Document Detail

Enhanced cardiac protein glycosylation (O-GlcNAc) of selected mitochondrial proteins in rats artificially selected for low running capacity.
MedLine Citation:
PMID:  23132757     Owner:  NLM     Status:  MEDLINE    
O-linked β-N-acetyl glucosamine (O-GlcNAc) is a posttranslational modification consisting of a single N-acetylglucosamine moiety attached by an O-β-glycosidic linkage to serine and threonine residues of both nuclear and cytosolic proteins. Analogous to phosphorylation, the modification is reversible and dynamic, changing in response to stress, nutrients, hormones, and exercise. Aims of this study were to examine differences in O-GlcNAc protein modification in the cardiac tissue of rats artificially selected for low (LCR) or high (HCR) running capacity. Hyperinsulinemic-euglycemic clamps in conscious animals assessed insulin sensitivity while 2-[(14)C] deoxyglucose tracked both whole body and tissue-specific glucose disposal. Immunoblots of cardiac muscle examined global O-GlcNAc modification, enzymes that control its regulation (OGT, OGA), and specific proteins involved in mitochondrial oxidative phosphorylation. LCR rats were insulin resistant disposing of 65% less glucose than HCR. Global tissue O-GlcNAc, OGT, OGA, and citrate synthase were similar between groups. Analysis of cardiac proteins revealed enhanced O-GlcNAcylation of mitochondrial Complex I, Complex IV, VDAC, and SERCA in LCR compared with HCR. These results are the first to establish an increase in specific protein O-GlcNAcylation in LCR animals that may contribute to progressive mitochondrial dysfunction and the pathogenesis of insulin resistance observed in the LCR phenotype.
Virginia L Johnsen; Darrell D Belke; Curtis C Hughey; Dustin S Hittel; Russell T Hepple; Lauren G Koch; Steven L Britton; Jane Shearer
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-11-06
Journal Detail:
Title:  Physiological genomics     Volume:  45     ISSN:  1531-2267     ISO Abbreviation:  Physiol. Genomics     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-01-08     Completed Date:  2013-06-11     Revised Date:  2014-01-10    
Medline Journal Info:
Nlm Unique ID:  9815683     Medline TA:  Physiol Genomics     Country:  United States    
Other Details:
Languages:  eng     Pagination:  17-25     Citation Subset:  IM    
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MeSH Terms
Absorptiometry, Photon
Analysis of Variance
Carbon Radioisotopes / metabolism
Citrate (si)-Synthase / metabolism
Fatty Acids, Nonesterified / blood
Glucose / metabolism
Glucose Clamp Technique / methods
Insulin Resistance / physiology*
Mitochondrial Proteins / genetics*,  metabolism*
Models, Animal*
Myocardium / metabolism*
N-Acetylglucosaminyltransferases / metabolism
Oxidative Phosphorylation
Rats, Inbred Strains
Running / physiology*
Grant Support
MOP 79397//Canadian Institutes of Health Research; R01 DK-077200/DK/NIDDK NIH HHS; R0D012098A//PHS HHS; R24 RR-017718/RR/NCRR NIH HHS
Reg. No./Substance:
0/Carbon Radioisotopes; 0/Fatty Acids, Nonesterified; 0/Mitochondrial Proteins; EC (si)-Synthase; EC 2.4.1.-/N-Acetylglucosaminyltransferases; EC 2.4.1.-/UDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase; IY9XDZ35W2/Glucose

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

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