Potential of N-glycan in cell adhesion and migration as either a positive or negative regulator
Potential of N-glycan in cell adhesion and migration as either a positive or negative regulator
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DOI：
10.4161/cam.2.4.6748
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发表时间：
2008-10-01
影响因子：
3.2
通讯作者：
Taniguchi, Naoyuki
中科院分区：
文献类型：
--
作者：
Gu, Jianguo;Taniguchi, Naoyuki
糖基化是最丰富的翻译后修饰反应之一，真核生物中几乎一半的已知蛋白质都是糖基化的。事实上，低聚糖结构（glycan）的变化与许多生理和病理事件有关，包括细胞粘附、迁移、细胞生长、细胞分化和肿瘤侵袭。糖基化反应是由糖基转移酶催化的，它将糖链添加到各种复杂的碳水化合物上，如糖蛋白、糖脂和蛋白聚糖。功能糖组学利用糖基转移酶对糖进行重塑，是表征糖功能的一种很有前途的工具。在这里，我们将重点研究n -乙酰氨基葡萄糖转移酶III （GnT-III）和n -乙酰氨基葡萄糖转移酶V （GnT-V）对n -聚糖的重塑对整合素生物学功能的正调控和负调控。n -乙酰氨基葡萄糖转移酶III和n -乙酰氨基葡萄糖转移酶V催化支链n -聚糖的形成，分别分割GlcNAc和β 1,6 GlcNAc。通常，整合素被GnT-III修饰，抑制细胞迁移和癌症转移。相反，经GnT-V修饰的整合素促进细胞迁移和肿瘤侵袭。
Glycosylation is one of the most abundant posttranslational modification reactions, and nearly half of all known proteins in eukaryotes are glycosylated. In fact, changes in oligosaccharide structure (glycan) are associated with many physiological and pathological events, including cell adhesion, migration, cell growth, cell differentiation and tumor invasion. Glycosylation reactions are catalyzed by the action of glycosyltransferases, which add sugar chains to various complex carbohydrates such as glycoproteins, glycolipids and proteoglycans. Functional glycomics, which uses sugar remodeling by glycosyltransferases, is a promising tool for the characterization of glycan functions. Here, we will focus on the positive and negative regulation of biological functions of integrins by the remodeling of N-glycans with N-acetylglucosaminyltransferase III (GnT-III) and N-acetylglucosaminyltransferase V (GnT-V), which catalyze branched N-glycan formations, bisecting GlcNAc and beta 1,6 GlcNAc, respectively. Typically, integrins are modified by GnT-III, which inhibits cell migration and cancer metastasis. In contrast, integrins modified by GnT-V promote cell migration and cancer invasion.