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Epinephrine and the Ca 2+ ionophore A23187 synergistically induce platelet aggregation without protein kinase C activation
Author(s) -
Olbrich Christine,
Siess Wolfgang
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80144-9
Subject(s) - apyrase , chemistry , epinephrine , phosphatidic acid , protein kinase a , platelet , ionophore , myosin light chain kinase , phosphorylation , platelet activation , biochemistry , protein phosphorylation , medicine , endocrinology , enzyme , biology , phospholipid , membrane
Aspirin‐pretreated, 32 P‐prelabeled, washed human platelets resuspended in a buffer containing apyrase and 2% plasma were exposed to epinephrine and the Ca 2+ ionophore A23187. Epinephrine potentiated platelet aggregation (not secretion), the production of [ 32 P]phosphatidic acid and myosin light chain phosphorylation induced by A23187. No phosphorylation of the 40 kDa protein, the substrate of protein kinase C, was observed. We conclude that G 1 ‐protein activation evoked by epinephrine and Ca 2+ mobilization caused by A23187 represents a novel synergism for platelet aggregation and that protein kinase C activation, under these conditions is not needed for platelet aggregation.