Takahashi Motoko, Tsuda Takeo, Ikeda Yoshitaka, Honke Koichi, Taniguchi Naoyuki
Department of Biochemistry, Osaka Univerisity Graduate School of Medicine, B1, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Glycoconj J. 2004;20(3):207-12. doi: 10.1023/B:GLYC.0000024252.63695.5c.
Secreted proteins and membrane proteins are frequently post-translationally modified by oligosaccharides. Therefore, many glycoproteins are involved in signal transduction. One example is growth factor receptors, which are membrane proteins that often contain oligosaccharides. The oligosaccharides in those growth factor receptors play crucial roles in receptor functions. An analysis of glycosyltransferase-transfectants revealed that the branching structures of oligosaccharide also serve as important determinants. For example, N-glycans of epidermal growth factor receptor (EGFR) are involved in receptor sorting, ligand binding and dimerization. The addition of a bisecting GlcNAc to N-glycans increases the endocytosis of EGFR. N-glycans of Trk, a high affinity nerve growth factor receptor, also affect its function. Thus, oligosaccharides play an important role in growth factor signaling.
分泌蛋白和膜蛋白经常在翻译后被寡糖修饰。因此，许多糖蛋白参与信号转导。一个例子是生长因子受体，它们是通常含有寡糖的膜蛋白。那些生长因子受体中的寡糖在受体功能中起关键作用。对糖基转移酶转染细胞的分析表明，寡糖的分支结构也起着重要的决定作用。例如，表皮生长因子受体（EGFR）的N-聚糖参与受体分选、配体结合和二聚化。向N-聚糖中添加一个平分型GlcNAc会增加EGFR的内吞作用。Trk（一种高亲和力神经生长因子受体）的N-聚糖也会影响其功能。因此，寡糖在生长因子信号传导中起重要作用。
