Inhibition of prostaglandin synthesis by lysolecithin

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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 languageEnglish (US)
Pages (from-to)1168-1174
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Oct 24 1977
Externally publishedYes

Bibliographical note

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


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