Gu Jianguo, Taniguchi Naoyuki
Department of Biochemistry, Osaka University Graduate School of Medicine, B1, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Glycoconj J. 2004;21(1-2):9-15. doi: 10.1023/B:GLYC.0000043741.47559.30.
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. This review summarizes effects of the posttranslational modification of N-glycans of alpha3beta1 and alpha5beta1 integrins on their association, activation and biological functions, by using biochemical and genetic approaches.
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，并将基质蛋白与细胞骨架相连。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，调节多种过程，如增殖、分化、凋亡和细胞迁移。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多种因素调节，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介导，如N - 乙酰葡糖胺基转移酶III、V和α1,6岩藻糖基转移酶等，它们催化糖苷键的形成。本综述通过生化和遗传学方法总结了α3β1和α5β1整合素的N - 聚糖翻译后修饰对其结合、激活和生物学功能的影响。
