Regulation of integrin functions by N-glycans
Regulation of integrin functions by N-glycans
复制标题
DOI：
10.1023/b:glyc.0000043741.47559.30
复制
发表时间：
2004-01-01
影响因子：
3
通讯作者：
Taniguchi, N
中科院分区：
文献类型：
--
作者：
Gu, JG;Taniguchi, N
整合素是细胞表面跨膜糖蛋白，其在细胞-ECM相互作用中作为粘附受体起作用并将基质蛋白连接到细胞骨架。整合素在细胞骨架组织和细胞内信号转导中起重要作用，调节各种过程，如增殖、分化、凋亡和细胞迁移。虽然整联蛋白介导的粘附是基于α和亚基与确定的肽序列的结合，但这种结合的强度受多种因素调节，包括整联蛋白的糖基化状态。糖基化反应通过糖基转移酶如N-乙酰葡糖胺基转移酶III、V和α 1，6岩藻糖基转移酶等的催化作用来催化，其催化糖苷键的形成。本文综述了α 3 β 1和α 5 β 1整合素的N-聚糖的翻译后修饰对其结合、活化和生物学功能的影响。
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 a and 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.