LIPASE RESEARCH

ENZYMES INDIGENOUS TO MILK | Lipases and Esterases

noreply@blogger.com (Diagnostic Research) — Mon, 09 May 2011 21:03:00 +0000

Abstract
Bovine milk contains a native lipoprotein lipase (LPL) that preferentially acts on emulsified substrates at water–oil interfaces and several esterases that preferentially act on soluble ester substrates. The lipase is by far the most abundant, most studied, best characterized, and of most practical significance. It is synthesized in the mammary gland and transported to the milk where, under certain circumstances, it catalyzes the hydrolysis of triacylglycerols to free fatty acids and mono- and diacylglycerols. It is mostly bound to the casein micelles but can move to the milk fat globule membrane under conditions that induce lipolysis of the globular fat. It is a glycoprotein of molecular mass 100 kDa and requires lipoproteins or apolipoproteins for full activity. By contrast, the esterases in milk are not well characterized. They are present in low concentrations except in abnormal milks such as colostrum and mastitic milks. The types reported include arylesterases, carboxylesterases, and cholinesterases. They seem to have no significant technological importance in milk. Human milk contains a relatively high concentration of a bile salt-stimulated lipase, in addition to LPL, which does not appear to be present in bovine milk. It has a role in the digestion of milk fat in neonates.

Encyclopedia of Dairy Sciences (Second Edition)
Pages 304-307

White and green tea polyphenols inhibit pancreatic lipase in vitro

noreply@blogger.com (Diagnostic Research) — Mon, 15 Nov 2010 20:26:00 +0000

Abstract
Green, white and black teas were assayed for inhibition of pancreatic lipase activity in vitro. White tea proved to be more effective than green tea with black tea showing little inhibition even at 200 μg GAE/ml. The EC50 values for inhibition were 22 μg/ml for white tea and 35 μg/ml for green tea; both easily achievable from normal infusions of tea. Liquid chromatography-mass spectroscopy analysis showed that white and green teas had essentially equal amounts of flavan-3-ols but green tea had higher levels of flavonols. White tea had higher levels of 5-galloyl quinic acid, digalloyl glucose, trigalloyl glucose and the tannin, strictinin.

After chromatography on Sephadex LH-20, the main inhibitory fraction was enriched in strictinin and fractions enriched in other components were ineffective. This suggests that strictinin content may be crucial for inhibition of pancreatic lipase. However, the possibility of synergies between the polyphenols cannot be disregarded.

Anais Gondoina, Dominic Grussua, Derek Stewarta and Gordon J. McDougall

Gut Wall Compromise in the Presence of Pancreatic Enzymes Causes Circulatory Shock

noreply@blogger.com (Diagnostic Research) — Wed, 15 Sep 2010 20:06:00 +0000

ABSTRACT

Pancreatic proteolytic enzymes (PEs) in the ischemic intestine play a central role in multisystem organ failure, which can be prevented by protease inhibition in the small intestine lumen. PEs, if allowed to circulate systemically may also result in shock. However, it is unclear whether enzyme liberation in an intestine with increased permeability alone leads to shock. To test this idea the non-ischemic rat small intestinal lumen was perfused for two hours with either (A) PEs, (B) interventions designed to increase lumenal permeability (N-acetylcysteine (NAC) + atropine + increased flow) or (C) both, and animals were observed for shock and organ failure. PEs perfused (Groups A and C) included trypsin, chymotrypsin, elastase, amylase and lipase at concentrations 2 log greater than baseline values. Group A (n=6) maintained baseline blood pressures as did other groups perfused with single enzymes alone. However all animals in Group C (n=6) developed hypotension, significant increases in gut permeability (p<0.001) and died (p<0.001). Group B (n=6) developed mild hypotension (NS) and increased gut permeability (p<0.05) compared to controls but there were no deaths. These experiments demonstrate for the first time that increased gut permeability in the presence of lumenal PEs is sufficient to induce shock. PEs, if allowed to penetrate the gut wall result in multiorgan failure and death. Supported by NIH Grant GM085072

Erik B. Kistler1,2 and Geert W. Schmid-Schonbein1
1 Department of Bioengineering
2 Department of Anesthesia, University of California, San Diego, San Diego, CA

