Grossly abnormal proteolysis of von Willebrand factor (VWF) in a patient heterozygous for a gene deletion and mutation in the dimerization area of VWF

Thrombosis and Haemostasis

Volumn 84, Issue 4, 2000, Pages 729-730

  Castaman, G ^a   Eikenboom, J C J ^a   Lattuada, A ^a   Rodeghiero, F ^a  

^a SAN BORTOLO HOSPITAL   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; PEPTIDE FRAGMENT; TYROSINE; VON WILLEBRAND FACTOR;

ALLELE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DIMERIZATION; ENDOPLASMIC RETICULUM; FEMALE; GENE DELETION; GENE MUTATION; GENETIC SCREENING; GENOTYPE; HETEROZYGOTE; HOMOZYGOSITY; HUMAN; LETTER; MALE; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DEGRADATION; VON WILLEBRAND DISEASE;

EID: 0033789724     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1614098     Document Type: Letter

References (6)

1. Characterization of the genetic defects in type 1 and 3 von Willebrand disease patients of Italian origin
2. Defective dimerization of von Willebrand factor subunits due to a Cys → Arg mutation in type IID von Willebrand disease
3. Characterization of the von Willebrand factor gene (vWF) in von Willebrand disease type III patients from 24 families of Swedish and Finnish origin
4. Cysteine mutations of von Willebrand factor correlate with different types of von Willebrand disease
5. Subunit composition of plasma von Willebrand factor. Cleavage is present in normal individuals, increased in type IIA and IIB von Willebrand disease, but minimal in variants with aberrant structure of individuals oligomers (types IIC, IID, and IIE)
6. Heightened proteolysis of the von Willebrand factor subunit in patients with von Willebrand disease hemizygous or homozygous for the C2362F mutation