ФАКТОР ВИЛЛЕБРАНДА В НОРМЕ И ПРИ ПАТОЛОГИИ

Von Willebrand factor (vWF), a key component of hemostasis, is synthesized in endothelial cells and megakaryocytes and released into the blood as high molecular weight multimeric glycoproteins weighing up to 20 million daltons. Blood plasma metalloprotease ADAMTS13 cleaves ultra-large vWF multimers to smaller multimeric and oligomeric molecules. Molecules vWF attach to sites of damage to the surface of arterioles and capillaries and unfold under conditions of shear stress. On the unfolded vWF molecule, regions interacting with receptors on the platelet membrane are exposed. After binding to the vWF filaments, platelets are activated; platelets circulating in the vessels are additionally attached to them, and as a result, thrombi are formed, microvessels are blocked, and bleeding stops. This review describes the history of the discovery of vWF, presents data on the mechanisms of vWF secretion and its structure, and characterizes the processes of vWF exchange in the body in normal and pathological conditions.