Document Detail


Concerted action of human carboxyl ester lipase and pancreatic lipase during lipid digestion in vitro: importance of the physicochemical state of the substrate.
MedLine Citation:
PMID:  3349096     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The pancreatic enzyme carboxyl ester lipase (CEL) has been shown to hydrolyse a large number of different esters, including triacylglycerols, cholesteryl esters and retinyl esters with an absolute requirement for bile salts. Some of the lipids that are substrates for CEL can also be hydrolysed by pancreatic lipase. In order to investigate the relative roles of human CEL and pancreatic lipase, the two enzymes were incubated on a pH-stat with isotope-labelled lipid substrate mixtures in physicochemical forms resembling the state of the dietary lipids in human intestinal contents. In the first set of experiments, cholesteryl oleate (CO) and retinyl palmitate (RP) were solubilised in an emulsion of triolein (TO) stabilised by egg phosphatidylcholine and bile salts. Lipase (always added together with its cofactor, colipase) hydrolysed TO, with monoolein and oleic acid as end-products, whereas CEL alone could not hydrolyse TO in the presence of phosphatidylcholine (PC). Lipase alone did not hydrolyse CO or RP, but CEL did hydrolyse these esters if lipase was present. Release of [3H]glycerol from labelled TO increased only slightly if CEL was added compared to lipase alone, suggesting that monoolein hydrolysis was slow under these conditions. In the second set of experiments, CO and RP were dissolved in bile salt/monoolein/oleic acid dispersions with varying bile salt concentrations. CEL hydrolysed CO and RP more rapidly in a system with a high bile salt concentration containing mixed micelles than in a system with a low bile salt concentration, where the lipids were dispersed in the form of mixed micellar and non-micellar aggregates; both types of aggregate have been reported to exist in human intestinal contents. In conclusion, these data suggest that the main function of CEL under physiological conditions is to hydrolyse cholesteryl and retinyl esters, provided that the triacylglycerol oil phase is hydrolysed by pancreatic lipase, which probably causes a transfer of the substrate lipids of CEL from the oil emulsion phase to an aqueous bile salt/lipolytic product phase. Depending on the bile salt/lipolytic product ratio, the substrate will reside in either micellar or non-micellar lipid aggregates, of which the micellar state is preferred by CEL.
Authors:
M B Lindström; B Sternby; B Borgström
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  959     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1988 Mar 
Date Detail:
Created Date:  1988-05-06     Completed Date:  1988-05-06     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  178-84     Citation Subset:  IM    
Affiliation:
Department of Medical and Physiological Chemistry, University of Lund, Sweden.
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MeSH Terms
Descriptor/Qualifier:
Bile Acids and Salts / metabolism
Carboxylic Ester Hydrolases / metabolism*
Chemistry, Physical
Cholesterol Esters / metabolism
Digestion
Emulsions
Humans
Lipid Metabolism*
Micelles
Pancreas / enzymology*
Phosphatidylcholines / metabolism
Physicochemical Phenomena
Triglycerides / metabolism
Vitamin A / analogs & derivatives,  metabolism
Chemical
Reg. No./Substance:
0/Bile Acids and Salts; 0/Cholesterol Esters; 0/Emulsions; 0/Micelles; 0/Phosphatidylcholines; 0/Triglycerides; 11103-57-4/Vitamin A; 79-81-2/retinol palmitate; EC 3.1.1.-/Carboxylic Ester Hydrolases

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