionary&lt;/span&gt;&lt;/b&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;will also be&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;very&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;useful&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;for&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;medical&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;students&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;and&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;practicing physicians&lt;/span&gt; &lt;span class="hps atn" title="Klik untuk terjemahan alternatif"&gt;(&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;including&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;resident&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;therein&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;)&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;.&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Each&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;entry&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;contains a&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;basic&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;definition&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;,&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;followed&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;by&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;a&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;more&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;detailed&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;explanation&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;or&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;description&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;.&lt;/span&gt;&lt;br /&gt;
&lt;br /&gt;
&lt;b&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Oxford&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Concise&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Medical&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Dictionary&lt;/span&gt;&lt;/b&gt;&lt;span class="hps atn" title="Klik untuk terjemahan alternatif"&gt;&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;equipped with&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;a&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;feature&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;article&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;written&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;for&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;a clear&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;and&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;concise&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;English&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;without the use of&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;technical&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;jargon&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;yng&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;unnecessary&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;.&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;For&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;this&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;reason&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;the book&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;this&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;dictionary&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;will be&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;very&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;interesting&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;and&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;valuable&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;to readers who&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;need a&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;medical&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;dictionary&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;at home&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;.&lt;/span&gt;&lt;br /&gt;
&lt;br /&gt;
&lt;b&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Oxford&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Concise&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Medical&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Dictionary&lt;/span&gt;&lt;/b&gt;&lt;span class="hps atn" title="Klik untuk terjemahan alternatif"&gt;&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;&lt;/span&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;presented&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;in&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;MSDict&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;electronic format&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;by&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;the developer&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;.