Binding of the von Willebrand factor A1 domain to histone
Activation of the von Willebrand Factor (vWF) A1 domain is a critical factor in regulating the
interaction of vWF with its platelet membrane receptor, the glycoprotein (GP) Ib-IX-V
complex. This activation controls vWF-dependent platelet adhesion at high shear. The vWF-
GP Ib-IX-V interaction is induced in vivo by exposure of platelet-rich plasma to high shear
force, or by association of vWF with one or more unidentified components of the
subendothelial matrix. In vitro, soluble vWF is activated to bind to platelets by …
interaction of vWF with its platelet membrane receptor, the glycoprotein (GP) Ib-IX-V
complex. This activation controls vWF-dependent platelet adhesion at high shear. The vWF-
GP Ib-IX-V interaction is induced in vivo by exposure of platelet-rich plasma to high shear
force, or by association of vWF with one or more unidentified components of the
subendothelial matrix. In vitro, soluble vWF is activated to bind to platelets by …
