Hydrolysis of triacylglycerol arachidonic and linoleic acid ester bonds by human pancreatic lipase and carboxyl ester lipase
(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.
(Less)
- author
- Chen, Q ; Sternby, B LU and Nilsson, A LU
- organization
- publishing date
- 1989-08-22
- type
- Contribution to journal
- 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}}, }