Monoclonal antibodies against human platelet membrane glycoprotein IIIa and collagen-induced platelet activation.

1989 ◽  
Vol 37 (2) ◽  
pp. 397-403 ◽  
Author(s):  
Hiroto KAWASHIMA ◽  
Atsushi TOMARU ◽  
Kazuo YAMAMOTO ◽  
Tsutomu TSUJI ◽  
Toshiaki OSAWA
Keyword(s):  
Monoclonal Antibodies ◽  
Platelet Activation ◽  
Human Platelet ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Platelet Membrane Glycoprotein ◽  
Glycoprotein Iiia

An additional HpaII polymorphism in exon 2 of the human platelet membrane glycoprotein IIIa gene

1994 ◽  
Vol 93 (3) ◽  
pp. 353-354 ◽  
Author(s):  
Bruno Perichon ◽  
Sylvie Clemenceau ◽  
Alain Romand ◽  
Jacques Elion ◽  
Cecile Kaplan ◽  
...  
Keyword(s):  
Human Platelet ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Exon 2 ◽  
Platelet Membrane Glycoprotein ◽  
Glycoprotein Iiia

Structure and function of the von Willebrand factor A1 domain: analysis with monoclonal antibodies reveals distinct binding sites involved in recognition of the platelet membrane glycoprotein Ib-IX-V complex and ristocetin-dependent activation

Blood ◽  
2000 ◽  
Vol 95 (1) ◽  
pp. 164-172 ◽  
Author(s):  
Mariagrazia De Luca ◽  
David A. Facey ◽  
Emmanuel J. Favaloro ◽  
Mark S. Hertzberg ◽  
James C. Whisstock ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Platelet Aggregation ◽  
Von Willebrand Factor ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Platelet Membrane Glycoprotein ◽  
And Function ◽  
A1 Domain ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Binding of the adhesive glycoprotein, von Willebrand factor (vWf), to the platelet membrane glycoprotein (GP) Ib-IX-V complex initiates platelet adhesion and aggregation at high shear stress in hemostasis and thrombosis. In this study, the GP Ib-IX-V binding site within the vWf A1 domain was analyzed using a panel of murine monoclonal antibodies raised against a 39/34-kd vWf fragment (Leu-480/Val-481–Gly-718) encompassing the A1 domain. One antibody, 6G1, strongly inhibited ristocetin-dependent vWf binding to platelets, but had no effect on botrocetin- or jaracetin-dependent binding, or asialo-vWf–dependent platelet aggregation. The 6G1 epitope was mapped to Glu-700–Asp-709, confirming the importance of this region for modulation of vWf by ristocetin. Like ristocetin, 6G1 activated the vWf A1 domain, because it enhanced binding of the 39/34-kd fragment to platelets. In contrast, 5D2 and CR1 completely inhibited asialo-vWf–induced platelet aggregation and ristocetin-induced vWf binding to GP Ib-IX-V. However, only 5D2 blocked botrocetin- and jaracetin-induced vWf binding to platelets and binding of vWf to botrocetin- and jaracetin-coated beads. Epitopes for 5D2 and CR1 were conformationally dependent, but not congruent. Other antibodies mapped to epitopes within the A1 domain (CR2 and CR15, Leu-494–Leu-512; CR2, Phe-536–Ala-554; CR3, Arg-578–Glu-596; CR11 and CR15, Ala-564–Ser-582) were not functional, identifying regions of the vWf A1 domain not directly involved in vWf-GP Ib-IX-V interaction. The combined results provide evidence that the proline-rich sequence Glu-700–Asp-709 constitutes a regulatory site for ristocetin, and that ristocetin and botrocetin induce, at least in part, separate receptor-recognition sites on vWf. (Blood. 2000;95:164-172)

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