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Effect of pancreatic phospholipase A2 and gastric lipase on the action of pancreatic carboxyl ester lipase against lipid substrates in vitro

Lindstrom, Mats B; Persson, Johan LU ; Thurn, Lars and Borgström, Bengt LU (1991) In Biochimica et Biophysica Acta 1084(2). p.194-197
Abstract
Preincubation of a triolein/phospholipid/cholesteryl oleate-emulsion in vitro with either pancreatic phospholipase A2 (PLA2) or gastric lipase (GL) resulted in hydrolysis (measured by pH-stat-titration) of cholesteryl [3H]oleate only after human pancreatic carboxyl ester lipase (CEL) was added to the system. No appreciable hydrolysis was observed when CEL was added alone. Consequently, a concerted action either of PLA2 and CEL or of GL and CEL made the substrate cholesteryl oleate available for hydrolysis by CEL. This was the case when cholesteryl oleate was solubilised in a phospholipid-stabilised triglyceride emulsion, which is the physico-chemical form in which the major part of dietary cholesteryl esters are presented to the... (More)
Preincubation of a triolein/phospholipid/cholesteryl oleate-emulsion in vitro with either pancreatic phospholipase A2 (PLA2) or gastric lipase (GL) resulted in hydrolysis (measured by pH-stat-titration) of cholesteryl [3H]oleate only after human pancreatic carboxyl ester lipase (CEL) was added to the system. No appreciable hydrolysis was observed when CEL was added alone. Consequently, a concerted action either of PLA2 and CEL or of GL and CEL made the substrate cholesteryl oleate available for hydrolysis by CEL. This was the case when cholesteryl oleate was solubilised in a phospholipid-stabilised triglyceride emulsion, which is the physico-chemical form in which the major part of dietary cholesteryl esters are presented to the gastro-intestinal tract of man. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Gastric lipase, Phospholipase A2, Hydrolysis, Carboxyl ester lipase
in
Biochimica et Biophysica Acta
volume
1084
issue
2
pages
194 - 197
publisher
Elsevier
external identifiers
  • pmid:1854805
  • scopus:0025783042
ISSN
0006-3002
DOI
10.1016/0005-2760(91)90220-C
language
English
LU publication?
yes
id
b4c85a1d-f5db-44e1-a54d-014d6a3ec2cb (old id 1106060)
date added to LUP
2008-08-01 09:21:08
date last changed
2017-05-14 04:20:06
@article{b4c85a1d-f5db-44e1-a54d-014d6a3ec2cb,
  abstract     = {Preincubation of a triolein/phospholipid/cholesteryl oleate-emulsion in vitro with either pancreatic phospholipase A2 (PLA2) or gastric lipase (GL) resulted in hydrolysis (measured by pH-stat-titration) of cholesteryl [3H]oleate only after human pancreatic carboxyl ester lipase (CEL) was added to the system. No appreciable hydrolysis was observed when CEL was added alone. Consequently, a concerted action either of PLA2 and CEL or of GL and CEL made the substrate cholesteryl oleate available for hydrolysis by CEL. This was the case when cholesteryl oleate was solubilised in a phospholipid-stabilised triglyceride emulsion, which is the physico-chemical form in which the major part of dietary cholesteryl esters are presented to the gastro-intestinal tract of man.},
  author       = {Lindstrom, Mats B and Persson, Johan and Thurn, Lars and Borgström, Bengt},
  issn         = {0006-3002},
  keyword      = {Gastric lipase,Phospholipase A2,Hydrolysis,Carboxyl ester lipase},
  language     = {eng},
  number       = {2},
  pages        = {194--197},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta},
  title        = {Effect of pancreatic phospholipase A2 and gastric lipase on the action of pancreatic carboxyl ester lipase against lipid substrates in vitro},
  url          = {http://dx.doi.org/10.1016/0005-2760(91)90220-C},
  volume       = {1084},
  year         = {1991},
}