[Von Willebrand's disease].

: Von Willebrand's disease (vWD), one of the most frequent hereditary bleeding disorders, is associated with a deficiency or a defective structure of von Willebrand factor (vWF). The defect is transmitted by autosomal inheritance. vWF is a plasma glycoprotein which mediates platelet adherence to the subendothelium of the injured blood vessel and is thus indispensable for primary hemostasis. vWF is composed of identical subunits linked together by disulfide bridges. Each subunit contains binding site(s) for factor VIII, collagen and platelets. The highly polymeric vWF factor is the largest known plasma protein. Functional activity is preferentially associated with the largest multimeric forms of vWF. Binding of vWF onto collagen fibrils activates its platelet binding sites, which are apparently not accessible in circulating vWF. Aggregation of washed fixed platelets in the presence of ristocetin or collagen is used for assessment of vWF's biological activity. Important additional information for the diagnosis of vWD is provided by the antigen assay and by electrophoretic analysis of the multimeric pattern of vWF. In type I vWD, all polymeric forms of vWF are reduced in the same proportion, while only the largest, i.e. the most active, multimers are deficient in type II vWD. The most severe type III vWD is characterized by an undetectable concentration of vWF. DDAVP corrects the prolonged bleeding time in patients with mild forms of vWD. Cryoprecipitate or "virus inactivated" factor VIII concentrates are employed for substitution therapy. Our results suggest that the newly introduced "virus inactivated" factor VIII concentrate from SRK is likewise suitable for this purpose.