Inhibition of Pancreatic Lipase and the Renin Angiotensin System Synergistically Decreases Body Fat

noreply@blogger.com (Diagnostic Research) — Thu, 28 Jan 2010 19:09:00 +0000

We have recently demonstrated that mice lacking renin are lean, and excrete more fat in the feces, which is associated with less than 20 % expression of pancreatic lipase and colipase. Treating wild type (WT) mice with an angiotensin receptor blocker losartan (ARB) or an angiotensin converting enzyme (ACE) inhibitor enalapril does not affect body weight, body fat, fecal fat excretion and pancreatic lipase expression, although their colipase expression in the pancreas is decreased to the low levels of the Ren1c–/– mice. Because colipase is necessary for activation of lipase, we hypothesized that inhibition of both pancreatic lipase and colipase by combination of ARB or ACE inhibitor and lipase inhibitor (orlistat) more effectively decreases body weight and body fat than either of them alone. Treating WT mice with both losartan (0.45g/L in drinking water) and orlistat (200 mg/kg diet) for two weeks reduced the body fat significantly more than mice treated with losartan alone or orlistat alone (control 12.5±1.42 %, losartan 8.7±1.9 %, orlistat 3.8±0.8 %, losartan + orlistat 0.2±2.5 %).

The fecal fat content in mice treated with losartan and orlistat is also significantly higher than that of mice treated with losartan alone or orlistat alone (control 46.1±6.2 mg/day, losartan 32.0±4.0 mg/day, orlistat 137.1±9.6 mg/day, losartan + orlistat 186.0±39.6 mg/day). We conclude that inhibiting pancreatic lipase and colipase by using combination of lipase inhibitor and ARB or ACE inhibitor is a promising treatment of the metabolic syndrome.

Feng Li; Nobuyuki Takahashi
Univ of North Carolina at CH, Chapel Hill, NC

This research has received full or partial funding support from the American Heart Association, Mid-Atlantic Affiliate (Maryland, North Carolina, South Carolina, Virginia & Washington, DC

A Study of Pancreatic Function among Subjects over Ninety Years of Age

noreply@blogger.com (Diagnostic Research) — Tue, 24 Nov 2009 18:26:00 +0000

Pancreatology 2009;9:240-244 (DOI: 10.1159/000212090)

Background: Among the various studies of pancreatic function in the elderly published so far, none have dealt with subjects over 90 years of age. The aim of this study was to examine pancreatic function in healthy individuals over 90 years old.

Methods: Sixty-eight healthy noninstitutionalized elderly persons, aged 91-104 years, with a mean age of 95 years, and 63 younger controls were studied. Pancreatic function was studied by determining fecal elastase 1 concentration. In addition to this test, we also measured serum amylase, pancreatic isoamylase and lipase in 53 of the 68 elderly subjects.

Results: All but 1 of the 68 elderly subjects had normal elastase 1 values; the one who did not had a value slightly below normal. No significant difference with controls was found.

Serum pancreatic enzymes were normal in almost all of the 53 elderly studied; 3 had a mild elevation only of amylase and 1 had a persistent elevation of amylase, pancreatic isoamylase and lipase. Conclusions: In subjects over 90 years of age, exocrine pancreatic function continues to be normal; if an impairment occurs, it is mild and not significant for digestion of food.

In addition, serum pancreatic enzymes remain within normal limits in the vast majority of cases.

Lucio Gulloa, Patrizia Simonia, Marina Miglioria, Laura Lucrezioa, Michela Bassia, Franca Fraua, Pier Lorenzo Costaa, Vincenzo Nesticòb

aInstitute of Internal Medicine, University of Bologna, St. Orsola Hospital, Bologna, and
bInstitute of Internal Medicine, Civile Hospital, Catanzaro, Italy

Address of Corresponding Author

Ruptured ectopic pregnancy mimicking acute pancreatitis.

noreply@blogger.com (Diagnostic Research) — Thu, 20 Aug 2009 16:16:00 +0000

Mitura K, Romanczuk M.
Department of General Surgery, Siedlce Hospital, Siedlce, Poland.

INTRODUCTION: Ectopic pregnancy may lead to massive haemorrhage, infertility or death. Prompt diagnosis and treatment are crucial to save patients who would otherwise die. Serum amylase and lipase measurements are known biochemical markers of pancreatic inflammation and a recognized finding that may help diagnose acute pancreatitis. To the best of our knowledge (Medline, Pubmed, Cochrane Library have been researched) the following study presents the first case of ruptured ectopic pregnancy accompanied by markedly elevated amylase and lipase levels mimicking acute pancreatitis ever reported.