&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;MSDict&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;offers&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;best&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;experience&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;in&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;mobile&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;reference&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;and&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;is available&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;for&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;olatform&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;handheld&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;.&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;&lt;/span&gt;&lt;/span&gt;&lt;span class="" id="result_box" lang="en"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;This latest version&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;includes&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;unspecified&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;updates&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;on&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;enhancements&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;or&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;fixes&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;bugs&lt;/span&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;.&lt;/span&gt;&lt;/span&gt;&lt;br /&gt;
&lt;br /&gt;
&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="" id="result_box" lang="en"&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;&lt;b&gt;&lt;span style="color: black;"&gt;Download&lt;/span&gt;&lt;/b&gt;&lt;/span&gt;&lt;/span&gt;&lt;span class="" id="result_box" lang="en"&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;&lt;b&gt;&lt;span style="color: black;"&gt; &lt;/span&gt;&lt;/b&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span style="font-size: large;"&gt;&lt;b&gt;&lt;span class="" id="result_box" lang="en"&gt;&lt;span class="" title="Klik untuk terjemahan alternatif"&gt;&lt;a href="http://www.mediafire.com/?vtkf14c9hfo8zfl" style="color: blue;"&gt;Oxford Concise Medical Dictionary.jar&lt;/a&gt;&lt;/span&gt;&lt;/span&gt;&lt;/b&gt;&lt;/span&gt;&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/oxford-concise-medical-dictionary.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiKutBVryUbPKE88fV2LROJHfEPxYw27IdruM3fbMB3AR_rLjmW3wFHm_qswT97OdTCywH0Ky-akPKp-_5Aecdj3LVVLD56gwRJdSzpuD5y3tEo0BpJG_mKZp3D4Pj0JZM8XzwsfHrtGiM/s72-c/Medical+Dictionary+for+Mobile.jpg" width="72"/><thr:total>0</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-250431522650963262</guid><pubDate>Sun, 12 Jun 2011 13:18:00 +0000</pubDate><atom:updated>2011-06-13T18:15:51.129+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">Medical Jokes</category><title>Low Blood Pressure</title><description>&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiEPHxv3bGTV_SJpDoYaWvzUhdbHkK0ISjFTGBhKaKg-WlL3_F016vyvPg-_zBWahd0OFhTj66TFgb8MMaaPYNMMekNGiZLraqYnPtOKopnh7KqcxMYq-wQF4opgdqXOKNCjbxjH5BZbO0/s1600/Blood+Cartoon.jpg" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiEPHxv3bGTV_SJpDoYaWvzUhdbHkK0ISjFTGBhKaKg-WlL3_F016vyvPg-_zBWahd0OFhTj66TFgb8MMaaPYNMMekNGiZLraqYnPtOKopnh7KqcxMYq-wQF4opgdqXOKNCjbxjH5BZbO0/s320/Blood+Cartoon.jpg" width="320" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Seorang sejawat ditugasi oleh Lembaga Transfusi Darah PMI DKI Jaya untuk melaksanakan"&gt;&lt;/span&gt;&lt;/span&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Seorang sejawat ditugasi oleh Lembaga Transfusi Darah PMI DKI Jaya untuk melaksanakan"&gt;A colleague was assigned by the Institute of Blood Transfusion taking&lt;/span&gt;&lt;span style="background-color: white;" title="kegiatan pengambilan darah pada anggota keluarga besar salah satu ludruk terkenal"&gt; activities in one large family of famous &lt;a href="http://en.wikipedia.org/wiki/Ludruk" style="color: blue;"&gt;ludruk&lt;/a&gt; &lt;/span&gt;&lt;span style="background-color: white;" title="di wilayah Jakarta."&gt;in the Jakarta area. &lt;/span&gt;&lt;span style="background-color: white;" title="Setelah memeriksa seorang pasien, terjadilah percakapan sebagai berikut"&gt;After examining a patient, the following conversation happened...&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Setelah memeriksa seorang pasien, terjadilah percakapan sebagai berikut"&gt;&lt;br /&gt;
&lt;/span&gt;&lt;span style="background-color: white;" title="Dokter : &amp;quot;Bapak, darahnya tidak bisa diambil. Bapak"&gt;&lt;b&gt;Doctor&lt;/b&gt; : Mr. Paijo, your blood couldn't be retrieved. &lt;/span&gt;&lt;/span&gt;&lt;span class="long_text short_text" id="result_box" lang="en" style="background-color: white;"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Now, you&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;can't&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;be&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;blood&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;donors&lt;/span&gt;&lt;/span&gt;&lt;span class="long_text" id="result_box" style="background-color: white;"&gt;&lt;span style="background-color: white;" title="sekarang tidak bisa donor&amp;quot;"&gt;... :(&lt;/span&gt;&lt;/span&gt;&lt;b style="background-color: white;"&gt;&lt;span class="long_text short_text" id="result_box" lang="en"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;&amp;nbsp;&lt;/span&gt;&lt;/span&gt;&lt;/b&gt;&lt;br /&gt;
