Evidence map›Paper›PMID 17627985›Full record

ArticleThe Journal of physiology2007

Effect of endurance exercise training on Ca2+ calmodulin-dependent protein kinase II expression and signalling in skeletal muscle of humans.

Adam J Rose, Christian Frøsig, Bente Kiens, Jørgen F P Wojtaszewski, Erik A Richter

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 86 citations in OpenAlex.

  1. Pooled it
  2. Intensive training and reduced volume increases muscle FXYD1 expression and phosphorylation at rest and during exercise in athletes.American journal of physiology. Regulatory, integrative and comparative physiology · 2016
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  15. Parallel epigenetic modifications induced by hatchery rearing in a Pacific salmon.Proceedings of the National Academy of Sciences of the United States of America · 2017
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  16. Regulation ofPhysiological reports · 2017
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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

5 authors at 1 institution in 1 country.

Adam J RoseCopenhagen Muscle Research Centre, Department of Exercise and Sport Sciences, Section of Human Physiology, University of Copenhagen, Universitetsparken 13, Copenhagen, Denmark 2100. arose@ifi.ku.dk
Christian Frøsig
Bente Kiens
Jørgen F P Wojtaszewski
Erik A Richter
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here the hypothesis that skeletal muscle Ca(2+)-calmodulin-dependent kinase II (CaMKII) expression and signalling would be modified by endurance training was tested. Eight healthy, young men completed 3 weeks of one-legged endurance exercise training with muscle samples taken from both legs before training and 15 h after the last exercise bout. Along with an approximately 40% increase in mitochondrial F(1)-ATP synthase expression, there was an approximately 1-fold increase in maximal CaMKII activity and CaMKII kinase isoform expression after training in the active leg only. Autonomous CaMKII activity and CaMKII autophosphorylation were increased to a similar extent. However, there was no change in alpha-CaMKII anchoring protein expression with training. Nor was there any change in expression or Thr(17) phosphorylation of the CaMKII substrate phospholamban with training. However, another CaMKII substrate, serum response factor (SRF), had an approximately 60% higher phosphorylation at Ser(103) after training, with no change in SRF expression. There were positive correlations between the increases in CaMKII expression and SRF phosphorylation as well as F(1)ATPase expression with training. After training, there was an increase in cyclic-AMP response element binding protein phosphorylation at Ser(133), but not expression, in muscle of both legs. Taken together, skeletal muscle CaMKII kinase isoform expression and SRF phosphorylation is higher with endurance-type exercise training, adaptations that are restricted to active muscle. This may contribute to greater Ca(2+) mediated regulation during exercise and the altered muscle phenotype with training.

Indexed as

Adaptation, PhysiologicalCalcium SignalingMuscle ContractionAdultCalcium-Binding ProteinsCalcium-Calmodulin-Dependent Protein Kinase Type 2Cyclic AMP Response Element-Binding ProteinEnzyme InductionExerciseHumansIsoenzymesMaleMitochondria, MuscleMuscle, SkeletalPhenotypePhospholambanCalcium-Binding ProteinsCalcium-Calmodulin-Dependent Protein Kinase Type 2Cyclic AMP Response Element-Binding ProteinIsoenzymesPhospholambanProton-Translocating ATPasesSerum Response FactorSRF protein, human

Identifiers

PMID17627985
PMCPMC2277010
OpenAlexW1522768491

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.