Document Detail


Glutathione depletion and acute exercise increase O-GlcNAc protein modification in rat skeletal muscle.
MedLine Citation:
PMID:  25416863     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Post-translational modification of intracellular proteins with O-linked β-N-acetylglucosamine (O-GlcNAc) profoundly affects protein structure, function, and metabolism. Although many skeletal muscle proteins are O-GlcNAcylated, the modification has not been extensively studied in this tissue, especially in the context of exercise. This study investigated the effects of glutathione depletion and acute exercise on O-GlcNAc protein modification in rat skeletal muscle. Diethyl maleate (DEM) was used to deplete intracellular glutathione and rats were subjected to a treadmill run. White gastrocnemius and soleus muscles were analyzed for glutathione status, O-GlcNAc and O-GlcNAc transferase (OGT) protein levels, and mRNA expression of OGT, O-GlcNAcase and glutamine:fructose-6-phosphate amidotransferase. DEM and exercise both reduced intracellular glutathione and increased O-GlcNAc. DEM upregulated OGT protein expression. The effects of the interventions were significant 4 h after exercise (P < 0.05). The changes in the mRNA levels of O-GlcNAc enzymes were different in the two muscles, potentially resulting from different rates of oxidative stress and metabolic demands between the muscle types. These findings indicate that oxidative environment promotes O-GlcNAcylation in skeletal muscle and suggest an interrelationship between cellular redox state and O-GlcNAc protein modification. This could represent one mechanism underlying cellular adaptation to oxidative stress and health benefits of exercise.
Authors:
Tina Tinkara Peternelj; Susan A Marsh; Natalie A Strobel; Aya Matsumoto; David Briskey; Vincent J Dalbo; Patrick S Tucker; Jeff S Coombes
Related Documents :
7469123 - Hybrid exercise echocardiograph.
11505203 - Quantification of limited augmentation of myocardial (99m)tc-tetrofosmin uptake at exer...
6477083 - Electromyographic amplitude normalization methods: improving their sensitivity as diagn...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-11-23
Journal Detail:
Title:  Molecular and cellular biochemistry     Volume:  -     ISSN:  1573-4919     ISO Abbreviation:  Mol. Cell. Biochem.     Publication Date:  2014 Nov 
Date Detail:
Created Date:  2014-11-23     Completed Date:  -     Revised Date:  2014-11-25    
Medline Journal Info:
Nlm Unique ID:  0364456     Medline TA:  Mol Cell Biochem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

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


Previous Document:  Up-regulation of UHRF1 by oncogenic Ras promoted the growth, migration, and metastasis of pancreatic...
Next Document:  New insights of superoxide dismutase inhibition of pyrogallol autoxidation.