O-GlcNAc modification of nucleocytoplasmic proteins and diabetes
O-GlcNAc modification of nucleocytoplasmic proteins and diabetes
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DOI：
10.1007/s00795-004-0264-1
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发表时间：
2005-06-01
影响因子：
1.8
通讯作者：
Kawakami, Hayato
中科院分区：
文献类型：
--
作者：
Akimoto, Yoshihiro;Hart, Gerald W.;Kawakami, Hayato
核蛋白和胞质蛋白在丝氨酸或苏氨酸残基上被O-连接的β-N-乙酰葡糖胺（O-GlcNAc）糖基化。O-GlcNAc修饰是多种翻译后修饰之一，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修饰的蛋白质在糖尿病中的作用，作为葡萄糖传感器。已表明己糖胺生物合成途径参与引起胰岛素抵抗和糖尿病并发症的机制。过量的葡萄糖进入己糖胺生物合成途径可能导致各种蛋白质的O-GlcNAc修饰升高。在这篇文章中，我们回顾了目前的数据有关的O-GlcNAc修饰和糖尿病之间的关系。
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.