Gu Jianguo
Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, Sendai, Japan.
Yakugaku Zasshi. 2007 Apr;127(4):571-8. doi: 10.1248/yakushi.127.571.
Integrins are cell surface transmembrane glycoproteins that function as adhesion receptors in cell-ECM interactions and link matrix proteins to the cytoskeleton. Integrins play an important role in cytoskeleton organization and in the transduction of intracellular signals, regulating various processes such as proliferation, differentiation, apoptosis, and cell migration. Although integrin-mediated adhesion is based on the binding of alpha and beta subunits to a defined peptide sequence, the strength of this binding is modulated by various factors including the status of glycosylation of integrin. Glycosylation reactions are catalyzed by the catalytic action of glycosyltransferases, such as N-acetylglucosaminyltransferase III, V and alpha1,6 fucosyltransferase, etc., which catalyze the formation of glycosidic bonds. In this talk we will briefly overview the N-glycan structures of integrins, such as alpha3beta1 and alpha5beta1, and their related functions arising from recent studies, which provide insight into some long-standing questions concerning N-glycosylation functions.
整合素是细胞表面跨膜糖蛋白，在细胞与细胞外基质（ECM）相互作用中作为黏附受体发挥作用，将基质蛋白与细胞骨架连接起来。整合素在细胞骨架组织以及细胞内信号转导中发挥重要作用，调节诸如增殖、分化、凋亡和细胞迁移等各种过程。尽管整合素介导的黏附基于α和β亚基与特定肽序列的结合，但这种结合的强度受到多种因素的调节，包括整合素的糖基化状态。糖基化反应由糖基转移酶的催化作用催化，如N-乙酰葡糖胺转移酶III、V和α1,6岩藻糖基转移酶等，它们催化糖苷键的形成。在本次讲座中，我们将简要概述整合素（如α3β1和α5β1）的N-聚糖结构及其近期研究产生的相关功能，这些研究为一些关于N-糖基化功能的长期问题提供了见解。
