Evidence map›Paper›PMID 24477538›Full record

ArticleAmerican journal of physiology. Regulatory, integrative and comparative physiology2014

EUK-134 ameliorates nNOSμ translocation and skeletal muscle fiber atrophy during short-term mechanical unloading.

John M Lawler, Mary Kunst, Jeff M Hord, Yang Lee, Kumar Joshi, Rachel E Botchlett, Angelo Ramirez, Daniel A Martinez

Abstract read
In one paragraph

Article in American journal of physiology. Regulatory, integrative and comparative physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

30 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Chaperone Proteins: The Rising Players in Muscle Atrophy.Journal of cachexia, sarcopenia and muscle · 2025
    Review
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  8. Article
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  10. Article
  11. How Postural Muscle Senses Disuse? Early Signs and Signals.International journal of molecular sciences · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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 2 institutions in 1 country.

John M LawlerRedox Biology and Cell Signaling Laboratory, Department of Health and Kinesiology, Texas A&M University, College Station, Texas;
Mary Kunst
Jeff M Hord
Yang Lee
Kumar Joshi
Rachel E Botchlett
Angelo Ramirez
Daniel A Martinez
Texas A&M University · USUniversity of Houston · US

Funding

Regulation of Oxidative Stress in the mdx DiaphragmR03AR054084 · NIAMS · TEXAS A&M UNIVERSITY · PI LAWLER, JOHN M · 2006 to 2008
$204k
NIAMS NIH HHS AR-054084
6 · The paper itself

Abstract

Reduced mechanical loading during bedrest, spaceflight, and casting, causes rapid morphological changes in skeletal muscle: fiber atrophy and reduction of slow-twitch fibers. An emerging signaling event in response to unloading is the translocation of neuronal nitric oxide synthase (nNOSμ) from the sarcolemma to the cytosol. We used EUK-134, a cell-permeable mimetic of superoxide dismutase and catalase, to test the role of redox signaling in nNOSμ translocation and muscle fiber atrophy as a result of short-term (54 h) hindlimb unloading. Fischer-344 rats were divided into ambulatory control, hindlimb-unloaded (HU), and hindlimb-unloaded + EUK-134 (HU-EUK) groups. EUK-134 mitigated the unloading-induced phenotype, including muscle fiber atrophy and muscle fiber-type shift from slow to fast. nNOSμ immunolocalization at the sarcolemma of the soleus was reduced with HU, while nNOSμ protein content in the cytosol increased with unloading. Translocation of nNOS from the sarcolemma to cytosol was virtually abolished by EUK-134. EUK-134 also mitigated dephosphorylation at Thr-32 of FoxO3a during HU. Hindlimb unloading elevated oxidative stress (4-hydroxynonenal) and increased sarcolemmal localization of Nox2 subunits gp91phox (Nox2) and p47phox, effects normalized by EUK-134. Thus, our findings are consistent with the hypothesis that oxidative stress triggers nNOSμ translocation from the sarcolemma and FoxO3a dephosphorylation as an early event during mechanical unloading. Thus, redox signaling may serve as a biological switch for nNOS to initiate morphological changes in skeletal muscle fibers.

Indexed as

Hindlimb SuspensionAldehydesAnimalsAntioxidantsCytosolDisease Models, AnimalForkhead Box Protein O3Forkhead Transcription FactorsMembrane GlycoproteinsMuscle Fibers, Fast-TwitchMuscle Fibers, SkeletalMuscle Fibers, Slow-TwitchMuscular AtrophyNADPH Oxidase 2NADPH OxidasesNitric Oxide Synthase Type I4-hydroxy-2-nonenalAldehydesAntioxidantsCybb protein, ratEUK-134Forkhead Box Protein O3Forkhead Transcription FactorsFOXO3 protein, ratMembrane GlycoproteinsNADPH Oxidase 2NADPH Oxidasesneutrophil cytosolic factor 1Nitric Oxide Synthase Type INos1 protein, ratOrganometallic CompoundsSalicylatesatrophydisuseFoxO3anNOSoxidative stressskeletal muscle

Identifiers

PMID24477538
PMCPMC3962621
OpenAlexW1995775121

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.