PMID: 2116341Aug 1, 1990Paper

Membrane-associated 41-kDa GTP-binding protein in collagen-induced platelet activation

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
G Walker, L Y Bourguignon

Abstract

Initially we established that the binding of collagen to human blood platelets stimulates both the rapid loss of PIP2 and the generation of inositol-4,5-bisphosphate (IP2) and inositol-1,4,5-triphosphate (IP3). These results indicate that the binding of collagen stimulates inositol phospholipid-specific phospholipase C during platelet activation. The fact that GTP or GTP-gamma-S augments, and pertussis toxin inhibits, collagen-induced IP3 formation suggests that a GTP-binding protein (or (or proteins) may be directly involved in the regulation of phospholipase C-mediated phosphoinositide turnover in human platelets. We have used several complementary techniques to isolate and characterize a platelet 41-kDa polypeptide (or polypeptides) that has a number of structural and functional similarities to the regulatory alpha i subunit of the GTP-binding proteins isolated from bovine brain. This 41-kDa polypeptide (or polypeptides) is found to be closely associated with at least four membrane glycoproteins (e.g., gp180, gp110, gp95, and gp75) in a 330-kDa complex that can be dissociated by treatment with high salt plus urea. Most important, we have demonstrated that antilymphoma 41-kDa (alpha i subunit of GTP-binding proteins) antibody...Continue Reading

Citations

Apr 22, 1991·International Journal of Cancer. Journal International Du Cancer·B R LesterL T Furcht
Sep 1, 2007·Arteriosclerosis, Thrombosis, and Vascular Biology·Suzanne J A KorporaalJan-Willem N Akkerman
May 10, 1991·Science·M I SimonN Gautam

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