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Hydrolysis of triacylglycerol arachidonic and linoleic acid ester bonds by human pancreatic lipase and carboxyl ester lipase

Chen, Q ; Sternby, B LU and Nilsson, A LU (1989) In Biochimica et Biophysica Acta 1004(3). p.85-372
Abstract

The hydrolysis of polyenoic fatty acid ester bonds with pure human colipase-dependent lipase, with carboxyl ester lipase (CEL) and with these enzymes in combination was studied, using [3H]arachidonic- and [14C]linoleic acid-labelled rat chylomicrons as a model substrate. During the hydrolysis with colipase-dependent lipase, the amount of 3H appearing in 1,2-X-diacylglycerol (DG) markedly exceeded that of 14C. When CEL was added in addition this [3H]DG was efficiently hydrolyzed. CEL alone hydrolyzed the triacylglycerol (TG) at a low rate. The hydrolysis pattern with human duodenal content was similar to that seen with colipase-dependent lipase and CEL in combination. Increasing the concentration of taurodeoxycholate (TDC) and... (More)

The hydrolysis of polyenoic fatty acid ester bonds with pure human colipase-dependent lipase, with carboxyl ester lipase (CEL) and with these enzymes in combination was studied, using [3H]arachidonic- and [14C]linoleic acid-labelled rat chylomicrons as a model substrate. During the hydrolysis with colipase-dependent lipase, the amount of 3H appearing in 1,2-X-diacylglycerol (DG) markedly exceeded that of 14C. When CEL was added in addition this [3H]DG was efficiently hydrolyzed. CEL alone hydrolyzed the triacylglycerol (TG) at a low rate. The hydrolysis pattern with human duodenal content was similar to that seen with colipase-dependent lipase and CEL in combination. Increasing the concentration of taurodeoxycholate (TDC) and taurocholate (TC) or of TDC alone stimulated the hydrolysis of [3H]- and [14C]TG, but increased the accumulation of labelled DG that could act as substrate for CEL. It is suggested that very-long-chain polyenoic fatty acids of DG formed during the action of the colipase-dependent lipase on TG containing these fatty acids may be a physiological substrate for CEL.

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publication status
published
subject
keywords
Arachidonic Acid, Arachidonic Acids/metabolism, Bile Acids and Salts/pharmacology, Carboxylesterase, Carboxylic Ester Hydrolases/physiology, Chylomicrons/metabolism, Humans, Hydrolysis, In Vitro Techniques, Linoleic Acid, Linoleic Acids/metabolism, Lipase/physiology, Pancreas/enzymology, Time Factors, Triglycerides/metabolism
in
Biochimica et Biophysica Acta
volume
1004
issue
3
pages
14 pages
publisher
Elsevier
external identifiers
  • pmid:2503032
  • scopus:0024446393
ISSN
0006-3002
DOI
10.1016/0005-2760(89)90086-6
language
English
LU publication?
yes
id
0432d28f-65c6-49b0-bb64-f379d5273d3b
date added to LUP
2019-09-19 14:54:46
date last changed
2024-01-01 20:52:59
@article{0432d28f-65c6-49b0-bb64-f379d5273d3b,
  abstract     = {{<p>The hydrolysis of polyenoic fatty acid ester bonds with pure human colipase-dependent lipase, with carboxyl ester lipase (CEL) and with these enzymes in combination was studied, using [3H]arachidonic- and [14C]linoleic acid-labelled rat chylomicrons as a model substrate. During the hydrolysis with colipase-dependent lipase, the amount of 3H appearing in 1,2-X-diacylglycerol (DG) markedly exceeded that of 14C. When CEL was added in addition this [3H]DG was efficiently hydrolyzed. CEL alone hydrolyzed the triacylglycerol (TG) at a low rate. The hydrolysis pattern with human duodenal content was similar to that seen with colipase-dependent lipase and CEL in combination. Increasing the concentration of taurodeoxycholate (TDC) and taurocholate (TC) or of TDC alone stimulated the hydrolysis of [3H]- and [14C]TG, but increased the accumulation of labelled DG that could act as substrate for CEL. It is suggested that very-long-chain polyenoic fatty acids of DG formed during the action of the colipase-dependent lipase on TG containing these fatty acids may be a physiological substrate for CEL.</p>}},
  author       = {{Chen, Q and Sternby, B and Nilsson, A}},
  issn         = {{0006-3002}},
  keywords     = {{Arachidonic Acid; Arachidonic Acids/metabolism; Bile Acids and Salts/pharmacology; Carboxylesterase; Carboxylic Ester Hydrolases/physiology; Chylomicrons/metabolism; Humans; Hydrolysis; In Vitro Techniques; Linoleic Acid; Linoleic Acids/metabolism; Lipase/physiology; Pancreas/enzymology; Time Factors; Triglycerides/metabolism}},
  language     = {{eng}},
  month        = {{08}},
  number       = {{3}},
  pages        = {{85--372}},
  publisher    = {{Elsevier}},
  series       = {{Biochimica et Biophysica Acta}},
  title        = {{Hydrolysis of triacylglycerol arachidonic and linoleic acid ester bonds by human pancreatic lipase and carboxyl ester lipase}},
  url          = {{http://dx.doi.org/10.1016/0005-2760(89)90086-6}},
  doi          = {{10.1016/0005-2760(89)90086-6}},
  volume       = {{1004}},
  year         = {{1989}},
}