Evidence map›Paper›PMID 25416863›Full record

ArticleMolecular and cellular biochemistry2015

Glutathione depletion and acute exercise increase O-GlcNAc protein modification in rat skeletal muscle.

Tina Tinkara Peternelj, Susan A Marsh, Natalie A Strobel, Aya Matsumoto, David Briskey, Vincent J Dalbo, Patrick S Tucker, Jeff S Coombes

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Article in Molecular and cellular biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
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  4. Article
  5. Article
  6. ProteinMetabolites · 2022
    Review
  7. Article
  8. Cells · 2022
    Review
  9. Article
  10. Review
  11. Role ofPhysiological reviews · 2021
    Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Modulation of angiotensin II signaling following exercise training in heart failure.American journal of physiology. Heart and circulatory physiology · 2015
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 5 institutions in 2 countries.

Tina Tinkara PeterneljAntioxidant Research Group, School of Human Movement Studies, The University of Queensland, St Lucia, Brisbane, QLD, 4072, Australia, tina.peternelj@uqconnect.edu.au.
Susan A Marsh
Natalie A Strobel
Aya Matsumoto
David Briskey
Vincent J Dalbo
Patrick S Tucker
Jeff S Coombes
University of Queensland · AUCentral Queensland University · AUBaker Heart and Diabetes Institute · AUUniversity of Western Australia · AUWashington State University Spokane · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Oxidative StressAnimalsGlutathioneMaleatesMuscle, SkeletalN-AcetylglucosaminyltransferasesPhysical Conditioning, AnimalProtein Processing, Post-TranslationalRatsdiethyl maleateGlutathioneMaleatesN-AcetylglucosaminyltransferasesO-GlcNAc transferase

Identifiers

PMID25416863
OpenAlexW2003332720

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.