CASE REPORT: A previously healthy, nulliparous 35-year-old woman was admitted to hospital with a 2-day history of abdominal pain and vomiting. Her last menstrual period was 7 weeks before presentation. At the admission, the patient was hemodynamically stable. The abdomen was soft with tenderness in its mesogastric area. Blood tests revealed markedly elevated activities of the pancreatic enzymes. Acute pancreatitis was the early clinical diagnosis and subsequent therapy was initiated. After 12 hours the condition of the patient suddenly worsened. She was clinically shocked with pallor, hypotension and tachycardia. Laboratory tests revealed anaemia and increased activities of pancreatic enzymes. An ultrasound examination demonstrated an accumulation of intraperitoneal fluid in the pelvis. Subsequently, the patient was subjected to immediate laparotomy. The peritoneal cavity contained large amount of blood. A cystic mass was found and extracted from the ruptured and bleeding right fallopian tube. Histological examination confirmed a rupture of an ectopic pregnancy of a 6-week-old foetus with an intact gestational sac. The patient made an uneventful recovery and was discharged from hospital after 8 days.

CONCLUSIONS: Our case proves that a misdiagnosed ruptured ectopic pregnancy in the event of elevated activities of pancreatic enzymes may lead to delayed diagnosis of haemorrhage to peritoneum, resulting in hemodynamic instability

The level and clinical significance of pancreatic enzymes in survivors of acute paraquat poisoning

noreply@blogger.com (Diagnostic Research) — Mon, 22 Jun 2009 16:03:00 +0000

INTRODUCTION: Acute paraquat poisoning is often fatal. When ingested, paraquat affects multiple organs including the lung, gastrointestinal tract, pancreas, kidney, heart, and central nervous system. Our center previously found that initial pancreatic function was related to the prognosis of patients with acute paraquat poisoning. However, pancreatic injury after paraquat intoxication has been incompletely studied.

METHODS: This study analyzed the clinical outcome and extent of pancreatic injury in 34 survivors of acute paraquat poisoning. Paraquat exposure was assessed based on a quantitative measure of the plasma level of paraquat by high-performance liquid chromatography. The subsequent variations in the level of pancreatic enzymes, clinical symptoms, and abdominal computed tomography were obtained. Outcomes after acute paraquat poisoning were categorized as pancreatic enzyme elevation group (elevation group: amylase >160 IU/L and lipase >100 IU/L) and nonelevation group.

RESULTS: Pancreatic enzyme elevations occurred in seven cases (20.6%), and the level of pancreatic enzymes peaked at day 7. The elevation in pancreatic enzymes after paraquat ingestion was positively correlated with the plasma paraquat level (p < 0.05 at days 4 and 7). Creatinine was higher in the elevation group. Abdominal computed tomography of the seven cases showed no evidence of pancreatitis, and significant abdominal pain was not observed.

DISCUSSION: Pancreatic enzyme elevation reflects the systemic toxicity and multiorgan involvement following acute paraquat poisoning. CONCLUSIONS: Pancreatic injury was subtle and the elevation of pancreatic enzymes in survivors is clinically benign.

Gil HW, Yang JO, Lee EY, Hong SY.
Department of Internal Medicine, Cheonan Hospital, Soonchunhyang University, Cheonan, Republic of Korea

Amylase and lipase measurements in paediatric patients with traumatic pancreatic injuries.

noreply@blogger.com (Diagnostic Research) — Wed, 20 May 2009 01:10:00 +0000

Department of Paediatrics, University of Hawaii John A. Burns School of Medicine, Honolulu, HI 96826, United States. WMatsuno@Creighton.edu

INTRODUCTION: Pancreatic injuries occur in up to 10% of paediatric patients who suffer blunt trauma. Initial amylase and lipase measurements have not been helpful as a screening tool to detect pancreatic injuries. However, one primarily adult study suggests that a delayed measurement may be useful. MATERIALS AND METHODS: A retrospective chart review was conducted of patients admitted to a Level I paediatric trauma centre from April 1996 to November 2006 with traumatic pancreatic injuries.

