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过去几年,对von Willebrand因子(vW-F)的结构和功能的了解取得了一些进展。该多聚体的糖蛋白有双重作用:调节血小板粘附、聚集和作为因子Ⅷ的血浆中载体。对vWF几个功能区性质的新发现业已导致对该分子与因子Ⅷ、肝素、血小板糖蛋白I_b和胶原相互作用的识别。目前,已克隆出vWF,并测定了其一级氨基酸顺序,正更为详尽地了解其复杂的结构和多种功能,本文综述近年来有关vWF和vW病的研究进展。
In the past few years, some progress has been made in understanding the structure and function of von Willebrand factor (vW-F). The multimeric glycoprotein serves a dual role in regulating platelet adhesion, aggregation and as a plasma carrier of factor VIII. New discoveries of the nature of several functional domains of vWF have led to the identification of the molecule’s interaction with factor VIII, heparin, platelet glycoprotein I_b, and collagen. At present, vWF has been cloned and its primary amino acid sequence has been determined, and its complex structure and multiple functions are being studied in more detail. This review summarizes recent advances in the research of vWF and vW.