[Structure and function of the factor VIII/von Willebrand factor complex]

Z Gesamte Inn Med. 1990 Mar 1;45(3):65-8.
[Article in German]

Abstract

In the blood plasma factor VIII is bound to the von Willebrand factor. The primary structure of the two proteins were clarified by gene clonation. Factor VIII descends from a precursor protein with 2,351 amino acids by splitting of 19 amino acid residues and is activated by partial proteolysis. In the blood coagulation factor VIII acts as co-factor for the activation of factor X by factor IX in the presence of phospholipids and Ca++ within the intrinsic coagulation system. The formation of the von Willebrand factor takes place by splitting of 22 and 741 amino acid residues, respectively, from pre-pro-von Willebrand factor via pro-von Willebrand factor. The subunits of the von Willebrand factor consist od 2,050 amino acid residues. In the blood plasma the von Willebrand factor is existing as a mixture of multimeres. Receptors of the von Willebrand factor on the thrombocytic membrane are the glycoproteins GPIb and GPIIb/GPIIIa, by means of which the adhesion of thrombocytes at the subendoethelium of the vascular wall and the aggregation of thrombocytes are mediated.

Publication types

  • English Abstract
  • Review

MeSH terms

  • Amino Acids / metabolism
  • Cloning, Molecular
  • Factor VIII / physiology*
  • Humans
  • Peptides / metabolism
  • Platelet Membrane Glycoproteins*
  • Receptors, Cell Surface / physiology*
  • von Willebrand Factor / physiology*

Substances

  • Amino Acids
  • Peptides
  • Platelet Membrane Glycoproteins
  • Receptors, Cell Surface
  • von Willebrand Factor
  • von Willebrand factor receptor
  • Factor VIII