RESULTS: The trauma database identified 51 patients with traumatic pancreatic injuries. Inclusion and exclusion criteria were met by 26 patients. Patients with initial amylase and lipase levels measured greater than 2h post-injury were more consistently elevated compared to those patients who had levels measured at 2h or less post-injury. There was a significant association between time of measurement and an increased amylase level (p=0.012). No significant association was found for lipase measurements (p=0.178).

DISCUSSION AND CONCLUSIONS: In children with blunt pancreatic injury, elevated serum amylase levels were seen in a significantly higher percentage of patients with initial measurements at greater than 2h post-injury compared to those measured at 2h or less. Lipase measurements demonstrated a similar trend. Delayed amylase and lipase measurements may be helpful to detect pancreatic injuries, but further study is needed.

The effects of a new human leukocyte elastase inhibitor (recombinant guamerin) on cerulein-induced pancreatitis in rats

noreply@blogger.com (Diagnostic Research) — Thu, 17 Jul 2008 21:12:00 +0000

Background
Pancreatic and neutrophil elastase can aggravate or induce acute pancreatitis. Although increased elastase levels in the plasma of pancreatitis patients and animal models have been reported, the mechanism by which elastase is involved in the pathogenesis of acute pancreatitis has not yet been elucidated. We aimed to investigate the effects and the possible mechanism of a new human leukocyte elastase inhibitor (recombinant guamerin) in the treatment of cerulein-induced acute pancreatitis in rats.

Methods
Fifty Sprague–Dawley rats were divided into three groups: a saline-infused control group (I), a cerulein-induced acute pancreatitis group (II), and a cerulein plus guamerin infusion group (III). Guamerin (1–2 μmol/kg/h) was infused continuously in group III. The severity of pancreatitis was determined biochemically, histologically, and by cytokine changes between groups I, II and III.

Results
Significant differences in serum amylase , lipase , and pancreatic wet weight were observed in each group, respectively (group I; 2346.2 IU/L, 9.9 IU/L, 1.4 ± 0.3 g, group II; 13,596.8 IU/L, 7439.4 IU/L, 2.2 ± 0.5 g, group III; 9443.2 IU/L, 4516.3 IU/L, 1.7 ± 0.6 g). Serum IL-6 and TNF- [AU1]level peaked 1–4 h and 1–2 h. After the induction of pancreatitis, IL-6 and TNF- levels were decreased in group III than group II, (group I; 13.1/4.0 pg/mL, group II; 198.5/63.2 pg/mL, group III; 102.1/13.1 pg/mL), but no significant difference in IL-1β was observed. Histologic gradings and severity, such as vacuolization, inflammation, lobular disarray, and edema of the pancreas, were significantly lower in the cerulein plus guamerin infusion group III.

Conclusions
Recombinant guamerin, a new human leukocyte elastase inhibitor, may decrease the severity of pancreatitis and diminish pancreatic acinar cell injury by inhibition of neutrophilic infiltration and cytokine activation in the initial stage of cerulein-induced acute pancreatitis in rats.

ARTICLE

Enzymatic preparation of chitooligosaccharides by commercial lipase

noreply@blogger.com (Diagnostic Research) — Mon, 30 Jun 2008 21:19:00 +0000

The effect of a commercial lipase on chitosan degradation was investigated. When four chitosans with various degrees of deacetylation were used as substrates, the lipase showed higher optimal pH toward chitosan with higher DD (degree of deacetylation). The optimal temperature of the lipase was 55 °C for all chitosans. The enzyme exhibited higher activity to chitosans which were 82.8% and 73.2% deacetylated. Kinetics experiments show that chitosans with DD of 82.8% and 73.2% which resulted in lower Km values had stronger affinity for the lipase. The chitosan hydrolysis carried out at 37 °C produced larger quantity of COS (chitooligosaccharides) than that at 55 °C when the reaction time was longer than 6 h, and COS yield of 24 h hydrolysis at 37 °C was 93.8%. Products analysis results demonstrate that the enzyme produced glucosamine and chitooligosaccharides with DP (degree of polymerization) of 2–6 and above, and it acted on chitosan in both exo- and endo-hydrolytic manner.

