Factor VIII Light Chain Contains a Binding Site for Factor X That Contributes to the Catalytic Efficiency of Factor Xase

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The factor VIII C1 domain contributes to platelet binding.

Activated factor VIII (FVIIIa) forms a procoagulant complex with factor IXa on negatively charged membranes, including activated platelet surfaces. Membrane attachment involves the FVIII C2 domain; involvement of the adjacent C1 domain has not been established. Binding of recombinant FVIII C1C2 and C2 proteins to platelets was detected by flow cytometry using (1) anti-C2 monoclonal antibody ESH...

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von Willebrand factor is a cofactor for thrombin-catalyzed cleavage of the factor VIII light chain.

The proteolytic activation of highly purified, heterodimeric porcine factor VIII and factor VIII-von Willebrand factor complex by thrombin was compared at I 0.17, pH 7.0, 22 degrees C. During the activation of factor VIII, heavy-chain cleavage is necessary to activate the procoagulant function, whereas light-chain cleavage is required to dissociate factor VIII from von Willebrand factor. The ki...

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FACTOR V AND VIII INHIBITOR IN PATIENTS WITH COMBINED FACTOR V AND VIII DEFICIENCY

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Background: Factor VIII administration to hemophilia A patients results in an immune response (inhibitor formation) which significantly complicates the therapy. The present study was performed to determine the prevalence of inhibitor development in hemophilia A patients receiving recombinant factor VIII therapy. Materials and Methods: This was an observational descriptive study. Clotting fac...

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ژورنال

عنوان ژورنال: Biochemistry

سال: 2012

ISSN: 0006-2960,1520-4995

DOI: 10.1021/bi201731p