Akimoto Yoshihiro, Hart Gerald W, Hirano Hiroshi, Kawakami Hayato
Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo, 181-8611, Japan.
Med Mol Morphol. 2005 Jun;38(2):84-91. doi: 10.1007/s00795-004-0264-1.
Nuclear and cytosolic proteins are glycosylated on serine or threonine residues by O-linked beta-N-acetylglucosamine (O-GlcNAc). O-GlcNAc modification is one of various posttranslational modifications and seems to be involved in the modulation of transcription and signal transduction. Accumulating data suggest a role for O-GlcNAc-modified proteins in diabetes, acting as a glucose sensor. It has been suggested that the hexosamine biosynthetic pathway is involved in the mechanism causing insulin resistance and diabetic complications. Excess glucose entering into the hexosamine biosynthetic pathway might cause elevated O-GlcNAc modification of various proteins. In this article, we review the current data regarding the relationship between O-GlcNAc modification and diabetes.
细胞核和胞质蛋白在丝氨酸或苏氨酸残基上通过O-连接的β-N-乙酰葡糖胺（O-GlcNAc）进行糖基化。O-GlcNAc修饰是各种翻译后修饰之一，似乎参与转录和信号转导的调节。越来越多的数据表明，O-GlcNAc修饰的蛋白在糖尿病中发挥作用，充当葡萄糖传感器。有人提出，己糖胺生物合成途径参与了导致胰岛素抵抗和糖尿病并发症的机制。进入己糖胺生物合成途径的过量葡萄糖可能导致各种蛋白的O-GlcNAc修饰增加。在本文中，我们综述了有关O-GlcNAc修饰与糖尿病之间关系的当前数据。