Dong-Xia Leea, Wen-Shui Xiaa, b, , and Jia-Li Zhang

ARTICLE

Bile-salt stimulated lipase in human milk binds DC-SIGN and inhibits HIV-1 transmission

noreply@blogger.com (Diagnostic Research) — Mon, 30 Jun 2008 21:10:00 +0000

Background
Approximately 20% of HIV-1 infected breastfeeding mothers transmit virus to their infants. It has been hypothesized that dendritic cells expressing C-type lectins, such as DC-SIGN, play an important role in the establishment of infection with HIV-1 and several other pathogens.

Within our laboratory we have identified that Bile Salt Stimulated Lipase (BSSL) is able to bind to DC-SIGN and block HIV-1 transmission via dendritic cells. The C-terminal part of BSSL contains a highly polymorphic repeat section coded by exon 11 of the gene and is composed of an array of 11 amino acid repeats.

Materials and methods
We have studied a large number of human breast milk samples from HIV-1 negative mothers. The BSSL protein was analyzed by size fractionation and iso-electric focusing. We studied the genomic structure of the gene through PCR amplification and sequencing of the BSSL repeats for a group of selected mothers.

Results
Milk samples from a large number of different mothers (n=25) were identified that demonstrated variant levels of inhibition to viral transfer. We have studied specific BSSL genotypic as well as phenotypic properties in order to identify what provides for the large variation of milk binding DC-SIGN. The tested milk samples were divided into weak binding and strong binding groups based on their DC-SIGN binding capacity. When comparing the PCR results for the BSSL repeat number we identified a link between the number of repeat domains and inhibition, with the more repeats binding less efficiently. A selection of weak and strong binders with identical repeat numbers was also made. Sequencing of this selected group revealed a mutation in the repeat section of an extreme weak binder on an interesting position with regards to BSSL glycosylation. Further analysis at the proteomic level was performed with a higher molecular mass for BSSL in the weak binding group being identified. Analysis of the DIGE results showed a shift in pI of BSSL in the weak binding group for 3 out of 5 cases.

Conclusions
Our results demonstrate that multiple factors contribute to the differential binding of human milk to DC-SIGN. Variation in the DC-SIGN binding capacities of BSSL may provide for alterations in transmission patterns of pathogens or in altering the immune mediated responses mounted in children against milk-borne pathogens. Furthermore, understanding these differences in BSSL could aide in the development of new agents aimed at preventing pathogen transmission across a mucosal barrier.

Immobilized Lipase Candida sp. 99-125 Catalyzed Methanolysis of Glycerol Trioleate: Solvent Effect

noreply@blogger.com (Diagnostic Research) — Fri, 23 May 2008 21:48:00 +0000

The immobilized lipase Candida sp. 99-125 catalyzed methanolysis of glycerol trioleate was studied in twelve different solvents in order to deduce the solvent effect through an attempt to correlate the highest yield with such solvent properties as hydrophobicity (log P), dielectric constant (ε), and Hildebrand solubility parameter (δ). The results showed that the conversion of glycerol trioleate and yield of oleic acid methyl ester were quite dependent on the solvent. The catalyst lipase in various solvents also needed different optimum amount of water to keep its maximum activity, and generally this lipase in more hydrophobic solvents required more water. The correlation between the highest yield and log P value was found to be reasonable except deviation of data points of certain solvents, while no obvious correlation existed between the other two parameters, dielectric constant (ε) and Hildebrand solubility parameter (δ), and the enzyme activity. The study revealed that more hydrophobic solvents such as n-hexane or cyclohexane were more suitable solvents for Candida sp. 99-125 catalyzed transesterification of glycerol trioleate to oleic acid methyl ester.

Jike Lua, Kaili Niea, Fang Wanga and Tianwei Tan, a,
aBeijing Bioprocess Key Laboratory, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, PR China

Endothelial Lipase Is Increased In Vivo by Inflammation in Humans

noreply@blogger.com (Diagnostic Research) — Tue, 29 Jan 2008 20:40:00 +0000

BACKGROUND: -Endothelial lipase (EL) is a plasma lipase that we previously reported to be significantly correlated with all features of the metabolic syndrome in humans, including directly with measures of adiposity and inversely with high-density lipoprotein cholesterol levels.

We hypothesized that inflammation associated with obesity results in upregulation of EL. We determined the relationship between inflammatory markers and EL levels in a cohort of healthy persons recruited on the basis of family history of coronary disease.

