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γ‐Thrombin‐induced phospholipase A 2 activation in rabbit platelets: Comparison with α‐thrombin
Author(s) -
Touqui Lhousseine,
Jandrot-Perrus Martine,
Vargaftig B.Boris
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)81142-1
Subject(s) - thrombin , platelet , chemistry , calcium , ionophore , platelet activation , arachidonic acid , endocrinology , platelet activating factor , intracellular , biophysics , medicine , phospholipase c , biochemistry , enzyme , biology , organic chemistry
γ‐Thrombin stimulated release of [ 3 H]arachidonic acid ([ 3 H]AA) accompanied by a significant production of PAF and lyso‐PAF by rabbit platelets. These responses, which reflect PLA 2 activation, were observed after a prolonged lag and to a lower extent when compared to those induced by α‐thrombin which evoked a much higher elevation in intracellular calcium. This elevation together with [ 3 H]AA release were markedly reduced by EDTA. However, addition of ionophore A23187 enhanced the release of [ 3 H]AA by γ‐thrombin to the levels similar to those of α‐thrombin. We conclude that γ‐thrombin is able to activate PLA 2 and suggest that calcium influx may be a limiting factor for this activation.