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Protein O-GlcNAcylation in diabetes and diabetic complications

Protein O-GlcNAcylation in diabetes and diabetic complications The post-translational modification of serine and threonine residues of proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is highly ubiquitous, dynamic and inducible. Protein O-GlcNAcylation serves as a key regulator of critical biological processes including transcription, translation, proteasomal degradation, signal transduction and apoptosis. Increased O-GlcNAcylation is directly linked to insulin resistance and to hyperglycemia-induced glucose toxicity, two hallmarks of diabetes and diabetic complications. In this review, we briefly summarize what is known about protein O-GlcNAcylation and nutrient metabolism, as well as discuss the commonly used tools to probe changes of O-GlcNAcylation in cultured cells and in animal models. We then focus on some key proteins modified by O-GlcNAc, which play crucial roles in the etiology and progression of diabetes and diabetic complications. Proteomic approaches are also highlighted to provide a system view of protein O-GlcNAcylation. Finally, we discuss how aberrant O-GlcNAcylation on certain proteins may be exploited to develop methods for the early diagnosis of pre-diabetes and/or diabetes. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Expert Review of Proteomics Taylor & Francis

Protein O-GlcNAcylation in diabetes and diabetic complications

Expert Review of Proteomics , Volume 10 (4): 16 – Aug 1, 2013
16 pages

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References (159)

Publisher
Taylor & Francis
Copyright
© 2013 Informa UK Ltd
ISSN
1744-8387
eISSN
1478-9450
DOI
10.1586/14789450.2013.820536
pmid
23992419
Publisher site
See Article on Publisher Site

Abstract

The post-translational modification of serine and threonine residues of proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is highly ubiquitous, dynamic and inducible. Protein O-GlcNAcylation serves as a key regulator of critical biological processes including transcription, translation, proteasomal degradation, signal transduction and apoptosis. Increased O-GlcNAcylation is directly linked to insulin resistance and to hyperglycemia-induced glucose toxicity, two hallmarks of diabetes and diabetic complications. In this review, we briefly summarize what is known about protein O-GlcNAcylation and nutrient metabolism, as well as discuss the commonly used tools to probe changes of O-GlcNAcylation in cultured cells and in animal models. We then focus on some key proteins modified by O-GlcNAc, which play crucial roles in the etiology and progression of diabetes and diabetic complications. Proteomic approaches are also highlighted to provide a system view of protein O-GlcNAcylation. Finally, we discuss how aberrant O-GlcNAcylation on certain proteins may be exploited to develop methods for the early diagnosis of pre-diabetes and/or diabetes.

Journal

Expert Review of ProteomicsTaylor & Francis

Published: Aug 1, 2013

Keywords: diabetes; diabetic complications; hyperglycemia; insulin resistance; O -GlcNAc; O -GlcNAcomics; proteomics

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