tailieunhanh - Báo cáo khoa học: Dual P2Y12 receptor signaling in thrombin-stimulated platelets – involvement of phosphoinositide 3-kinase b but not c isoform in Ca2+ mobilization and procoagulant activity

During thrombus formation, thrombin, which is abundantly present at sites of vascular injury, activates platelets in part via autocrine-produced ADP. We investigated the signaling pathways by which thrombin and ADP in synergy induced platelet Ca 2+ elevation and procoagulant activity, and we monitored the consequences for the coagulation process. | ỊFEBS Journal Dual P2Y12 receptor signaling in thrombin-stimulated platelets - involvement of phosphoinositide 3-kinase b but not c isoform in Ca2 mobilization and procoagulant activity Paola E. J. van der Meijden1 Simone M. Schoenwaelder2 Marion A. H. Feijge1 Judith M. E. M. Cosemans1 Imke C. A. Munnix1 Reinhard Wetzker3 Regine Heller3 Shaun P. Jackson2 and Johan W. M. Heemskerk1 1 Department of Biochemistry Cardiovascular Research Institute Maastricht CARIM University of Maastricht the Netherlands 2 Australian Centre for Blood Diseases Monash University Alfred MedicalResearch Centre and Education Precinct AMREP Melbourne Australia 3 Institute of Molecular CellBiology University HospitalJena Germany Keywords ADP P2Y12 procoagulant activity thrombin Correspondence J. W. M. Heemskerk Department of Biochemistry University of Maastricht PO Box 616 6200 MD Maastricht the Netherlands Fax 31 43 3884159 Tel 31 43 3881671 E-mail Received 19 June 2007 revised 25 October 2007 accepted 26 November 2007 doi During thrombus formation thrombin which is abundantly present at sites of vascular injury activates platelets in part via autocrine-produced ADP. We investigated the signaling pathways by which thrombin and ADP in synergy induced platelet Ca2 elevation and procoagulant activity and we monitored the consequences for the coagulation process. Even at high thrombin concentration autocrine and added ADP enhanced and prolonged Ca2 depletion from internal stores via stimulation of the P2Y12 receptors. This P2Y12-dependent effect was mediated via two distinct signaling pathways. The first is enhanced Ca2 mobilization by the inositol 1 4 5-trisphosphate receptors due to inhibition of protein kinase A. The second pathway concerns prolonged activation of phosphoinositide 3-kinase PI3-K and phospholipase C. Experiments with phosphoinositide 3-kinase isoform-selective inhibitors and p110y deficient platelets demonstrated .

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