&lt;div style="background-color: white;"&gt;&lt;b&gt;&lt;span class="long_text short_text" id="result_box" lang="en"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Ludruk&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;Players&lt;/span&gt;&lt;/span&gt;&lt;/b&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Pemain ludruk I : &amp;quot;Kenapa dokter?&amp;quot;"&gt;&lt;b&gt; I&lt;/b&gt; : Why is Doctor ?&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="background-color: white;"&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Pemain ludruk I : &amp;quot;Kenapa dokter?&amp;quot;"&gt; &lt;/span&gt;&lt;span style="background-color: white;" title="Dokter : &amp;quot;Tekanan darah Bapak ini rendah&amp;quot;"&gt;&lt;b&gt;Doctor&lt;/b&gt; : He has low blood pressure... :( &lt;/span&gt;&lt;span style="background-color: white;" title="Pemain ludruk I (dengan agak cemas) : &amp;quot;Bagaimana mengobatinya dokter?&amp;quot;"&gt;&lt;b&gt;&amp;nbsp;&lt;/b&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="background-color: white;"&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Pemain ludruk I (dengan agak cemas) : &amp;quot;Bagaimana mengobatinya dokter?&amp;quot;"&gt;&lt;b&gt;Ludruk Players I&lt;/b&gt; (with a bit anxious): How to treat it Doctor ?&lt;/span&gt;&lt;span style="background-color: white;" title="Pemain ludruk II (nyeletuk) : &amp;quot;Gampang mas, makan saja &amp;quot;tangga&amp;quot;, kan nanti"&gt;&lt;b&gt;&amp;nbsp;&lt;/b&gt;&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;div style="background-color: white;"&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Pemain ludruk II (nyeletuk) : &amp;quot;Gampang mas, makan saja &amp;quot;tangga&amp;quot;, kan nanti"&gt;&lt;b&gt;Ludruk Players II&lt;/b&gt; (&lt;i&gt;nyeletuk&lt;/i&gt;): &lt;/span&gt;&lt;/span&gt;&lt;span class="long_text short_text" id="result_box" lang="en"&gt;&lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;It&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;is very&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;easy&lt;/span&gt; &lt;span class="hps" title="Klik untuk terjemahan alternatif"&gt;friend&lt;/span&gt;&lt;/span&gt;&lt;span class="long_text" id="result_box"&gt;&lt;span style="background-color: white;" title="Pemain ludruk II (nyeletuk) : &amp;quot;Gampang mas, makan saja &amp;quot;tangga&amp;quot;, kan nanti"&gt;, only eating a ladder, Later...&lt;/span&gt;&lt;span style="background-color: white;" title="tekanan darahnya jadi naik tinggi!!&amp;quot;"&gt;yours blood pressure rise so high !.... XD&lt;/span&gt;&lt;/span&gt;&lt;/div&gt;&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/low-blood-pressure.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEiEPHxv3bGTV_SJpDoYaWvzUhdbHkK0ISjFTGBhKaKg-WlL3_F016vyvPg-_zBWahd0OFhTj66TFgb8MMaaPYNMMekNGiZLraqYnPtOKopnh7KqcxMYq-wQF4opgdqXOKNCjbxjH5BZbO0/s72-c/Blood+Cartoon.jpg" width="72"/><thr:total>4</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-6424295094988373181</guid><pubDate>Sat, 11 Jun 2011 12:54:00 +0000</pubDate><atom:updated>2011-06-11T19:54:49.365+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cytoplasm</category><title>Signal Reception</title><description>&lt;div class="contentBody" style="text-align: justify;"&gt;Cells in a multicellular organism need to communicate with  one another to regulate their development into tissues, to control their growth  and division, and to coordinate their functions. Many cells form communicating  junctions that couple adjacent cells, allowing the exchange of ions and small  molecules (see Chapter 4: Epithelial Tissue). Through these channels, also  called gap junctions, signals pass directly from cell to cell without reaching  the extracellular fluid. In other cases, cells display membrane-bound signaling  molecules that influence other cells in direct physical contact.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-create.g?blogID=1016184987758340627" name="711793"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;Extracellular signaling molecules, or messengers, mediate  three kinds of communication between cells. In &lt;b&gt;endocrine signaling,&lt;/b&gt;  hormones are carried in the blood to target cells (ie, cells with specific  receptors to a hormone) throughout the body; in &lt;b&gt;paracrine signaling,&lt;/b&gt;  chemical mediators are rapidly metabolized so that they act on local cells only;  and in &lt;b&gt;synaptic signaling,&lt;/b&gt; neurotransmitters act only on adjacent nerve  cells through special contact areas called &lt;b&gt;synapses&lt;/b&gt; (see Chapter 9: Nerve  Tissue &amp;amp; the Nervous System). In some cases, paracrine signals act on the  same cell type that produced the messenger molecule, a phenomenon called  &lt;b&gt;autocrine signaling.&lt;/b&gt; Each cell type in the body contains a distinctive  set of receptor proteins that enables it to respond to a complementary set of  signaling molecules in a specific, programmed way (Figure 2–9).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-9&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEh6cZJDjJB-GzD9zA11d2GLYD5Qeuf9C0fdQdzotxT1q1-nzK-oq007Sgu5p1149G2C_WfqV9Y2bgPywD0pqFr4Nln_4cm7rQUpiHsqe55h6UuxYyI2PPNCsNDhP5EbVwmA473E0z5MDK8/s1600/Figure+2-9.