TY - JOUR
T1 - The platelet cytoskeleton regulates the aggregation-dependent synthesis of phosphatidyl inositol 3,4 bisphosphate induced by thrombin
AU - Torti, M
AU - BERTONI, Alessandra
AU - SINIGAGLIA, Fabiola
AU - Balduini, C
AU - Payrastre, B
AU - Plantavid, M
AU - Chap, H
AU - Mauco, G.
N1 - Funding Information:
This work was supported by grants from the INSERM-CNR agreement (to G.M and C.B.), from Ministero dell’ Università e della Ricerca Scientifica e Tecnologica (MURST, PRIN 1997), and from CNR (target project biotechnology). We thank Marco Bellaviti (Department of Biochemistry, University of Pavia, Italy) for technical assistance in the preparation of the figures.
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
UR - https://iris.uniupo.it/handle/11579/31883
M3 - Article
SN - 0014-5793
VL - 466
SP - 355
EP - 358
JO - FEBS Letters
JF - FEBS Letters
ER -