Human von Willebrand factor (VWF) (VWF)

Human von Willebrand factor (VWF) is a large, multimeric glycoprotein that plays a central role in blood coagulation and primary hemostasis [1, 7]. It is synthesized exclusively in endothelial cells and megakaryocytes, where it is stored in Weibel-Palade bodies and alpha-granules, respectively, before being released into the plasma as high-molecular-weight multimers [3, 14]. VWF serves two primary functions: it acts as a molecular bridge between subendothelial collagen and platelet glycoprotein Ib (GPIb) receptors at sites of vascular injury, and it serves as a protective carrier for coagulation Factor VIII, preventing its premature degradation [1, 9]. Quantitative or qualitative defects in VWF result in von Willebrand disease (VWD), the most common inherited bleeding disorder in humans [4, 6]. Conversely, abnormally high levels of VWF or the presence of ultra-large multimers—often due to a deficiency in the cleavage enzyme ADAMTS13—can lead to life-threatening thrombotic conditions such as thrombotic thrombocytopenic purpura (TTP) [7, 14]. Therapeutic interventions include VWF replacement therapies (recombinant or plasma-derived), agents that stimulate endogenous VWF release like desmopressin, and targeted inhibitors such as caplacizumab, which blocks the VWF-platelet interaction to treat TTP [1, 11, 12].

Other names

von Willebrand factorVWFF8VWFFactor VIII-related antigen

Inhibition of the VWF A1 domain to prevent platelet adhesion; Replacement of deficient or dysfunctional VWF protein; Stimulation of endogenous VWF release from endothelial cells.