The platelet cytoskeleton regulates the aggregation-dependent synthesis of phosphatidylinositol 3,4-bisphosphate induced by thrombin

Mauro Torti, Alessandra Bertoni, Fabiola Sinigaglia, Cesare Balduini, Bernard Payrastre, Monique Plantavid, Hugues Chap, Gerard Mauco

Research output: Contribution to journalArticlepeer-review

Abstract

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)P2) 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)P2 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)P2. (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)355-358
Number of pages4
JournalFEBS Letters
Volume466
Issue number2-3
DOIs
Publication statusPublished - 28 Jan 2000
Externally publishedYes

Keywords

  • Cytochalasin D
  • Cytoskeleton
  • Phosphatidylinositol 3-kinase
  • Platelet

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