Fressinaud E, Meyer D
Centre de Transfusion, Angers, France.
Blood Coagul Fibrinolysis. 1991 Apr;2(2):333-40. doi: 10.1097/00001721-199104000-00017.
von Willebrand factor (vWF) is a multimeric glycoprotein which has a dual role in haemostasis, functioning as carrier protein for Factor VIII and mediating platelet adhesion to exposed subendothelium (SE). vWF interacts with components of the SE such as collagen and heparin-like glycosaminoglycans as well as with two platelet membrane receptors: glycoprotein (GP) Ib and GPIIb/IIIa. These multiple binding functions explain its definition as an adhesive protein. vWF promotes platelet adhesion at the high shear rates which correspond to the rheologic conditions of the microcirculation or of narrowed arterial vessels. The role of the vWF-GPIb interaction in platelet adhesion is well known; that of the vWF-GPIIb/IIIa interaction has been more recently demonstrated through the use of monoclonal antibodies (MAbs) or synthetic peptides blocking vWF-binding to GPIIb/IIIa. In addition, perfusion studies in native, non-anticoagulated blood emphasize the concept that vWF is also essential for thrombus formation at high shear stress. Thus, vWF fragments, synthetic peptides or MAbs blocking the functional domains of vWF represent potential therapeutic strategies to prevent the development of thrombosis.
血管性血友病因子（vWF）是一种多聚体糖蛋白，在止血过程中发挥双重作用，它作为因子VIII的载体蛋白，并介导血小板黏附于暴露的内皮下层（SE）。vWF与SE的成分如胶原蛋白和类肝素糖胺聚糖相互作用，还与两种血小板膜受体相互作用：糖蛋白（GP）Ib和GPIIb/IIIa。这些多种结合功能解释了其作为黏附蛋白的定义。vWF在对应于微循环或狭窄动脉血管流变学条件的高剪切速率下促进血小板黏附。vWF - GPIb相互作用在血小板黏附中的作用是众所周知的；vWF - GPIIb/IIIa相互作用的作用最近通过使用阻断vWF与GPIIb/IIIa结合的单克隆抗体（MAb）或合成肽得以证实。此外，对天然未抗凝血液的灌注研究强调了vWF在高剪切应力下对血栓形成也至关重要的概念。因此，阻断vWF功能域的vWF片段、合成肽或MAb代表了预防血栓形成发展的潜在治疗策略。
