Evidence map›Paper›PMID 23296747›Full record

ArticleJournal of cellular biochemistry2013

Selective inhibition of ATPase activity during contraction alters the activation of p38 MAP kinase isoforms in skeletal muscle.

Jeffrey J Brault, Natalie M Pizzimenti, John N Dentel, Robert W Wiseman

Open access · greenAbstract read
In one paragraph

Article in Journal of cellular biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. What can ATP content tell us about Barth syndrome muscle phenotypes?Journal of translational genetics and genomics · 2025
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  17. Review
  18. Ca²⁺-pumping impairment during repetitive fatiguing contractions in single myofibers: role of cross-bridge cycling.American journal of physiology. Regulatory, integrative and comparative physiology · 2013
    Article
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

4 authors at 2 institutions in 1 country.

Jeffrey J BraultDepartment of Kinesiology, East Carolina University, Greenville, North Carolina, USA.
Natalie M Pizzimenti
John N Dentel
Robert W Wiseman
Michigan State University · USEast Carolina University · US

Funding

Mechanisms of Metabolic Dysfunction in Type 2 DiabetesR01DK095210 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BEARD, DANIEL A, WISEMAN, ROBERT W · 2012 to 2016
$2.7M
NIDDK NIH HHS DK 095210NIDDK NIH HHS R01 DK095210
6 · The paper itself

Abstract

Muscle contractions strongly activate p38 MAP kinases, but the precise contraction-associated sarcoplasmic event(s) (e.g., force production, energetic demands, and/or calcium cycling) that activate these kinases are still unclear. We tested the hypothesis that during contraction the phosphorylation of p38 isoforms is sensitive to the increase in ATP demand relative to ATP supply. Energetic demands were inhibited using N-benzyl-p-toluene sulphonamide (BTS, type II actomyosin) and cyclopiazonic acid (CPA, SERCA). Extensor digitorum longus muscles from Swiss Webster mice were incubated in Ringer's solution (37°C) with or without inhibitors and then stimulated at 10 Hz for 15 min. Muscles were immediately freeze-clamped for metabolite and Western blot analysis. BTS and BTS + CPA treatment decreased force production by 85%, as measured by the tension time integral, while CPA alone potentiated force by 310%. In control muscles, contractions resulted in a 73% loss of ATP content and a concomitant sevenfold increase in IMP content, a measure of sustained energetic imbalance. BTS or CPA treatment lessened the loss of ATP, but BTS + CPA treatment completely eliminated the energetic imbalance since ATP and IMP levels were nearly equal to those of non-stimulated muscles. The independent inhibition of cytosolic ATPase activities had no effect on contraction-induced p38 MAPK phosphorylation, but combined treatment prevented the increase in phosphorylation of the γ isoform while the α/β isoforms unaffected. These observations suggest that an energetic signal may trigger phosphorylation of the p38γ isoform and also may explain how contractions differentially activate signaling pathways.

Indexed as

AnimalsEnzyme ActivationIndolesIn Vitro TechniquesIsoenzymesMaleMiceMitogen-Activated Protein Kinase 12Muscle ContractionMuscle, SkeletalMyosinsPhosphorylationProtein Processing, Post-TranslationalSarcoplasmic Reticulum Calcium-Transporting ATPasesSulfonamidesToluenecyclopiazonic acidIndolesIsoenzymesMitogen-Activated Protein Kinase 12MyosinsN-benzyl-p-toluene sulfonamideSarcoplasmic Reticulum Calcium-Transporting ATPasesSulfonamidesToluene

Identifiers

PMID23296747
PMCPMC3806227
OpenAlexW1979697157

What OpenQuestion holds

Textmetadata
LicenceTDM
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.