Inhibition of prostaglandin synthesis by lysolecithin

W. Thomas Shier

doi:10.1016/0006-291X(77)91416-4

Inhibition of prostaglandin synthesis by lysolecithin

W. Thomas Shier

Research output: Contribution to journal › Article › peer-review

29 Scopus citations

Abstract

Exogenous lysolecithin inhibits prostaglandin E₂ synthesis from arachidonic acid in bovine seminal vesicle microsomes at plausible physiological levels (lysolecithin-to-protein ratios ≥ 0.03 [w/w]) by inhibiting fatty acid cyclo-oxygenase activity. Structurally defined lysolecithins with varying fatty acid chain length exhibit varying effectiveness as inhibitors. Addition of equimolar quantities of free fatty acid lowers the lysolecithin concetration required for inhibition. Exogenous lysolecithin inhibits unstimulated and thrombin-stimulated prostaglandin E₂ synthesis from endogenous substrate in SVBalb/3T3 cells. Serum treatment of SVBalb/3T3 cells, which generates endogenous lysolecithin and free fatty acids, decreases the efficiency of conversion of free arachidonic acid to prostaglandins. These results suggest a possible role for the products of phospholipase A2 action in the regulation of prostaglandin synthesis.

Original language	English (US)
Pages (from-to)	1168-1174
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	78
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(77)91416-4
State	Published - Oct 24 1977
Externally published	Yes

Bibliographical note

Funding Information:
This work was supported by the Theodore Gildred Foundation Health Service Grants CA16123 and CA14195 from the National

Access

10.1016/0006-291X(77)91416-4

OpenUrl availability

Full text

Cite this

@article{19389e33759b4f6cb3e7ae370ae57d75,

title = "Inhibition of prostaglandin synthesis by lysolecithin",

abstract = "Exogenous lysolecithin inhibits prostaglandin E2 synthesis from arachidonic acid in bovine seminal vesicle microsomes at plausible physiological levels (lysolecithin-to-protein ratios ≥ 0.03 [w/w]) by inhibiting fatty acid cyclo-oxygenase activity. Structurally defined lysolecithins with varying fatty acid chain length exhibit varying effectiveness as inhibitors. Addition of equimolar quantities of free fatty acid lowers the lysolecithin concetration required for inhibition. Exogenous lysolecithin inhibits unstimulated and thrombin-stimulated prostaglandin E2 synthesis from endogenous substrate in SVBalb/3T3 cells. Serum treatment of SVBalb/3T3 cells, which generates endogenous lysolecithin and free fatty acids, decreases the efficiency of conversion of free arachidonic acid to prostaglandins. These results suggest a possible role for the products of phospholipase A2 action in the regulation of prostaglandin synthesis.",

author = "Shier, {W. Thomas}",

note = "Funding Information: This work was supported by the Theodore Gildred Foundation Health Service Grants CA16123 and CA14195 from the National",

year = "1977",

month = oct,

day = "24",

doi = "10.1016/0006-291X(77)91416-4",

language = "English (US)",

volume = "78",

pages = "1168--1174",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "4",

}

TY - JOUR

T1 - Inhibition of prostaglandin synthesis by lysolecithin

AU - Shier, W. Thomas

N1 - Funding Information: This work was supported by the Theodore Gildred Foundation Health Service Grants CA16123 and CA14195 from the National

PY - 1977/10/24

Y1 - 1977/10/24

N2 - Exogenous lysolecithin inhibits prostaglandin E2 synthesis from arachidonic acid in bovine seminal vesicle microsomes at plausible physiological levels (lysolecithin-to-protein ratios ≥ 0.03 [w/w]) by inhibiting fatty acid cyclo-oxygenase activity. Structurally defined lysolecithins with varying fatty acid chain length exhibit varying effectiveness as inhibitors. Addition of equimolar quantities of free fatty acid lowers the lysolecithin concetration required for inhibition. Exogenous lysolecithin inhibits unstimulated and thrombin-stimulated prostaglandin E2 synthesis from endogenous substrate in SVBalb/3T3 cells. Serum treatment of SVBalb/3T3 cells, which generates endogenous lysolecithin and free fatty acids, decreases the efficiency of conversion of free arachidonic acid to prostaglandins. These results suggest a possible role for the products of phospholipase A2 action in the regulation of prostaglandin synthesis.

AB - Exogenous lysolecithin inhibits prostaglandin E2 synthesis from arachidonic acid in bovine seminal vesicle microsomes at plausible physiological levels (lysolecithin-to-protein ratios ≥ 0.03 [w/w]) by inhibiting fatty acid cyclo-oxygenase activity. Structurally defined lysolecithins with varying fatty acid chain length exhibit varying effectiveness as inhibitors. Addition of equimolar quantities of free fatty acid lowers the lysolecithin concetration required for inhibition. Exogenous lysolecithin inhibits unstimulated and thrombin-stimulated prostaglandin E2 synthesis from endogenous substrate in SVBalb/3T3 cells. Serum treatment of SVBalb/3T3 cells, which generates endogenous lysolecithin and free fatty acids, decreases the efficiency of conversion of free arachidonic acid to prostaglandins. These results suggest a possible role for the products of phospholipase A2 action in the regulation of prostaglandin synthesis.

UR - http://www.scopus.com/inward/record.url?scp=0017662999&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017662999&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(77)91416-4

DO - 10.1016/0006-291X(77)91416-4

M3 - Article

C2 - 921769

AN - SCOPUS:0017662999

SN - 0006-291X

VL - 78

SP - 1168

EP - 1174

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

Inhibition of prostaglandin synthesis by lysolecithin

Abstract

Bibliographical note

Access

OpenUrl availability

Other files and links

Fingerprint

Cite this