Abstract
The von Willebrand factor (vWF) is a plasma protein that mediates platelet adhesion and leukocyte recruitment to vascular injury sites and carries coagulation factor VIII, a building block of the intrinsic pathway of coagulation. The presence of ultra-large multimers of vWF in the bloodstream is associated with spontaneous thrombosis, whereas its deficiency leads to bleeding. In cardiovascular pathology, the progression of the heart valve disease results in vWF deficiency and cryptogenic gastrointestinal bleeding. The association between higher plasma levels of vWF and thrombotic complications of coronary artery disease was described. Of note, it is not the plasma levels that are crucial for vWF hemostatic activity, but vWF activation, triggered by a rise in shear rates. vWF becomes highly reactive with platelets upon unfolding into a stretched conformation, at shear rates above the critical value (more than 5000 s−1), which might occur at sites of arterial stenosis and injury. The activation of vWF and its counterbalance by ADAMTS-13, the vWF-cleaving protease, might contribute to complications of cardiovascular diseases. In this review, we discuss vWF involvement in complications of cardiovascular diseases and possible diagnostic and treatment approaches.
Highlights
The von Willebrand Factor is a large multimeric glycoprotein, present in blood plasma, endothelial cells, megakaryocytes, and platelets
Conclusions von Willebrand Factor (vWF) plays an important role in cardiovascular disease
Though abundant data show that the plasma levels of vWF are increased and ADAMTS-13 levels are decreased in CAD, especially in myocardial infarction (MI), this does not necessarily reflect a causal relationship between elevated plasma vWF and MI
Summary
The von Willebrand Factor (vWF) is a large multimeric glycoprotein, present in blood plasma, endothelial cells, megakaryocytes, and platelets It plays a major role in hemostasis, mediating platelet adhesion to vascular injury sites. It binds and protects coagulation factor VIII (FVIII) from degradation [1]. SShheeaarr rraattee--iinndduucceedd aaccttiivvaattiioonn ooff tthhee vvoonn WWilillelebbrraanndd ffaaccttoorraattththeessitieteooffaaththeerorosscclelerorotitcic nnaarrrorowwininggoof faavveesssesel.l. Unfolded by high shear rates, the vWF threads can self-associate and form long strands and web-like structures, further stimulating platelet adhesion [19]. Smaller vessels, Unfolded by high shear rates, the vWF threads can self-associate and form long strands and web-like structures, further stimulating platelet adhesion [19]. The ability of unfolded vWF to self-associate under high-shear rates was studied in vitro in endothelialized microvessels. A myocardial ischemia/reperfusion study in ADAMTS-13-knockout mice showed that infusion of recombinant ADAMTS-13 substantially reduced myocardial apoptosis, troponin-I release, and resulted in a 9-fold reduction in the number of neutrophils infiltrating the ischemic zone [32]
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