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Leu 697-->Val mutation in mature von Willebrand factor is responsible
for type IIB von Willebrand disease
L Hilbert, C Gaucher, C de Romeuf, MH Horellou, T Vink and C Mazurier
Laboratoire de Recherche sur l'Hemostase, Centre Regional de Transfusion
Sanguine de Lille, France.
Type IIB von Willebrand disease is characterized by the selective loss of
high molecular weight von Willebrand factor (vWF) multimers from plasma and
enhanced platelet agglutination of platelet-rich-plasma in the presence of
low concentrations of ristocetin. We identified, in two related patients, a
C-->G transversion resulting in the substitution of Valine for Leucine
at position 697 of the mature subunit of vWF. We reproduced this mutation
in vWF cDNA and expressed the recombinant protein in Cos-7 cells. The
subunit composition and multimeric structure of mutated protein
(rvWFLeu697Val) were similar to the wild- type recombinant (WTrvWF).
Ristocetin-induced binding of rvWFLeu697Val to platelets was markedly
increased in the presence of low doses of ristocetin and slightly increased
with botrocetin as compared with that for WTrvWF, whereas collagen binding
was not affected by the mutation. These data show that the Leu 697-->Val
substitution is not a rare polymorphism but is responsible for the subtype
IIB characteristic abnormalities identified in the two affected patients;
however, it is not located in the area of vWF (amino acid 540 to amino acid
578) where most of the other type IIB mutations have already been reported.
Volume 83,
Issue 6,
pp. 1542-1550,
03/15/1994
Copyright © 1994 by The American Society of Hematology
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