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The physical spacing between the von Willebrand factor D'D3 and A1 domains regulates platelet adhesion in vitro and in vivo

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Essentials The role of von Willebrand factor (VWF) domains in regulating platelet adhesion was studied in vivo. Multimeric VWF with spacers at the N‐ and C‐terminus of VWF‐A1 were systematically… Click to show full abstract

Essentials The role of von Willebrand factor (VWF) domains in regulating platelet adhesion was studied in vivo. Multimeric VWF with spacers at the N‐ and C‐terminus of VWF‐A1 were systematically tested. N‐terminal modified VWF avidly bound platelet GpIbα, causing VWD Type2B like phenotype in mice. Novel anti‐D'D3 mAbs suggest that changes at the D'D3‐A1 interface may be biologically relevant.

Keywords: platelet adhesion; von willebrand; willebrand factor

Journal Title: Journal of Thrombosis and Haemostasis
Year Published: 2018

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