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Absent collagen binding in a VWF A3 domain mutant: utility of the VWF:CB in diagnosis of VWD

2010; Elsevier BV; Volume: 8; Issue: 6 Linguagem: Inglês

10.1111/j.1538-7836.2010.03869.x

1538-7933

Veronica H. Flood, Carol A. Lederman, J.S. WREN, Pamela A. Christopherson, Kenneth D. Friedman, Raymond Hoffmann, Robert R. Montgomery,

Blood Coagulation and Thrombosis Mechanisms

Von Willebrand factor (VWF) tethers platelets to injured subendothelium through binding sites for collagen and platelet glycoprotein Ib (GPIb). The collagen binding site has been localized to the VWF A1 and A3 domains [1]. This interaction is measured in vitro by the VWF collagen binding assay, or VWF:CB [2,3]. VWD guidelines recently published by the NHLBI suggest restricting use of the VWF:CB to subjects who have abnormal initial screening results with VWF antigen (VWF:Ag) and VWF ristocetin cofactor activity (VWF:RCo) [4].