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The platelet cytoskeleton regulates the aggregation‐dependent synthesis of phosphatidylinositol 3,4‐bisphosphate induced by thrombin
Author(s) -
Torti Mauro,
Bertoni Alessandra,
Sinigaglia Fabiola,
Balduini Cesare,
Payrastre Bernard,
Plantavid Monique,
Chap Hugues,
Mauco Gerard
Publication year - 2000
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/s0014-5793(00)01100-5
Subject(s) - phosphatidylinositol , cytoskeleton , phosphatidic acid , thrombin , cytochalasin , cytochalasin d , wortmannin , microbiology and biotechnology , cytochalasin b , chemistry , actin cytoskeleton , platelet , actin , microfilament , biochemistry , thrombin receptor , concanavalin a , biophysics , biology , kinase , cell , in vitro , membrane , immunology , phospholipid
Pretreatment of intact platelets with cytochalasin D prevented actin polymerization and cytoskeleton reorganization induced by thrombin, but did not affect platelet aggregation. Under these conditions, synthesis of phosphatidylinositol 3,4‐bisphosphate (PtdIns(3,4)P 2 ) stimulated by thrombin was strongly inhibited, while production of phosphatidic acid was unaffected. The inhibitory effect of cytochalasin D was not observed when platelet aggregation was prevented by the RGDS peptide. We also found that cytochalasin D did not affect PtdIns(3,4)P 2 synthesis induced by concanavalin A (ConA), which is known to occur through an aggregation‐independent mechanism. Moreover, thrombin, but not ConA, induced the translocation of phosphatidylinositol 3‐kinase to the cytoskeleton. This process was equally inhibited by both the RGDS peptide and cytochalasin D. These results demonstrate that the cytoskeleton represents a functional link between thrombin‐induced aggregation and synthesis of PtdIns(3,4)P 2 .