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="210" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEh6cZJDjJB-GzD9zA11d2GLYD5Qeuf9C0fdQdzotxT1q1-nzK-oq007Sgu5p1149G2C_WfqV9Y2bgPywD0pqFr4Nln_4cm7rQUpiHsqe55h6UuxYyI2PPNCsNDhP5EbVwmA473E0z5MDK8/s320/Figure+2-9.bmp" width="320" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Cells respond to chemical signals according to the library of  receptors they have. In this schematic representation, three cells appear with  different receptors, and the extracellular environment contains several ligands  that will interact with the appropriate receptors. Considering that the  extracellular environment contains a multitude of molecules, it is important  that ligands and the respective receptors exhibit complementary morphology and  great affinity.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&amp;nbsp;&amp;nbsp;&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Signaling molecules differ in their water solubility. Small  &lt;b&gt;hydrophobic signaling molecules,&lt;/b&gt; such as steroid and thyroid hormones,  diffuse through the plasma membrane of the target cell and activate receptor  proteins inside the cell. In contrast, &lt;b&gt;hydrophilic signaling molecules,&lt;/b&gt;  including neurotransmitters, most hormones, and local chemical mediators  (paracrine signals), activate receptor proteins on the surface of target cells.  These receptors, which span the cell membrane, relay information to a series of  intracellular intermediaries that ultimately passes the signal to its final  destination in either the cytoplasm or the nucleus. The numerous intercellular  hydrophilic messengers rely on membrane proteins that direct the flow of  information from the receptor to the rest of the cell. The best studied of these  proteins are the &lt;b&gt;G proteins,&lt;/b&gt; so named because they bind to guanine  nucleotides. Once a &lt;b&gt;first messenger&lt;/b&gt; (hormone, neurotransmitter, paracrine  signal) binds to a receptor, conformational changes occur in the receptor; this,  in turn, activates the G protein–guanosine diphosphate complex (Figure 2–10). A  guanosine diphosphate–guanosine triphosphate exchange releases the&amp;nbsp; subunit of the G  protein, which acts on other membrane-bound intermediaries called  &lt;b&gt;effectors.&lt;/b&gt; Often, the effector is an enzyme that converts an inactive  precursor molecule into an active &lt;b&gt;second messenger,&lt;/b&gt; which can diffuse  through the cytoplasm and carry the signal beyond the cell membrane. Second  messengers trigger a cascade of molecular reactions that leads to changes in  cell behavior. The examples listed in Table 2–2 illustrate the diversity of G  proteins present in various tissues and their roles in regulating important cell  functions.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 2-10&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEj-W9SvlZfEz6A6U5du9-5pRnyTA9cZETbE1Z_pEQsa_jCZQyCpIAGSyZNvHjGqUePLoLpc8VwdbUPIjKdr9juEJfdcTpv2WiWDh0JfnO62LKBn02s6hczAbdG78h9j-Qrf-2-DvI6UJFM/s1600/Figure+2-10.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEj-W9SvlZfEz6A6U5du9-5pRnyTA9cZETbE1Z_pEQsa_jCZQyCpIAGSyZNvHjGqUePLoLpc8VwdbUPIjKdr9juEJfdcTpv2WiWDh0JfnO62LKBn02s6hczAbdG78h9j-Qrf-2-DvI6UJFM/s400/Figure+2-10.bmp" width="346" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Diagram illustrating how G proteins switch effectors on and off.  (Modified and reprinted, with permission, from Linder M, Gilman AG: G proteins.  Sci Am 1992;267:56.)&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;table bgcolor="#ffffff" border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#cccccc" style="border-left: rgb(102,102,102) 1px solid; border-right: rgb(102,102,102) 1px solid; border-top: rgb(102,102,102) 1px solid;"&gt;&lt;table border="0" cellpadding="3" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td&gt;&lt;div class="tableTitle"&gt;Table 2–2. A Sampling of Physiological Effects Mediated by G  Proteins.&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td&gt;&lt;table bgcolor="#666666" border="0" cellpadding="3" cellspacing="1"&gt;&lt;colgroup span="5"&gt;&lt;/colgroup&gt; &lt;thead&gt;
&lt;tr class="font12"&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Stimulus&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Affected Cell Type&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;G Protein&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Effector&lt;/th&gt; &lt;th align="left" bgcolor="#ffffff" valign="top"&gt;Effect&lt;/th&gt;&lt;/tr&gt;
&lt;/thead&gt; &lt;tbody&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Epinephrine,  glucagon&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Liver cells&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;G&lt;sub&gt;s&lt;/sub&gt;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Adenylyl cyclase&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Breakdown of  glycogen&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Epinephrine,  glucagon&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Fat cells&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;G&lt;sub&gt;s&lt;/sub&gt;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Adenylyl cyclase&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Breakdown of  fat&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Luteinizing hormone&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Ovarian