O-GlcNAc modification of nucleocytoplasmic proteins and diabetes (original) (raw)

Abstract

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.

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Authors and Affiliations

1. Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo, 181-8611, Japan
   Yoshihiro Akimoto, Hiroshi Hirano & Hayato Kawakami
2. Department of Biological Chemistry, Johns Hopkins School of Medicine, Baltimore, MD, USA
   Gerald W. Hart
3. Nittai Jusei Medical College for Judo Therapeutics, Tokyo, Japan
   Hiroshi Hirano

Authors

1. Yoshihiro Akimoto
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2. Gerald W. Hart
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3. Hiroshi Hirano
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4. Hayato Kawakami
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Corresponding author

Correspondence toYoshihiro Akimoto.

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Akimoto, Y., Hart, G., Hirano, H. et al. _O_-GlcNAc modification of nucleocytoplasmic proteins and diabetes.Med Mol Morphol 38, 84–91 (2005). https://doi.org/10.1007/s00795-004-0264-1

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• Received: 26 April 2004
• Accepted: 08 June 2004
• Issue Date: June 2005
• DOI: https://doi.org/10.1007/s00795-004-0264-1

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