Nakato Hiroshi, Kimata Koji
Department of Molecular and Cellular Biology, and Arizona Cancer Center, University of Arizona, Tucson 85724, USA.
Biochim Biophys Acta. 2002 Dec 19;1573(3):312-8. doi: 10.1016/s0304-4165(02)00398-7.
Heparan sulfate chains have markedly heterogeneous structures in which distinct patterns of sulfation determine the binding specificity for ligand proteins. These "fine structures" of heparan sulfate are mainly produced by the regulated introduction of sulfate groups at the N-, 2-O-, 6-O-, and 3-O-positions of the sugar chain. Recent biochemical, histochemical, and genetic studies have demonstrated that different fine structures mediate distinct molecular recognition events to regulate a variety of cellular functions. In this review, we focus on the molecular basis of growth factor control by the sulfation status of heparan sulfate.
硫酸乙酰肝素链具有明显的异质性结构，其中不同的硫酸化模式决定了对配体蛋白的结合特异性。硫酸乙酰肝素的这些“精细结构”主要是通过在糖链的N-、2-O-、6-O-和3-O-位有规律地引入硫酸基团而产生的。最近的生化、组织化学和遗传学研究表明，不同的精细结构介导不同的分子识别事件，以调节多种细胞功能。在这篇综述中，我们重点关注硫酸乙酰肝素硫酸化状态对生长因子控制的分子基础。
