Evidence map›Paper›PMID 17540697›Full record

ArticleThe Journal of physiology2007

Exercise improves phosphatidylinositol-3,4,5-trisphosphate responsiveness of atypical protein kinase C and interacts with insulin signalling to peptide elongation in human skeletal muscle.

Christian Frøsig, Mini P Sajan, Stine J Maarbjerg, Nina Brandt, Carsten Roepstorff, Jørgen F P Wojtaszewski, Bente Kiens, Robert V Farese, 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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 23% 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, 41 citations in OpenAlex.

  1. Trial
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  6. Long-Term Recreational Football Training and Health in Aging.International journal of environmental research and public health · 2020
    Review
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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

9 authors at 3 institutions in 2 countries.

Christian FrøsigCopenhagen Muscle Research Centre, Section of Human Physiology, Department of Exercise and Sport Sciences, University of Copenhagen, 13, Universitetsparken, DK-2100, Copenhagen, Denmark.
Mini P Sajan
Stine J Maarbjerg
Nina Brandt
Carsten Roepstorff
Jørgen F P Wojtaszewski
Bente Kiens
Robert V Farese
Erik A Richter
University of Copenhagen · DKJames A. Haley Veterans' Hospital · USUniversity of South Florida · US

Funding

Activation of Atypical PKC by Insulin and Other AgonistsR01DK065969 · NIDDK · UNIVERSITY OF SOUTH FLORIDA · PI FARESE, ROBERT V · 2004 to 2014
$2.8M
NIDDK NIH HHS R01 DK065969
6 · The paper itself

Abstract

We investigated if acute endurance-type exercise interacts with insulin-stimulated activation of atypical protein kinase C (aPKC) and insulin signalling to peptide chain elongation in human skeletal muscle. Four hours after acute one-legged exercise, insulin-induced glucose uptake was approximately 80% higher (N = 12, P < 0.05) in previously exercised muscle, measured during a euglycaemic-hyperinsulinaemic clamp (100 microU ml(-1)). Insulin increased (P < 0.05) both insulin receptor substrate (IRS)-1 and IRS-2 associated phosphatidylinositol (PI)-3 kinase activity and led to increased (P < 0.001) phosphorylation of Akt on Ser(473) and Thr(308) in skeletal muscle. Interestingly, in response to prior exercise IRS-2-associated PI-3 kinase activity was higher (P < 0.05) both at basal and during insulin stimulation. This coincided with correspondingly altered phosphorylation of the extracellular-regulated protein kinase 1/2 (ERK 1/2), p70S6 kinase (P70S6K), eukaryotic elongation factor 2 (eEF2) kinase and eEF2. aPKC was similarly activated by insulin in rested and exercised muscle, without detectable changes in aPKC Thr(410) phosphorylation. However, when adding phosphatidylinositol-3,4,5-triphosphate (PIP3), the signalling product of PI-3 kinase, to basal muscle homogenates, aPKC was more potently activated (P = 0.01) in previously exercised muscle. Collectively, this study shows that endurance-type exercise interacts with insulin signalling to peptide chain elongation. Although protein turnover was not evaluated, this suggests that capacity for protein synthesis after acute endurance-type exercise may be improved. Furthermore, endurance exercise increased the responsiveness of aPKC to PIP3 providing a possible link to improved insulin-stimulated glucose uptake after exercise.

Indexed as

AdultBlood GlucoseExerciseGlucose Clamp TechniqueHumansHyperinsulinismInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsLactatesMaleMuscle, SkeletalPeptide Chain Elongation, TranslationalPhosphatidylinositol PhosphatesPhosphoproteinsProtein Kinase CBlood GlucoseInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsIRS1 protein, humanIRS2 protein, humanLactatesphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol PhosphatesPhosphoproteinsProtein Kinase C

Identifiers

PMID17540697
PMCPMC2075270
OpenAlexW1924506987

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.