follicles&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;G&lt;sub&gt;s&lt;/sub&gt;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Adenylyl cyclase&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Increased synthesis of  estrogen and progesterone&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Antidiuretic hormone&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Kidney cells&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;G&lt;sub&gt;s&lt;/sub&gt;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Adenylyl cyclase&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Conservation of water by  kidney&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Acetylcholine&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Heart muscle cells&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;G&lt;sub&gt;j&lt;/sub&gt;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Potassium channel&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Slowed heart rate and  decreased pumping force&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Enkephalins, endorphins,  opioids&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Brain neurons&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;G&lt;sub&gt;j&lt;/sub&gt;/G&lt;sub&gt;o&lt;/sub&gt;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Calcium and potassium  channels, adenylyl cyclase&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Changed electrical  activity of neurons&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Angiotensin&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Smooth muscle cells in  blood vessels&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;G&lt;sub&gt;q&lt;/sub&gt;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Phospholipase C&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Muscle contraction;  elevation of blood pressure&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Odorants&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Neuroepithelial cells in  nose&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;G&lt;sub&gt;olf&lt;/sub&gt;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Adenylyl cyclase&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Detection of  odorants&lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Light&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Rod and cone cells in  retina&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;G&lt;sub&gt;t&lt;/sub&gt;&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Cyclic GMP  phosphodiesterase&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Detection of visual  signals &lt;/td&gt;&lt;/tr&gt;
&lt;tr class="font12"&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Pheromone&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Baker's yeast&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;GPA1&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Unknown&lt;/td&gt; &lt;td align="left" bgcolor="#ffffff" class="font12" valign="top"&gt;Mating of cells&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;div class="font12"&gt;Reproduced, with permission, from Linder M, Gilman AG: G  proteins. Sci Am 1992;267:56.&lt;/div&gt;&lt;div class="font12"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font12"&gt;&lt;b&gt;&lt;i style="color: red;"&gt;Medical Application&lt;/i&gt;&lt;/b&gt;&lt;/div&gt;&lt;div class="font12" style="text-align: justify;"&gt;Several diseases have been shown to be due to defective receptors. For example,  pseudohypoparathyroidism and a type of dwarfism are due to nonfunctioning  parathyroid and growth hormone receptors. In these two conditions the glands  produce the respective hormones, but the target cells do not respond, because  they lack normal receptors.&lt;/div&gt;&lt;div class="font12"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font12"&gt;&lt;b&gt;Signaling Mediated by Intracellular Receptors&lt;/b&gt;&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;Steroid hormones are small hydrophobic (lipid-soluble)  molecules; binding reversibly to carrier proteins in the plasma transports them  in the blood. Once released from their carrier proteins, they diffuse through  the plasma membrane lipids of the target cell and bind reversibly to specific  steroid hormone–receptor proteins in the cytoplasm or the nucleus. The binding  of hormone activates the receptor, enabling it to bind with high affinity to  specific DNA sequences; this generally increases the level of transcription from  specific genes. Each steroid hormone is recognized by a different member of a  family of homologous receptor proteins. Thyroid hormones are modified lipophilic  amino acids that also act on intracellular receptors.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td bgcolor="#ffffff" valign="top"&gt;&lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Afzelius BA, Eliasson R: Flagellar mutants in  man: on the heterogeneity of the immotile-cilia syndrome. J Ultrastruct Res  1979;69:43. [PMID: 501788] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Aridor M, Balch WE: Integration of endoplasmic  reticulum signaling in health and disease. Nat Med 1999;5:745. [PMID: 10395318]  &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Barrit GJ: &lt;i&gt;Communication Within Animal  Cells&lt;/i&gt;. Oxford University Press, 1992. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Becker WM et al: &lt;i&gt;The World of the Cell&lt;/i&gt;,  4th ed. Benjamin/Cummings, 2000. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Bretscher MS: The molecules of the cell  membrane. Sci Am 1985;253:100. [PMID: 2416050] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brinkley BR: Microtubule organizing centers.  Annu Rev Cell Biol 1985;1:145. [PMID: 3916316] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Brown MS et al: Recycling receptors: the  round-trip itinerary of migrant membrane proteins. Cell 1983;32:663. [PMID:  6299572] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Cooper GM: &lt;i&gt;The Cell: A Molecular  Approach&lt;/i&gt;. ASM Press/Sinauer Associates, Inc., 1997. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: &lt;i&gt;A Guided Tour of the Living  Cell&lt;/i&gt;. Freeman, 1984. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;DeDuve C: Microbodies in the living cell. Sci  Am 1983;248:74. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Dustin P: &lt;i&gt;Microtubules&lt;/i&gt;, 2nd ed.  Springer-Verlag, 1984. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Farquhar MG: Progress in unraveling pathways of  Golgi traffic. Annu Rev Cell Biol 1985;1:447. [PMID: 3916320] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Fawcett D: &lt;i&gt;The Cell&lt;/i&gt;, 2nd ed. Saunders,  1981. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Krstíc RV: &lt;i&gt;Ultrastructure of the Mammalian  Cell&lt;/i&gt;. Springer-Verlag, 1979. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Mitchison TJ, Cramer LP: Actin-based cell  motility and cell locomotion. Cell 1996;84:371. [PMID: 8608590] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Osborn M, Weber K: Intermediate filaments:  cell-type-specific markers in differentiation and pathology. Cell 1982;31:303.  [PMID: 6891619] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Pfeffer SR, Rothman JE: Biosynthetic protein  transport and sorting in the endoplasmic reticulum. Annu Rev Biochem  1987;56:829. [PMID: 3304148] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Rothman J: The compartmental organization of  the Golgi apparatus. Sci Am 1985;253:74. [PMID: 3929377] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Simons K, Ikonen E: How cells handle  cholesterol. Science 2000;290:1721. [PMID: 11099405] &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Tzagoloff A: &lt;i&gt;Mitochondria&lt;/i&gt;. Plenum, 1982.  &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Weber K, Osborn M: The molecules of the cell  matrix. Sci Am 1985;253:110. [PMID: 4071030] &lt;/td&gt;&lt;/tr&gt;
&lt;/tbody&gt;&lt;/table&gt;&lt;/td&gt;&lt;/tr&gt;
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&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/signal-reception.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEh6cZJDjJB-GzD9zA11d2GLYD5Qeuf9C0fdQdzotxT1q1-nzK-oq007Sgu5p1149G2C_WfqV9Y2bgPywD0pqFr4Nln_4cm7rQUpiHsqe55h6UuxYyI2PPNCsNDhP5EbVwmA473E0z5MDK8/s72-c/Figure+2-9.bmp" width="72"/><thr:total>2</thr:total><author>noreply@blogger.com (deztroyer28)</author></item><item><guid isPermaLink="false">tag:blogger.com,1999:blog-1016184987758340627.post-1367548884875584282</guid><pubDate>Fri, 10 Jun 2011 14:31:00 +0000</pubDate><atom:updated>2011-06-10T21:34:40.045+07:00</atom:updated><category domain="http://www.blogger.com/atom/ns#">The Cell Nucleus</category><title>Cell Division</title><description>&lt;div class="contentBody" style="text-align: justify;"&gt;Cell division, or mitosis (Gr. &lt;i&gt;mitos,&lt;/i&gt; a thread), can  be observed with the light microscope. During this process, the parent cell  divides, and each of the daughter cells receives a chromosomal set identical to  that of the parent cell. Essentially, a longitudinal duplication of the  chromosomes takes place, and these chromosomes are distributed to the daughter  cells. The phase between two mitoses is called &lt;b&gt;interphase,&lt;/b&gt; during which  the nucleus appears as it is normally observed in microscopic preparations. The  process of mitosis is subdivided into phases to facilitate its study (Figures  3-15, 3-16, and 3-17).&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="tableTitle"&gt;&lt;b&gt;Figure 3-15&lt;/b&gt;&lt;/div&gt;&lt;div class="font11"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgOOyuRxqq9sfDg7j5NcVsyySbX_SseLuc1d3COy2j4CmU0eWSGuXdqYm0A48Up0k3LLdOJmpRlEptlupfShJCSF5Nsi0MnAP86DUlBTiqb73Vmpens7BaAhyphenhyphen88a8uPAp_ke3sUkSxzz-Y/s1600/Figure+3-15.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="251" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgOOyuRxqq9sfDg7j5NcVsyySbX_SseLuc1d3COy2j4CmU0eWSGuXdqYm0A48Up0k3LLdOJmpRlEptlupfShJCSF5Nsi0MnAP86DUlBTiqb73Vmpens7BaAhyphenhyphen88a8uPAp_ke3sUkSxzz-Y/s400/Figure+3-15.bmp" width="400" /&gt;&lt;/a&gt;Phases of mitosis.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
