Mechanisms involved in platelet activation induced by a monoclonal antibodye anti glycoprotein IIb–IIIa: Inositol phosphate production is not the primary event

Bachelot, C; Sulpice, Jean Claude; Giraud, Françoise; Rendu, Francine

doi:10.1016/0898-6568(91)90030-x

Cited by 11 publications

(12 citation statements)

References 27 publications

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“…Most tyrosine proteins are phosphorylated during platelet activation induced by physiological agonists such as thrombin and collagen [2][3][4], as well as by thapsgargin [5,6], or the monoclonal antibody P256 directed against the integrin C~Hb133, the receptor for fibrinogen also named glycoprotein IIb-IIIa [7]. Among the tyrosine phosphorylated proteins described in platelets, some have been detected in cellular contact regions and are related to platelet aggregation such as the focal adhesion kinase FAK [8].…”

Section: ~ Introductionmentioning

confidence: 99%

Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c‐Src in human platelets

et al. 1996

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Protein tyrosine phosphatase 1C (PTP1C), highly expressed in hematopoietic cells, is a soluble protein tyrosine phosphatase containing two Src homology 2 (SH2) domains at the N-terminns and two putative sites of tyrosine phosphorylation at the C-terminus. This paper reports that PTP1C and c-Src could be coimmunoprecipitated during thrombin-induced platelet activation. Moreover, association between the two signalling proteins occurred only after PTP1C had been tyrosine phosphorylated. In in vitro experiments, PTPIC bound to the SH2 domain of c-Src, suggesting that association between tyrosine phosphorylated PTP1C and c-Src was mediated by the SH2 domain of c-Src. Finally, in resting platelets, PTP1C was mainly found in the Nonidet P-40 soluble fraction whereas following thrombin-induced activation, around 17% of PTP1C was associated with the insoluble fraction.

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Section: ~ Introductionmentioning

confidence: 99%

Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c‐Src in human platelets

et al. 1996

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“…Notable among the former was a monoclonal antibody (mAb) specific for GPIIb-IIIa, which was shown to activate platelets (Bachelot et al, 1990;Stuttle et al, 1991). Whereas the antibody induced full platelet activation, the F(ab')2 fragments induced only weak aggregation, without activation of phospholipase C or granule release (Bachelot et al, 1991). Therefore this mAb represented a good tool to the specific study of 'post-occupancy events' which occur after ligand binding to GPIIb-IIIa (Ginsberg et al, 1990;Phillips et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Functional implications of tyrosine protein phosphorylation in platelets. Simultaneous studies with different agonists and inhibitors

Bachelot

Cano

Grelac

et al. 1992

Biochemical Journal

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During activation of platelets by agonists, a number of proteins become phosphorylated at tyrosine residues. Using immunoblotting with a monoclonal anti-phosphotyrosine antibody, we have compared the different phosphotyrosine-protein (PTP) profiles of platelets stimulated with thrombin, collagen, ADP, arachidonic acid, phorbol myristate acetate and P256, an anti-glycoprotein-IIb-IIIa (GPIIb-IIIa) monoclonal antibody (mAb). Only a few PTPs were observed in resting platelets, of molecular masses 130, 64, 56-60 and 36 kDa. After stimulation by different agonists these proteins were more intensely phosphorylated and additional PTPs appeared with molecular masses of 170, 150, 140, 120, 105/97 (doublet), 85, 80, 75 and 45 kDa. The kinetics of phosphorylation differed from one agonist to another, but no significant differences in the overall patterns were detected, except in presence of ADP and P256-F(ab')2, which induced only the additional tyrosine phosphorylation of the 64 kDa protein and to a lesser extent that of a 75 kDa protein. The use of various agonists and the inhibitors (staurosporine, ajoene and RGDS) permitted a better characterization of the relationship between the different steps of activation and phosphorylation on tyrosine residues. The studies suggest the following conclusions: (i) stimulation of tyrosine phosphorylation occurs after activation of protein kinase C; (ii) there is a relationship between ligand binding to GPIIb-IIIa and the tyrosine phosphorylation of the 64 kDa protein; and (iii) there is a close relationship between PTP formation and the intensity of platelet activation and aggregation.

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“…The results were not clear, as was the case for protein kinase C activation. Indeed, phosphatidylinositol (3,4)-bisphosphate production (Bachelot C, L Cantley, unpublished results) or pleckstrin phosphorylation 63 was not always observed in experiments when platelets aggre gated. Since these phospholipids are closely related to ty rosine kinase activity in other cells, it is tempting to corre late the two series of results and to question what is the functional role of GPIIb/IIIa in the specific tyrosine phos phorylation and in the D-3 phosphoinositide synthesis.…”

Section: Intracellular Events Induced By Receptor Occupancymentioning

confidence: 97%

Anti-GPIIb/IIIa Antibodies: Powerful Tools to Investigate Function and Regulation of an Integrin

Bachelot¹,

Rendu²,

Gulino³

1995

Semin Thromb Hemost

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Mechanisms involved in platelet activation induced by a monoclonal antibodye anti glycoprotein IIb–IIIa: Inositol phosphate production is not the primary event

Cited by 11 publications

References 27 publications

Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c‐Src in human platelets

Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c‐Src in human platelets

Functional implications of tyrosine protein phosphorylation in platelets. Simultaneous studies with different agonists and inhibitors

Anti-GPIIb/IIIa Antibodies: Powerful Tools to Investigate Function and Regulation of an Integrin

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