Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Hydrolysis of phosphatidylinositol by human panreatic phospholipase A2

Barros, H. ; Sternby, Berit LU and Nilsson, Åke LU (1990) In Scandinavian Journal of Gastroenterology 25(2). p.134-140
Abstract
Pure human pancreatic phospholipase A2 efficiently hydrolyzed the 2-ester bond of 14C-2-linoleoyl and 14C-2-arachidonyl phosphatidylinositol (PI). The rate of hydrolysis varied markedly with the bile salt (sodium taurocholate to sodium taurodeoxycholate, 3:4 mol/mol) concentration, the hydrolysis being decreased with increasing bile salt to PI ratio. The influence of bile salts was thus similar to that which has earlier been described for the hydrolysis of phosphatidylcholine (PC) with pig pancreatic phospholipase A2. When 2-3H-arachidonyl PC and 2-14C-arachidonyl PI were incorporated into a mixed substrate, PI was hydrolyzed even faster than PC, the hydrolysis of both phospholipids varying in the same manner with bile salt concentration.... (More)
Pure human pancreatic phospholipase A2 efficiently hydrolyzed the 2-ester bond of 14C-2-linoleoyl and 14C-2-arachidonyl phosphatidylinositol (PI). The rate of hydrolysis varied markedly with the bile salt (sodium taurocholate to sodium taurodeoxycholate, 3:4 mol/mol) concentration, the hydrolysis being decreased with increasing bile salt to PI ratio. The influence of bile salts was thus similar to that which has earlier been described for the hydrolysis of phosphatidylcholine (PC) with pig pancreatic phospholipase A2. When 2-3H-arachidonyl PC and 2-14C-arachidonyl PI were incorporated into a mixed substrate, PI was hydrolyzed even faster than PC, the hydrolysis of both phospholipids varying in the same manner with bile salt concentration. 2-14C-arachidonyl PI was also efficiently hydrolyzed by human duodenal content, although at a somewhat slower rate than 2-3H-arachidonyl PC. It is concluded that PI is a good substrate for human phospholipase A2. This minor but arachidonate-rich dietary phospholipid may thus be digested and absorbed by pathways similar to those of the major dietary and bile phospholipid, phosphatidylcholine. (Less)
Please use this url to cite or link to this publication:
author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Scandinavian Journal of Gastroenterology
volume
25
issue
2
pages
134 - 140
publisher
Taylor & Francis
external identifiers
  • pmid:2305210
  • scopus:0025338976
ISSN
1502-7708
DOI
10.3109/00365529009107934
language
English
LU publication?
yes
id
9351764d-c65c-417d-be0c-5ec43504e7d6
date added to LUP
2019-06-24 10:27:17
date last changed
2024-01-01 12:34:48
@article{9351764d-c65c-417d-be0c-5ec43504e7d6,
  abstract     = {{Pure human pancreatic phospholipase A2 efficiently hydrolyzed the 2-ester bond of 14C-2-linoleoyl and 14C-2-arachidonyl phosphatidylinositol (PI). The rate of hydrolysis varied markedly with the bile salt (sodium taurocholate to sodium taurodeoxycholate, 3:4 mol/mol) concentration, the hydrolysis being decreased with increasing bile salt to PI ratio. The influence of bile salts was thus similar to that which has earlier been described for the hydrolysis of phosphatidylcholine (PC) with pig pancreatic phospholipase A2. When 2-3H-arachidonyl PC and 2-14C-arachidonyl PI were incorporated into a mixed substrate, PI was hydrolyzed even faster than PC, the hydrolysis of both phospholipids varying in the same manner with bile salt concentration. 2-14C-arachidonyl PI was also efficiently hydrolyzed by human duodenal content, although at a somewhat slower rate than 2-3H-arachidonyl PC. It is concluded that PI is a good substrate for human phospholipase A2. This minor but arachidonate-rich dietary phospholipid may thus be digested and absorbed by pathways similar to those of the major dietary and bile phospholipid, phosphatidylcholine.}},
  author       = {{Barros, H. and Sternby, Berit and Nilsson, Åke}},
  issn         = {{1502-7708}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{134--140}},
  publisher    = {{Taylor & Francis}},
  series       = {{Scandinavian Journal of Gastroenterology}},
  title        = {{Hydrolysis of phosphatidylinositol by human panreatic phospholipase A2}},
  url          = {{http://dx.doi.org/10.3109/00365529009107934}},
  doi          = {{10.3109/00365529009107934}},
  volume       = {{25}},
  year         = {{1990}},
}