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&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 3-16&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjPWhLbFFp9Vz8rfg-QWP5lT-R9_OswbDcTVnWY507x3JNX2UCazT9LW1w9AKnDS-NZvEPAIq-Th2Vip4A2rHuUD4QtOazzDyw-oEeBCnDfazrjs-emUE2pNgL8Er4sWLSFoU_qr6cGHog/s1600/Figure+3-16+A.bmp" imageanchor="1" style="clear: left; float: left; margin-bottom: 1em; margin-right: 1em;"&gt;&lt;/a&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjPWhLbFFp9Vz8rfg-QWP5lT-R9_OswbDcTVnWY507x3JNX2UCazT9LW1w9AKnDS-NZvEPAIq-Th2Vip4A2rHuUD4QtOazzDyw-oEeBCnDfazrjs-emUE2pNgL8Er4sWLSFoU_qr6cGHog/s400/Figure+3-16+A.bmp" width="333" /&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjbunbkF9Po06v7JBExM5kLuUPtrHhGAXqjZ9FFZ-lnfTMTJ_X6s2LVj8oyybIFAFz4HMCKpSraORbJ1pWwYI9u-xzPBSGzBuJJcSbXV-9sdEg3YNQeQRs3EMPtnDtQ-QscMfPr677J6J4/s1600/Figure+3-16+B.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjbunbkF9Po06v7JBExM5kLuUPtrHhGAXqjZ9FFZ-lnfTMTJ_X6s2LVj8oyybIFAFz4HMCKpSraORbJ1pWwYI9u-xzPBSGzBuJJcSbXV-9sdEg3YNQeQRs3EMPtnDtQ-QscMfPr677J6J4/s400/Figure+3-16+B.bmp" width="333" /&gt;&lt;/a&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgx3CUkcIjGcQQ6t27uE0mTxzhKDNoDZ0meY_5fW2EOigHQbhOFGoVo9mRxRUFwfz2qb6QE2sAv9XNMxEciUMZ-n8rdynCF7olLg_9TYtip71KkzlfgGWD7XLeZdV-Qj8a5x4eMJrVUuLM/s1600/Figure+3-16+C.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgx3CUkcIjGcQQ6t27uE0mTxzhKDNoDZ0meY_5fW2EOigHQbhOFGoVo9mRxRUFwfz2qb6QE2sAv9XNMxEciUMZ-n8rdynCF7olLg_9TYtip71KkzlfgGWD7XLeZdV-Qj8a5x4eMJrVUuLM/s400/Figure+3-16+C.bmp" width="356" /&gt;&lt;/a&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg0SnxQdgI0-Ucqnzm1sGLBV1lHZ4FcCkPBCenOLzG5KtJk1wiBEffBwMnkeAID6AkBHRI3FB4UZtNqH2DaMxUOzRVMxuvpbvW-utc19iuBHTSe4L27va_jHgCy_kH4ehCq4tTCrg2u6iQ/s1600/Figure+3-16+D.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEg0SnxQdgI0-Ucqnzm1sGLBV1lHZ4FcCkPBCenOLzG5KtJk1wiBEffBwMnkeAID6AkBHRI3FB4UZtNqH2DaMxUOzRVMxuvpbvW-utc19iuBHTSe4L27va_jHgCy_kH4ehCq4tTCrg2u6iQ/s400/Figure+3-16+D.bmp" width="296" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div style="text-align: justify;"&gt;Photomicrograph of cultured cells to show cell division.  Picrosiriusâ€“hematoxylin stain. Medium magnification. &lt;b&gt;A:&lt;/b&gt; Interphase  nuclei. Note the chromatin and nucleoli inside each nucleus. &lt;b&gt;B:&lt;/b&gt; Prophase.  No distinct nuclear envelope, no nucleoli. Condensed chromosomes. &lt;b&gt;C:&lt;/b&gt;  Metaphase. The chromosomes are located in a plate at the cell equator. &lt;b&gt;D:&lt;/b&gt;  Late anaphase. The chromosomes are located in both cell poles, to distribute the  DNA equally between the daughter cells.&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;b&gt;Figure 3-17&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjuUPHK-5FTSL22xBSCb1H1Yf7UXWpTejw1YVs6OSA9YA93SdmuSNd0kqXt3jNqMPH0WvoumegMKb5F4eekD0dPqruT6u873Af_uD14DnY-GZDgEOVUSgR0gx5DiLZPWbyVXRii6xrEwTg/s1600/Figure+3-17.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="285" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjuUPHK-5FTSL22xBSCb1H1Yf7UXWpTejw1YVs6OSA9YA93SdmuSNd0kqXt3jNqMPH0WvoumegMKb5F4eekD0dPqruT6u873Af_uD14DnY-GZDgEOVUSgR0gx5DiLZPWbyVXRii6xrEwTg/s400/Figure+3-17.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Images obtained with a confocal laser scanning microscope from  cultured cells. An interphase nucleus and several nuclei are in several phases  of mitosis. DNA appears red, and microtubules in the cytoplasm are blue. Medium  magnification. &lt;b&gt;A:&lt;/b&gt; Interphase. A nondividing cell. &lt;b&gt;B:&lt;/b&gt; Prophase. The  blue structure over the nucleus is the centrosome. Note that the chromosomes are  becoming visible because of their condensation. The cytoplasm is acquiring a  round shape typical of cells in mitosis. &lt;b&gt;C:&lt;/b&gt; Metaphase. The chromosomes  are organized in an equatorial plane. &lt;b&gt;D:&lt;/b&gt; Anaphase. The chromosomes are  pulled to the cell poles through the activity of microtubules. &lt;b&gt;E:&lt;/b&gt; Early  telophase. The two sets of chromosomes have arrived at the cell poles to  originate the two daughter cells, which will contain sets of chromosomes similar  to those in the mother cell. &lt;b&gt;F:&lt;/b&gt; Telophase. The cytoplasm is being divided  by a constriction in the cell equator. Note that the daughter cells are round  and smaller than the mother cell. Soon they will increase in size and become  elongated. (Courtesy of R Manelli-Oliveira, R Cabado, and G  Machado-Santelli.)&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;The &lt;b&gt;prophase&lt;/b&gt; of mitosis is characterized by the  gradual coiling of nuclear chromatin (uncoiled chromosomes), giving rise to  several individual rod- or hairpin-shaped bodies (coiled chromosomes) that stain  intensely. At the end of prophase, the nuclear envelope is broken by  phosphorylation (addition of PO&lt;sub&gt;4&lt;/sub&gt;&lt;sup&gt;3-&lt;/sup&gt;) of the nuclear  lamina proteins, originating vesicles that remain in the cytoplasm. The  centrosomes with their centrioles separate, and a centrosome migrates to each  pole of the cell. The duplication of the centrosomes and centrioles starts in  the interphase, before mitosis. Simultaneously with centrosome migration, the  microtubules of the mitotic spindle appear between the two centrosomes, and the  nucleolus disintegrates.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=1367548884875584282" name="712708"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;During &lt;b&gt;metaphase,&lt;/b&gt; chromosomes, due to the activity  of microtubules, migrate to the equatorial plane of the cell, where each divides  longitudinally to form two chromosomes called sister chromatids. The chromatids  attach to the microtubules of the mitotic spindle (Figures 3-18 and 3-19) at  an electron-dense, DNA protein plaque, the &lt;b&gt;kinetochore&lt;/b&gt; (Gr.  &lt;i&gt;kinetos,&lt;/i&gt; moving, + &lt;i&gt;chora,&lt;/i&gt; central region), located close to the  &lt;b&gt;centromere&lt;/b&gt; (Gr. &lt;i&gt;kentron,&lt;/i&gt; center, + &lt;i&gt;meros,&lt;/i&gt; part) of each  chromatid.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="tableTitle"&gt;&lt;b&gt;Figure 3-18&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgKKX_quygpPaFQ5IBNC2BT_r4NPkVir-Sey9F24MUuVnbVtD7TFOY3nwrr4ShAdZwcpLAsCOGZWkN9zdjqCiR_Z1_IXavpW0E-O5-XwMBSskWLGlHtotFq7sfRwXiv3a7US6qRd8o5AF8/s1600/Figure+3-18.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="400" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgKKX_quygpPaFQ5IBNC2BT_r4NPkVir-Sey9F24MUuVnbVtD7TFOY3nwrr4ShAdZwcpLAsCOGZWkN9zdjqCiR_Z1_IXavpW0E-O5-XwMBSskWLGlHtotFq7sfRwXiv3a7US6qRd8o5AF8/s400/Figure+3-18.bmp" width="276" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Electron micrograph of a section of a rooster spermatocyte in  metaphase. The figure shows the two centrioles in each pole, the mitotic spindle  formed by microtubules, and the chromosomes in the equatorial plane. The arrows  show the insertion of microtubules in the centromeres. Reduced from  &lt;small&gt;x&lt;/small&gt;19,000. (Courtesy of R McIntosh.)&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Figure 3-19&lt;/b&gt;&lt;/div&gt;&lt;div class="separator" style="clear: both; text-align: center;"&gt;&lt;a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgaM6mWqC4AyPli-5RyG89sR2AO0DK0ISf3IneNklDw50WtTgYv895KWb-K3zNI5GMXVWewYNnv9Hb7i23d8bxkAPcsgSVIMJBAdFacH6UfJdFUR1Hly3MWL6ljtRm_Xa_DSmHyxWqgO0U/s1600/Figure+3-19.bmp" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"&gt;&lt;img border="0" height="317" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgaM6mWqC4AyPli-5RyG89sR2AO0DK0ISf3IneNklDw50WtTgYv895KWb-K3zNI5GMXVWewYNnv9Hb7i23d8bxkAPcsgSVIMJBAdFacH6UfJdFUR1Hly3MWL6ljtRm_Xa_DSmHyxWqgO0U/s400/Figure+3-19.bmp" width="400" /&gt;&lt;/a&gt;&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;Electron micrograph of the metaphase of a human lung cell in  tissue culture. Note the insertion of microtubules in the centromeres (arrows)  of the densely stained chromosomes. Reduced from &lt;small&gt;x&lt;/small&gt;50,000.  (Courtesy of R McIntosh.)&lt;/div&gt;&lt;div class="font11" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;In &lt;b&gt;anaphase,&lt;/b&gt; the sister chromatids separate from  each other and migrate toward the opposite poles of the cell, pulled by  microtubules. Throughout this process, the centromeres move away from the  center, pulling the remainder of the chromosome along. The centromere is the  constricted region of a mitotic chromosome that holds the two sister chromatids  together until the beginning of anaphase.&lt;/div&gt;&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=1367548884875584282" name="712710"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;b&gt;Telophase&lt;/b&gt; is characterized by the reappearance of  nuclei in the daughter cells. The chromosomes revert to their semidispersed  state, and the nucleoli, chromatin, and nuclear envelope reappear. While these  nuclear alterations are taking place, a constriction develops at the equatorial  plane of the parent cell and progresses until the cytoplasm and its organelles  are divided in two. This constriction is produced by microfilaments of actin  associated with myosin that accumulate in a beltlike shape beneath the cell  membrane.&lt;/div&gt;&lt;a href="http://www.blogger.com/post-edit.g?blogID=1016184987758340627&amp;amp;postID=1367548884875584282" name="712711"&gt;&lt;/a&gt; &lt;br /&gt;
&lt;div class="contentBody" style="text-align: justify;"&gt;Most tissues undergo constant cell turnover because of  continuous cell division and the ongoing death of cells. Nerve tissue and  cardiac muscle cells are exceptions, since they do not multiply postnatally and  therefore cannot regenerate. The turnover rate of cells varies greatly from one  tissue to another rapid in the epithelium of the digestive tract and the  epidermis and slow in the pancreas and the thyroid gland.&lt;/div&gt;&lt;div class="font11"&gt;&lt;br /&gt;
&lt;/div&gt;&lt;div class="contentHead3"&gt;&lt;b&gt;References&lt;/b&gt;&lt;/div&gt;&lt;table border="0" cellpadding="0" cellspacing="0"&gt;&lt;tbody&gt;
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&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Jordan EG, Cullis CA (editors): &lt;i&gt;The  Nucleolus&lt;/i&gt;. Cambridge University Press, 1982. &lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt; &lt;td class="contentBody" valign="top"&gt;Kornberg RD, Klug A: The nucleosome. Sci Am  1981;244:52. [PMID: 7209486] &lt;/td&gt;&lt;/tr&gt;
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&lt;div class="contentBody" style="text-align: justify;"&gt;&lt;/div&gt;</description><link>http://dehistology.blogspot.com/2011/06/cell-division.html</link><media:thumbnail xmlns:media="http://search.yahoo.com/mrss/" height="72" url="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEgOOyuRxqq9sfDg7j5NcVsyySbX_SseLuc1d3COy2j4CmU0eWSGuXdqYm0A48Up0k3LLdOJmpRlEptlupfShJCSF5Nsi0MnAP86DUlBTiqb73Vmpens7BaAhyphenhyphen88a8uPAp_ke3sUkSxzz-Y/s72-c/Figure+3-15.bmp" width="72"/><thr:total>76</thr:total><author>noreply@blogger.com (deztroyer28)</author></item></channel></rss>