Evidence map›Paper›PMID 24436296›Full record

ArticleJournal of applied physiology (Bethesda, Md. : 1985)2014

Application of the [γ-32P] ATP kinase assay to study anabolic signaling in human skeletal muscle.

Chris McGlory, Amanda White, Caroline Treins, Barry Drust, Graeme L Close, Don P M Maclaren, Iain T Campbell, Andrew Philp, Simon Schenk, James P Morton and 1 more

Abstract read
In one paragraph

Article in Journal of applied physiology (Bethesda, Md. : 1985), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 38 citations in OpenAlex.

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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

11 authors at 5 institutions in 3 countries.

Chris McGloryHealth & Exercise Sciences Research Group University of Stirling, Stirling, United Kingdom;
Amanda White
Caroline Treins
Barry Drust
Graeme L Close
Don P M Maclaren
Iain T Campbell
Andrew Philp
Simon Schenk
James P Morton
D Lee Hamilton
Liverpool John Moores University · GBUniversity of California, San Diego · USUniversity of Stirling · GBUniversité Paris Cité · FRUniversity of Birmingham · GB

Funding

Transgenic & Knock-out MouseP30DK063491 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PETER J TONTONOZ · 2003 to 2026
$40.4M
GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
National Center for Muscle Rehabilitation ResearchR24HD050837 · NICHD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LIEBER, RICHARD L., WARD, SAMUEL RICHARD · 2005 to 2014
$7.2M
SIRT1 and muscle insulin sensitivityR01AG043120 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SCHENK, SIMON · 2012 to 2016
$1.6M
Muscle Triglyceride Metabolism Core CenterP30AR058878 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LIEBER, RICHARD L. · 2009 to 2010
$925k
Medical Research Council MR/K00414X/1NIAMS NIH HHS P30 AR058878NIA NIH HHS R01 AG043120NICHD NIH HHS R24 HD050837NIDDK NIH HHS P30 DK063491NIGMS NIH HHS T32 GM007752
6 · The paper itself

Abstract

AMPK (AMP-dependant protein kinase)-mTORC1 (mechanistic target of rapamycin in complex 1)-p70S6K1 (ribosomal protein S6 kinase 1 of 70 kDa) signaling plays a crucial role in muscle protein synthesis (MPS). Understanding this pathway has been advanced by the application of the Western blot (WB) technique. However, because many components of the mTORC1 pathway undergo numerous, multisite posttranslational modifications, solely studying the phosphorylation changes of mTORC1 and its substrates may not adequately represent the true metabolic signaling processes. The aim of this study was to develop and apply a quantitative in vitro [γ-(32)P] ATP kinase assay (KA) for p70S6K1 to assess kinase activity in human skeletal muscle to resistance exercise (RE) and protein feeding. In an initial series of experiments the assay was validated in tissue culture and in p70S6K1-knockout tissues. Following these experiments, the methodology was applied to assess p70S6K1 signaling responses to a physiologically relevant stimulus. Six men performed unilateral RE followed by the consumption of 20 g of protein. Muscle biopsies were obtained at pre-RE, and 1 and 3 h post-RE. In response to RE and protein consumption, p70S6K1 activity as assessed by the KA was significantly increased from pre-RE at 1 and 3 h post-RE. However, phosphorylated p70S6K1(thr389) was not significantly elevated. AMPK activity was suppressed from pre-RE at 3 h post-RE, whereas phosphorylated ACC(ser79) was unchanged. Total protein kinase B activity also was unchanged after RE from pre-RE levels. Of the other markers we assessed by WB, 4EBP1(thr37/46) phosphorylation was the only significant responder, being elevated at 3 h post-RE from pre-RE. These data highlight the utility of the KA to study skeletal muscle plasticity.

Indexed as

ATP Synthetase ComplexesRadiopharmaceuticalsAdultAMP-Activated Protein KinasesAnimalsBlotting, WesternHumansImmunoprecipitationMaleMiceMice, KnockoutMuscle, SkeletalPhosphatesProto-Oncogene Proteins c-aktResistance TrainingRibosomal Protein S6 Kinases, 70-kDaAMP-Activated Protein KinasesATP Synthetase ComplexesPhosphatesProto-Oncogene Proteins c-aktRadiopharmaceuticalsRibosomal Protein S6 Kinases, 70-kDaAMPKmTORC1p70S6K1resistance exercise

Identifiers

PMID24436296
PMCPMC4116398
OpenAlexW1984952509

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.