Proteolytic inactivation of human factor VIII procoagulant protein by activated human protein C and its analogy with factor V.

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Fulcher CA, Gardiner JE, Griffin JH, Zimmerman TS

Proteolytic inactivation of human factor VIII procoagulant protein by activated human protein C and its analogy with factor V.

Blood. 1984 Feb;63(2):486-9.

PubMed ID

6419799 [ View in PubMed

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Abstract

Purified human factor VIII procoagulant protein (VIII:C) was treated with purified human activated protein C (APC) and the loss of VIII:C activity correlated with proteolysis of the VIII:C polypeptides. APC proteolyzed all VIII:C polypeptides with mol wt = 92,000 or greater, but not the doublet at mol wt = 79-80,000. These results and our previous thrombin activation studies of purified VIII:C, are analogous with similar studies of factor V and form the basis for the following hypothesis: activated VIII:C consists of heavy and light chain polypeptides [mol wt = 92,000 and mol wt = 79-80,000 (or 71-72,000), respectively] which are similar in Mr to the heavy and light chains of activated factor V. Thrombin activates VIII:C and V by generating these polypeptide chains from larger precursors and APC inactivates both molecules by cleavage at a site located in the heavy chain region of activated VIII:C and V.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Drotrecogin alfa	Coagulation factor V	Protein	Humans	Yes	Inhibitor	Details
Drotrecogin alfa	Coagulation factor VIII	Protein	Humans	Yes	Inhibitor	Details