Key result
The vWF A1 domain mediates critical platelet GPIbα interactions driving both hemostasis and pathological thrombosis.
This review provides an overview of the structural features of the von Willebrand factor A1 domain and its critical role in platelet adhesion and thrombus formation.
Highlights vWF A1-GPIbα as a potential antithrombotic target; leaves open efficacy and safety of selective inhibitors in trials.
The role of von Willebrand factor (VWF) in blocking hemorrhage is centered on its ability to act as a bridging adhesive molecule between platelets and components of the extracellular matrix or other platelets. In the course of chronic vascular diseases, moreover, the same properties of VWF may become the cause of pathological thrombus formation leading to arterial occlusion. There is convincing evidence that VWF functions involving interactions with platelets ultimately depend on binding to the membrane glycoprotein (GP) Ibalpha receptor mediated by the A1 domain. In this review, we present the current knowledge on the structural features of the VWF A1 domain that support its functions.
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Varughese et al. (2002) conducted a review in Hemorrhage and chronic vascular diseases. Von Willebrand Factor A1 Domain was evaluated. The von Willebrand factor A1 domain mediates critical interactions with the platelet glycoprotein Ibalpha receptor, supporting both physiological hemostasis and pathological thrombus formation.
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