Binding of pancreatic colipase to interfaces; effects of detergents

Borgström, Bengt

doi:10.1016/0014-5793(76)80931-3

Cited by 34 publications

(13 citation statements)

References 18 publications

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“…Clps encodes colipase that is secreted from the exocrine pancreas into the gastrointestinal tract [60]. Colipase may interact with pancreatic triglyceride lipase to facilitate the digestion of dietary fats.…”

Section: Discussionmentioning

confidence: 99%

Time-course microarray analysis for identifying candidate genes involved in obesity-associated pathological changes in the mouse colon

et al. 2016

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BackgroundObesity is known to increase the risk of colorectal cancer. However, mechanisms underlying the pathogenesis of obesity-induced colorectal cancer are not completely understood. The purposes of this study were to identify differentially expressed genes in the colon of mice with diet-induced obesity and to select candidate genes as early markers of obesity-associated abnormal cell growth in the colon.MethodsC57BL/6N mice were fed normal diet (11% fat energy) or high-fat diet (40% fat energy) and were euthanized at different time points. Genome-wide expression profiles of the colon were determined at 2, 4, 8, and 12 weeks. Cluster analysis was performed using expression data of genes showing log2 fold change of ≥1 or ≤−1 (twofold change), based on time-dependent expression patterns, followed by virtual network analysis.ResultsHigh-fat diet-fed mice showed significant increase in body weight and total visceral fat weight over 12 weeks. Time-course microarray analysis showed that 50, 47, 36, and 411 genes were differentially expressed at 2, 4, 8, and 12 weeks, respectively. Ten cluster profiles representing distinguishable patterns of genes differentially expressed over time were determined. Cluster 4, which consisted of genes showing the most significant alterations in expression in response to high-fat diet over 12 weeks, included Apoa4 (apolipoprotein A-IV), Ppap2b (phosphatidic acid phosphatase type 2B), Cel (carboxyl ester lipase), and Clps (colipase, pancreatic), which interacted strongly with surrounding genes associated with colorectal cancer or obesity.ConclusionsOur data indicate that Apoa4, Ppap2b, Cel, and Clps are candidate early marker genes associated with obesity-related pathological changes in the colon. Genome-wide analyses performed in the present study provide new insights on selecting novel genes that may be associated with the development of diseases of the colon.Electronic supplementary materialThe online version of this article (doi:10.1186/s12263-016-0547-x) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Time-course microarray analysis for identifying candidate genes involved in obesity-associated pathological changes in the mouse colon

et al. 2016

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“…In order to maintain full lipolytic activity in the presence of the physiological concentrations of bile salts, pancreatic lipases need a cofactor, the colipase [26,27]. Colipase has been found in the pancreatic juice of all mammals, avian, and in many lower vertebrates like dogfish (Squalus acanthius) [28,29].…”

Section: Discussionmentioning

confidence: 99%

Snail Hepatopancreatic Lipase: A New Member of Invertebrates Lipases' Group

Amara¹,

Fendri²,

Salem³

et al. 2009

Appl Biochem Biotechnol

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Higher animal's lipases are well characterized; however, much less is known about lipases from mollusks. A lipolytic activity was located in the land snail (Eobania vermiculata) digestive glands (hepatopancreas), from which a snail digestive lipase (SnDL) was purified. Pure SnDL has a molecular mass of 60 kDa; it does not present the interfacial activation phenomenon. It was found to be more active on short-chain triacylglycerols than on long-chain triacylglycerols. The NH2-terminal sequence of the SnDL shows 66% of identity with the 17 NH2-terminal amino acids of a putative lipase from sea urchin (Strongylocentrotus purpuratus). No sequence identity was found with known lipases. Interestingly, neither colipase nor bile salts were detected in the snail hepatopancreas. This suggests that colipase evolved in vertebrates simultaneously with the appearance of an exocrine pancreas and a true liver which produces bile salts. Altogether, these results suggest that SnDL is a member of a new group of digestive lipases belonging to invertebrates.

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“…Pancreatic colipase in the presence of bile salts has the same requirements for the quality of the interface and is hydrogen bonded to the lipase substrate interface. The interactions between colipase and the lipase substrate are less sensitive to bile salt concentration [4] and to salt and decrease at high pH values in the presence of bile salts [2] , possibly as an effect on the ionization of the amino groups in the protein which are engaged in the hydrogen bonding. As a consequence polar rather than hydrophobic interactions can be expected to be all important for the function of pancreatic lipase in the physiological situation, i.e., in the small intestinal contents.…”

Section: Discussionmentioning

confidence: 99%