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O-GlcNAcomics - Revealing Roles of O-GlcNAcylation in Disease Mechanisms and Development of Potential Diagnostics.
MedLine Citation:
PMID:  23640805     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
O-linked-β-N-acetylglucosamine (O-GlcNAc) is a dynamic post-translational modification of the 3'-hydroxyl groups of serine or threonine residues of nuclear, cytoplasmic, and mitochondrial proteins. The cycling of this modification is regulated in response to nutrients, stress, and other extracellular stimuli by the catalytic activities of O-GlcNAc transferase and O-GlcNAcase. O-GlcNAc is functionally similar to phosphorylation and has been demonstrated to play critical roles in numerous biological processes, including cell signaling, transcription, and disease etiology. Since its discovery nearly thirty years ago, studies have demonstrated that the O-GlcNAc is highly abundant and widespread, like phosphorylation however, the development of methodologies to study O-GlcNAc at the site level has been challenging. Recently, a number of studies have overcome these challenges and describe new tagging, enrichment, and mass spectrometric-based approaches to study O-GlcNAc in terms of its site identification, stoichiometry, and dynamics on proteins. The development of these methods are key for elucidation of O-GlcNAc's functional crosstalk with phosphorylation and other PTMs, and will serve to provide the necessary information for the development of site-specific antibodies, which will aid in the determination of a particular protein's site specific function. In this review, we describe these methods and summarize results obtained from them demonstrating the roles of O-GlcNAc in diabetes, cancer, Alzheimer's, and in learning and memory, while also describing how these new strategies have implicated O-GlcNAc as a potential diagnostic for the screening of patients for prediabetes. This article is protected by copyright. All rights reserved.
Authors:
Ronald J Copeland; Guanghui Han; Gerald W Hart
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-5-3
Journal Detail:
Title:  Proteomics. Clinical applications     Volume:  -     ISSN:  1862-8354     ISO Abbreviation:  Proteomics Clin Appl     Publication Date:  2013 May 
Date Detail:
Created Date:  2013-5-3     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101298608     Medline TA:  Proteomics Clin Appl     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
This article is protected by copyright. All rights reserved.
Affiliation:
Department of Biological Chemistry, The Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD, 21205-2185.
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