Enzymatic degradation of the factor-VIII-von-Willebrand protein: a unique tryptic fragment with ristocetin cofactor activity

Martin, SE; Marder, VJ; Francis, C.W.; Loftus, LS; Barlow, Grant H.

doi:10.1182/blood.v55.5.848.848

Cited by 50 publications

(7 citation statements)

References 31 publications

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“…The domain interacting with GPIb was found on a 116 kd tryptic fragment of vWF. After reduction a specific 53-55 kd doublet was recognized by a Mab inhibiting binding of vWF 63,73 to GPIb. 63 This doublet also interacted with platelets in the presence of ristocetin.…”

Section: Structure-function Relationship Of Vwfmentioning

confidence: 99%

Role of von Willebrand Factor in the Vessel Wall

Groot¹,

Sixma²

1987

Semin Thromb Hemost

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Section: Structure-function Relationship Of Vwfmentioning

confidence: 99%

Role of von Willebrand Factor in the Vessel Wall

Groot¹,

Sixma²

1987

Semin Thromb Hemost

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“…The hypothesis that PAF (or RCF) activity is only associated with the most polymerized forms of factor VIII is apparently contradicted, however, by some of the observations of Guisasola et al (26) and of Martin et al (27). They reported that proteolytic fragments of human factor VIII exist which have ristocetin cofactor activity, even though they are of low molecular weight.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Form of Bovine Factor VIII Which Does Not Aggregate Human Platelets

Kirby

1981

Thromb Haemost

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SummaryFractionation of partially purified bovine factor VIII on tricalcium citrate columns produces a material which contains high levels of factor VIII procoagulant activity and factor VIII- related antigen, but does not aggregate human platelets. The procoagulant activity can be blocked by human inhibitors of factor VIII: C and by rabbit antibody to bovine factor VIII. Its activity can be increased by thrombin modification. The apparent molecular weight of this form of factor VIII is significantly lower than that of the forms of factor VIII which contain platelet aggregating activity, and it exhibits a higher mobility on agarose electrophoresis.

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“…Antisera: Preparation and characterization of antisera against human vW protein were as described previously (10,21). Some experiments used antiserum purchased from Calbiochem-Behring Corp. Monospecific antifibronectin antiserum was a kind gift from Dr. R. O. Hynes (Massachusetts Institute of Technology) (22).…”

Section: Methodsmentioning

confidence: 99%

Inhibition of disulfide bonding of von Willebrand protein by monensin results in small, functionally defective multimers.

Wagner¹,

Mayadas²,

Urban-Pickering³

et al. 1985

The Journal of Cell Biology

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The biosynthesis of von Willebrand protein by human endothelial cells was impaired by the presence of the carboxylic ionophore monensin. Several processing steps that have been localized to the Golgi apparatus were affected in a dose-dependent manner, including carbohydrate processing, dimer multimerization, and precursor cleavage. Since multimerization was more susceptible to the ionophore than was precursor cleavage, it appears that these processing steps are separate events. As expected, dimer formation, which occurs in the rough endoplasmic reticulum, was unaffected by monensin. Thus, at high concentrations of monensin, only dimer molecules were produced and secreted. The observed inhibition of multimer formation and precursor cleavage were not likely the result of incomplete carbohydrate processing, since inhibition of complex carbohydrate formation by swainsonine did not interfere with the other processing steps. Monensin also affected the capacity of endothelial cells to store von Willebrand protein, as the ratio of secreted to cell-associated protein increased dramatically in the presence of monensin, and the processed forms could not be found in the treated cells. The low molecular weight multimers produced in the presence of monensin did not incorporate in the endothelial cells' extracellular matrix nor did they bind to the matrix of human foreskin fibroblasts. In summary, the presence of monensin in human endothelial cell culture produced experimental conditions that mimic Type IIA von Willebrand disease, in that the cells synthesized and secreted only low molecular weight von Willebrand protein multimers, which were functionally defective.

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Enzymatic degradation of the factor-VIII-von-Willebrand protein: a unique tryptic fragment with ristocetin cofactor activity

Cited by 50 publications

References 31 publications

Role of von Willebrand Factor in the Vessel Wall

Role of von Willebrand Factor in the Vessel Wall

Characterization of a Form of Bovine Factor VIII Which Does Not Aggregate Human Platelets

Inhibition of disulfide bonding of von Willebrand protein by monensin results in small, functionally defective multimers.

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