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A new L1446P mutation is responsible for impaired von Willebrand factor synthesis, structure, and function.
Casonato, Alessandra; Cattini, Maria Grazia; Soldera, Carmen; Marcato, Stefania; Sartorello, Francesca; Pontara, Elena; Pagnan, Antonio.
Afiliación
  • Casonato A; Department of Medical and Surgical Sciences, University of Padua Medical School, Padua, Italy. sandra.casonato@unipd.it
J Lab Clin Med ; 144(5): 254-9, 2004 Nov.
Article en En | MEDLINE | ID: mdl-15570243
We report on a new mutation (4337T-->C) in exon 28 of the von Willebrand factor (VWF) gene, resulting in a substitution of L with P at residue 1446 (L1446P) of pre-pro-VWF. The defect is transmitted as a dominant trait and induces a reduced VWF synthesis, an abnormal VWF multimer pattern and a deficient VWF-platelet glycoprotein Ib interaction. The proband had low plasma and platelet VWF antigen levels, a reduced VWF collagen-binding capacity, and a disproportionately low VWF ristocetin cofactor activity, associated with the absence of ristocetin-induced platelet aggregation. Multimer analysis showed that the smaller multimers were slightly low, whereas the larger ones were significantly reduced or absent, with a clear cutoff between the two patterns. Similar hemostatic findings were observed in the proband's sister and nephew. Desmopressin administration restored VWF levels to near normal, but this was not so for VWF ristocetin cofactor activity or ristocetin-induced platelet aggregation. VWF multimers improved after desmopressin, moreover, with the larger forms restored and the smaller ones still relatively more represented. Recombinant P1446 VWF synthesis was reduced at heterozygous level, and its multimer pattern was similar to that observed in plasma VWF. These findings confirm the role of L1446P mutation in determining the von Willebrand disease (VWD) phenotype observed in our patients. Given the lack of large and intermediate VWF multimers, and the fact that the VWF-platelet interaction defect appears to be partially independent of multimer pattern, the VWD associated with L1446P mutation may belong to the type 2A/2M VWD variant.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Factor de von Willebrand / Mutación Límite: Adult / Humans / Male Idioma: En Revista: J Lab Clin Med Año: 2004 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Factor de von Willebrand / Mutación Límite: Adult / Humans / Male Idioma: En Revista: J Lab Clin Med Año: 2004 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Estados Unidos