O-GlcNAc modification of nucleocytoplasmic proteins and diabetes

被引：42

作者：

Akimoto Y. ^{[1
]}

Hart G.W. ^{[2
]}

Hirano H. ^{[1
,3
]}

Kawakami H. ^{[1
]}

机构：

[1] Department of Anatomy, Kyorin University, School of Medicine, Mitaka

[2] Department of Biological Chemistry, Johns Hopkins School of Medicine, Baltimore, MD

[3] Nittai Jusei Medical College for Judo Therapeutics, Tokyo

来源：

Medical Molecular Morphology | 2005年 / 38卷 / 2期

关键词：

Aorta; Cornea; Diabetes; Glycosyltransferase; Hexosamine biosynthetic pathway; O-GlcNAc; Pancreas;

D O I：

10.1007/s00795-004-0264-1

中图分类号：

学科分类号：

摘要：

Nuclear and cytosolic proteins are glycosylated on serine or threonine residues by O-linked β-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. © The Japanese Society for Clinical Molecular Morphology 2005.

引用

页码：84 / 91

页数：7

共 59 条

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[2]

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[3]

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[10]

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