Platelets have more than one binding site for von Willebrand factor.
نویسندگان
چکیده
منابع مشابه
Platelets have more than one binding site for von Willebrand factor.
The binding of 125I-von Willebrand factor (125I-vWF) to platelets stimulated by thrombin, ADP, and a combination of ADP + epinephrine (EPI) is specific, saturable, and reversible. Active platelet metabolism and divalent cations are required for binding induced by these stimuli, but not by ristocetin, suggesting the existence of different mechanisms involved in the vWF-platelet interaction. A mo...
متن کاملInhibition of platelet-von Willebrand factor binding to platelets by adhesion site peptides.
Synthetic peptides containing the adhesion site recognition sequences present on the A alpha and gamma chains of fibrinogen were studied for their effect on the binding of endogenous platelet-von Willebrand factor (vWF) and exogenous plasma-vWf to thrombin-stimulated platelets. In agreement with previously reported data, the tetrapeptide consisting of the RGDS sequence was a more potent inhibit...
متن کاملFactor Vill/von Willebrand Factor Binding to von Willebrand’s Disease Platelets
A form of von Willebrand’s disease has been described with enhanced ristocetin-induced platelet aggregation and anodal migration of the factor VIll/von Willebrand factor protein (type lIb). We studied two families with this form of von Willebrand s disease and macrothrombocytopenia. We have found that these platelets bind more of the normal and intermediate-sized multimers of the factor VIll/vo...
متن کاملFactor VIII/von Willebrand factor binding to von Willebrand's disease platelets.
A form of von Willebrand's disease has been described with enhanced ristocetin-induced platelet aggregation and anodal migration of the factor VIII/von Willebrand factor protein (type IIb). We studied two families with this form of von Willebrand's disease and macrothrombocytopenia. We have found that these platelets bind more of the normal and intermediate-sized multimers of the factor VIII/vo...
متن کاملComparative analysis of type 2b von Willebrand disease mutations: implications for the mechanism of von Willebrand factor binding to platelets.
von Willebrand factor (vWF) is a multimeric glycoprotein that forms an adhesive link following vascular injury between the vessel wall and its primary ligand on the platelet surface, glycoprotein Ib (GpIb). Type 2b von Willebrand disease (vWD) is a qualitative form of vWD resulting from enhanced binding of vWF to platelets. Molecular characterization of the vWF gene in patients with type 2b vWD...
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ژورنال
عنوان ژورنال: Journal of Clinical Investigation
سال: 1983
ISSN: 0021-9738
DOI: 10.1172/jci110946