Takahashi Motoko, Kuroki Yoshio, Ohtsubo Kazuaki, Taniguchi Naoyuki
Department of Biochemistry, Sapporo Medical University School of Medicine, Sapporo, Japan.
Carbohydr Res. 2009 Aug 17;344(12):1387-90. doi: 10.1016/j.carres.2009.04.031. Epub 2009 May 4.
Among the various posttranslational modification reactions, glycosylation is the most common, and nearly 50% of all known proteins are thought to be glycosylated. In particular, most of the molecules involved in cell-cell communication are glycosylated, and glycosylation is thus implicated in many physiological and pathological events, including cell growth, cell-cell adhesion, and tumor metastasis. As many of the glycosyltransferases are cloned, it is becoming possible to alter the oligosaccharide structures artificially and examine the effects. Among the glycosyltransferases involved in the biosynthesis of N-glycan branching, this review will focus on the function of Fut8 and N-acetylglucosaminyltransferase III, which directly modify the N-glycan core. It is suggested that these two glycosyltransferases are involved in the conformation and the function of the modified proteins including cell-surface receptors and adhesion molecules.
在各种翻译后修饰反应中，糖基化是最常见的，据认为所有已知蛋白质中有近50%被糖基化。特别是，大多数参与细胞间通讯的分子都被糖基化，因此糖基化与许多生理和病理事件有关，包括细胞生长、细胞间粘附和肿瘤转移。随着许多糖基转移酶被克隆，人工改变寡糖结构并研究其效果变得可能。在参与N-聚糖分支生物合成的糖基转移酶中，本综述将重点关注Fut8和N-乙酰葡糖胺基转移酶III的功能，它们直接修饰N-聚糖核心。有人认为这两种糖基转移酶参与了包括细胞表面受体和粘附分子在内的修饰蛋白的构象和功能。
