Synergistic release of arachidonic acid from platelets by activators of protein kinase C and Ca super(2+) ionophores. Evidence for the role of protein phosphorylation in the activation of phospholipase A sub(2) and independence from the Na super(+)/H super(+) exchanger

The protein kinase C activators phorbol myristate acetate (PMA), mezerein, oleoylacetylglycerol, and (-)-indolactam V, although without direct effect on arachidonic acid release, greatly enhance the release of platelet arachidonic acid caused by the Ca super(2+) ionophores A23187 and ionomycin. In c...

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Bibliographic Details
Published in:Biochemistry (Easton) 1989-01, Vol.28 (18), p.7356-7363
Main Authors: Halenda, S P, Banga, H S, Zavoico, G B, Lau, Lit-Fui, Feinstein, M B
Format: Article
Language:English
Subjects:
arachidonic acid
man
phosphorylation
platelets
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Summary:The protein kinase C activators phorbol myristate acetate (PMA), mezerein, oleoylacetylglycerol, and (-)-indolactam V, although without direct effect on arachidonic acid release, greatly enhance the release of platelet arachidonic acid caused by the Ca super(2+) ionophores A23187 and ionomycin. In contrast, 4 alpha -phorbol 12,13-didecanoate and (+)-indolactam V, which lack the ability to activate kinase C, do not potentiate arachidonate release. Release of arachidonic acid occurs without activation of phospholipase C and is therefore mediated by phospholipase A sub(2).
ISSN:0006-2960