Document Detail

Swim-exercised mice show a decreased level of protein O-GlcNAcylation and expression of O-GlcNAc transferase in heart.
MedLine Citation:
PMID:  21493720     Owner:  NLM     Status:  MEDLINE    
Swim-training exercise in mice leads to cardiac remodeling associated with an improvement in contractile function. Protein O-linked N-acetylglucosamine (O-GlcNAcylation) is a posttranslational modification of serine and threonine residues capable of altering protein-protein interactions affecting gene transcription, cell signaling pathways, and general cell physiology. Increased levels of protein O-GlcNAcylation in the heart have been associated with pathological conditions such as diabetes, ischemia, and hypertrophic heart failure. In contrast, the impact of physiological exercise on protein O-GlcNAcylation in the heart is currently unknown. Swim-training exercise in mice was associated with the development of a physiological hypertrophy characterized by an improvement in contractile function relative to sedentary mice. General protein O-GlcNAcylation was significantly decreased in swim-exercised mice. This effect was mirrored in the level of O-GlcNAcylation of individual proteins such as SP1. The decrease in protein O-GlcNAcylation was associated with a decrease in the expression of O-GlcNAc transferase (OGT) and glutamine-fructose amidotransferase (GFAT) 2 mRNA. O-GlcNAcase (OGA) activity was actually lower in swim-trained than sedentary hearts, suggesting that it did not contribute to the decreased protein O-GlcNAcylation. Thus it appears that exercise-induced physiological hypertrophy is associated with a decrease in protein O-GlcNAcylation, which could potentially contribute to changes in gene expression and other physiological changes associated with exercise.
Darrell D Belke
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-04-14
Journal Detail:
Title:  Journal of applied physiology (Bethesda, Md. : 1985)     Volume:  111     ISSN:  1522-1601     ISO Abbreviation:  J. Appl. Physiol.     Publication Date:  2011 Jul 
Date Detail:
Created Date:  2011-07-12     Completed Date:  2013-07-08     Revised Date:  2013-09-26    
Medline Journal Info:
Nlm Unique ID:  8502536     Medline TA:  J Appl Physiol (1985)     Country:  United States    
Other Details:
Languages:  eng     Pagination:  157-62     Citation Subset:  IM    
Faculty of Kinesiology, University of Calgary, Calgary, Alberta, Canada.
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MeSH Terms
Acetylglucosamine / metabolism*
Adaptation, Physiological
Cardiomegaly / genetics,  metabolism*,  physiopathology
Gene Expression Regulation, Enzymologic
Muscle Contraction
Muscle Proteins / metabolism*
Myocardium / metabolism*
N-Acetylglucosaminyltransferases / genetics,  metabolism*
Nitrogenous Group Transferases / genetics,  metabolism
Physical Exertion*
Protein Processing, Post-Translational*
RNA, Messenger / metabolism
Reg. No./Substance:
0/Muscle Proteins; 0/RNA, Messenger; 56-45-1/Serine; 72-19-5/Threonine; 7512-17-6/Acetylglucosamine; EC 2.4.1.-/N-Acetylglucosaminyltransferases; EC 2.4.1.-/O-GlcNAc transferase; EC 2.6.-/GFPT2 protein, mouse; EC 2.6.-/Nitrogenous Group Transferases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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