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dc.contributor.authorMcGlory, Chrisen_UK
dc.contributor.authorWhite, Amanda Ten_UK
dc.contributor.authorTreins, Carolineen_UK
dc.contributor.authorDrust, Barryen_UK
dc.contributor.authorClose, Graeme Len_UK
dc.contributor.authorMacLaren, Don P Men_UK
dc.contributor.authorCampbell, Iain Ten_UK
dc.contributor.authorPhilp, Andrewen_UK
dc.contributor.authorSchenk, Simonen_UK
dc.contributor.authorMorton, James Pen_UK
dc.contributor.authorHamilton, David Leeen_UK
dc.description.abstractAMPK (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-32P] 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 p70S6K1thr389 was not significantly elevated. AMPK activity was suppressed from pre-RE at 3 h post-RE, whereas phosphorylated ACCser79 was unchanged. Total protein kinase B activity also was unchanged after RE from pre-RE levels. Of the other markers we assessed by WB, 4EBP1thr37/46 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.en_UK
dc.publisherAmerican Physiological Societyen_UK
dc.relationMcGlory C, White AT, Treins C, Drust B, Close GL, MacLaren DPM, Campbell IT, Philp A, Schenk S, Morton JP & Hamilton DL (2014) Application of the [γ-32P] ATP kinase assay to study anabolic signaling in human skeletal muscle. Journal of Applied Physiology, 116 (5), pp. 504-513.
dc.rightsThe publisher does not allow this work to be made publicly available in this Repository. Please use the Request a Copy feature at the foot of the Repository record to request a copy directly from the author. You can only request a copy if you wish to use this work for your own research or private study.en_UK
dc.titleApplication of the [γ-32P] ATP kinase assay to study anabolic signaling in human skeletal muscleen_UK
dc.typeJournal Articleen_UK
dc.rights.embargoreason[J Appl Physiol 2014.pdf] The publisher does not allow this work to be made publicly available in this Repository therefore there is an embargo on the full text of the work.en_UK
dc.citation.jtitleJournal of Applied Physiologyen_UK
dc.type.statusVoR - Version of Recorden_UK
dc.contributor.affiliationUniversity of Stirlingen_UK
dc.contributor.affiliationUniversity of California, San Diegoen_UK
dc.contributor.affiliationUniversity of Paris 5 (Rene Descartes University)en_UK
dc.contributor.affiliationLiverpool John Moores Universityen_UK
dc.contributor.affiliationLiverpool John Moores Universityen_UK
dc.contributor.affiliationLiverpool John Moores Universityen_UK
dc.contributor.affiliationLiverpool John Moores Universityen_UK
dc.contributor.affiliationUniversity of Birminghamen_UK
dc.contributor.affiliationUniversity of California, San Diegoen_UK
dc.contributor.affiliationLiverpool John Moores Universityen_UK
rioxxterms.apcnot requireden_UK
rioxxterms.typeJournal Article/Reviewen_UK
local.rioxx.authorMcGlory, Chris|en_UK
local.rioxx.authorWhite, Amanda T|en_UK
local.rioxx.authorTreins, Caroline|en_UK
local.rioxx.authorDrust, Barry|en_UK
local.rioxx.authorClose, Graeme L|en_UK
local.rioxx.authorMacLaren, Don P M|en_UK
local.rioxx.authorCampbell, Iain T|en_UK
local.rioxx.authorPhilp, Andrew|en_UK
local.rioxx.authorSchenk, Simon|en_UK
local.rioxx.authorMorton, James P|en_UK
local.rioxx.authorHamilton, David Lee|0000-0002-5620-4788en_UK
local.rioxx.projectInternal Project|University of Stirling|
local.rioxx.filenameJ Appl Physiol 2014.pdfen_UK
Appears in Collections:Faculty of Health Sciences and Sport Journal Articles

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