Furthermore, we directly tested the hypothesis that plasma EL concentrations would increase with induction of an inflammatory state by low-dose endotoxin in humans. Methods and Results-High-sensitivity C-reactive protein , interleukin 6, soluble tumor necrosis factor receptor II, soluble intercellular adhesion molecule 1, leptin, and adiponectin were measured in plasma of 858 subjects.

Significant direct correlations (P<0.001 for all) were found between EL concentrations and high-sensitivity C-reactive protein (r=0.28), interleukin-6 (r=0.22), soluble tumor necrosis factor receptor II (r=0.22), soluble intercellular adhesion molecule 1 (r=0.24), and leptin (r=0.20). An inverse correlation was present with adiponectin (r=-0.15, P<0.001). Adiponectin inhibited the tumor necrosis factor-alpha-stimulated EL secretion from cultured human coronary endothelial cells in a dose-dependent manner.

Experimental low-dose endotoxemia in 20 subjects resulted in a 2.5-fold increase in EL concentrations 12 to 16 hours after injection, which correlated temporally with decreases in both total and high-density lipoprotein phospholipid. Conclusions-In humans, plasma inflammatory markers are directly correlated with plasma EL concentrations, and experimental endotoxemia significantly increases plasma EL concentrations, proving that EL is upregulated by inflammation in humans. This mechanism may partially explain the low high-density lipoprotein cholesterol levels seen in obesity and metabolic syndrome.

School of Nursing, Institute of Translational Medicine and Therapeutics, School of Medicine, and Cardiovascular Institute, University of Pennsylvania, Philadelphia

Circulation. 2008 Jan 22

New procedure for the measurement of pancreatic lipase

noreply@blogger.com (Diagnostic Research) — Thu, 20 Dec 2007 20:02:00 +0000

Abstract
Background: Definitive substrates for the measurement of pancreatic lipase activity in human serum have not been conclusively identified owing to poor aqueous solubility and nonspecific susceptibility of substrates with existing methods. Thus, it is still important to propose new substrates for robust lipase measurements.

Methods: Reaction conditions were studied for a lipase method using newly synthesized 2,3-dibutyrylthio-1-propyl oleate as the substrate and 5,5′-dithio-bis-(2-nitro-benzoic acid) as the chromogen.

Results: Optimum conditions, using colipase and Mg++ in aqueous hexamethyl phosphoric triamide medium at pH 9.2, were defined. The substrate was highly selective to pancreatic lipase . The reaction increased linearly with lipase concentrations up to 500 U/l. The reference interval of serum lipase concentrations was 21.5–65 U/l. Using the Passing–Bablok regression analysis , the present assay shows a slope of 0.414, an intercept of − 2.4 U/l, and r-value of 0.992 in the comparison with the chromogenic method using the 6-methylresorufin ester of 1-O,2-O-dilauryl-rac-glycero-3-glutaric acid as the substrate.

Conclusion: Because of the simple composition of the reagents, the proposed procedure may represent a significant advancement in the commercially available methods for pancreatic lipase determination.

Clinica Chimica Acta
Volume 383, Issues 1-2, August 2007, Pages 85-90
Magohei Yamada , Toshio Fujita

Human Lipase

noreply@blogger.com (Diagnostic Research) — Mon, 05 Nov 2007 23:49:00 +0000

Pancreatic lipase is an enzyme secreted from the pancreas that uses hydrolysis to break a part fat molecules. Bile salts secreted from the liver and stored in gallbladder are released into the duodenum where they coat fat droplets. Because the droplets are small, their surface area is greater, allowing the lipase to break apart the fat more effectively. The resulting monomers are then moved by way of peristalsis along the small intestine to be absorbed into the lymphatic system by a specialized vessel called a lacteal.

Pancreatic lipase is secreted into the duodenum through the duct system of the pancreas. Normally lipase concentration in serum is very low. Under extreme disruption of pancreatic function, such as pancreatitis or pancreatic adenocarcinoma, the pancreas may begin to autolyse and release pancreatic enzymes into serum. Thus, through measurement of serum concentration of pancreatic lipase, pancreatitis can be diagnosed.

A blood test for lipase is ordered, often along with an amylase test, to help diagnose and monitor acute pancreatitis (inflammation of the pancreas), chronic pancreatitis, and other disorders that involve the pancreas.
Lipase testing is also occasionally used in the diagnosis and follow-up of cystic fibrosis, celiac disease, and Crohn's disease.