Cleavage of von Willebrand Factor by Granzyme M Destroys Its Factor VIII Binding Capacity
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منابع مشابه
Cleavage of von Willebrand Factor by Granzyme M Destroys Its Factor VIII Binding Capacity
Von Willebrand factor (VWF) is a pro-hemostatic multimeric plasma protein that promotes platelet aggregation and stabilizes coagulation factor VIII (FVIII) in plasma. The metalloproteinase ADAMTS13 regulates the platelet aggregation function of VWF via proteolysis. Severe deficiency of ADAMTS13 is associated with thrombotic thrombocytopenic purpura, but does not always correlate with its clinic...
متن کاملBinding of factor VIII to von willebrand factor is enabled by cleavage of the von Willebrand factor propeptide and enhanced by formation of disulfide-linked multimers.
von Willebrand factor (vWF) is a multimeric adhesive glycoprotein with one factor VIII binding site/subunit. Prior reports suggest that posttranslational modifications of vWF, including formation of N-terminal intersubunit disulfide bonds and subsequent cleavage of the propeptide, influence availability and/or affinity of factor VIII binding sites. We found that deletion of the vWF propeptide p...
متن کاملA monoclonal antibody to factor VIII inhibits von Willebrand factor binding and thrombin cleavage.
To study the interaction of human factor VIII (FVIII) with its various ligands, select regions of cDNA encoding FVIII light chain were cloned into the plasmid expression vector pET3B to overproduce FVIII protein fragments in the bacterium Escherichia coli. Partially purified FVIII protein fragments were used to produce monoclonal antibodies. One monoclonal antibody, 60-B, bound both an FVIII pr...
متن کاملFactor VIII/von Willebrand factor protein. Galactose a cryptic determinant of von Willebrand factor activity.
The normal Factor VIII/von Willebrand factor protein has the ability to agglutinate or aggregate normal platelets in the presence of ristocetin (von Willebrand factor activity). Removal of greater than 95% of the sialic acid from this protein by neuraminidase did not affect the von Willebrand factor or procoagulant activity. However, oxidation of the penultimate galactose of the asialo Factor V...
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...
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ژورنال
عنوان ژورنال: PLoS ONE
سال: 2011
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0024216