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Phorbol ester stimulates PAF synthesis via the activation of protein kinase C in rat leukocytes
Author(s) -
Hayashi Masahiko,
Imai Yohsuke,
Ohishi Sachiko
Publication year - 1991
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536501
Subject(s) - staurosporine , protein kinase c , acetyltransferase , phorbol , platelet activating factor , protein kinase a , microbiology and biotechnology , protein kinase inhibitor , phospholipase a2 , biochemistry , chemistry , phospholipase a , biology , enzyme , endocrinology , acetylation , gene
When rat pleural mononuclear leukocytes were stimulated with 1 μM phorbol myristate acetate (PMA), platelet‐activating factor (PAF)‐like activity was detected in the supernatant and the cellular fractions of the incubation mixture, as measured by rabbit platelet aggregation. C 16 PAF activity peaked at 30 min in both fractions. Acetyltransferase activity in the microsomal fraction of the stimulated cells also increased rapidly and showed a peak at 10 min. A protein kinase C inhibitor, staurosporine, and an inhibitor of phospholipase A 2 , p ‐bromophenacylbromide, inhibited stimulated PAF formation in both fractions. Staurosporine also inhibited PMA induced acetyltransferase activity. The data suggest that PMA stimulates PAF synthesis by the remodeling pathway in rat pleural cells through activation of both phospholipase A 2 and acetyltransferase, and that the acetyltransferase, in turn, may be activated through activation of protein kinase C.