Glycosylation is a key posttranslational modification, known to occur on more than half of all secreted proteins in man. As such, the role of N- and O-linked glycan structures in modulating various aspects of protein biology is an area of much research. Given their prevalence, it is perhaps unsurprising that variations in glycan structures have been demonstrated to play critical roles in modulating protein function and have been implicated in the pathophysiology of human diseases. von Willebrand factor (VWF), a plasma glycoprotein that is essential for normal hemostasis, is heavily glycosylated, containing 13 N-linked and 10 O-linked glycans. Together, these carbohydrate chains account for 20% of VWF monomeric mass, and have been shown to modulate VWF structure, function, and half-life. In this review, we focus on the specific role played by O-linked glycans in modulating VWF biology. Specifically, VWF O-linked glycans have been shown to modulate tertiary protein structure, susceptibility to ADAMTS13 proteolysis, platelet tethering, and VWF circulatory half-life.

糖基化是一种关键的翻译后修饰，已知发生在人体一半以上的所有分泌蛋白上。因此，N 和 O 连接的聚糖结构在调节蛋白质生物学各个方面的作用是一个大量研究的领域。鉴于它们的普遍性，聚糖结构的变化已被证明在调节蛋白质功能中起关键作用并与人类疾病的病理生理学有关，这也许不足为奇。血管性血友病因子 (VWF) 是一种对正常止血至关重要的血浆糖蛋白，它是高度糖基化的，含有 13 个 N 连接和 10 个 O 连接的聚糖。这些碳水化合物链共占 VWF 单体质量的 20%，并且已被证明可以调节 VWF 的结构、功能和半衰期。在本次审查中，我们专注于 O 连接聚糖在调节 VWF 生物学中所起的特定作用。具体而言，VWF O-连接聚糖已被证明可调节三级蛋白质结构、对 ADAMTS13 蛋白水解的敏感性、血小板束缚和 VWF 循环半衰期。