Whey protein intake after resistance exercise activates mTOR signaling in a dose-dependent manner in human skeletal muscle.

Ryo Kakigi, Toshinori Yoshihara, Hayao Ozaki, Yuji Ogura, Noriko Ichinoseki-Sekine, Hiroyuki Kobayashi, Hisashi Naito
Author Information
  1. Ryo Kakigi: Institute of Health and Sports Science & Medicine, Juntendo University, 1-1 Hiragagakuendai, Inzai, Chiba, 270-1695, Japan.

Abstract

PURPOSE: Protein ingestion after resistance exercise increases muscle protein synthesis (MPS) in a dose-dependent manner. However, the molecular mechanism(s) for the dose-dependency of MPS remains unclear. This study aimed to determine the dose response of mammalian target of rapamycin (mTOR) signaling in muscle with ingestion of protein after resistance exercise.
METHODS: Fifteen male subjects performed four sets of six unilateral isokinetic concentric knee extensions. Immediately after exercise, eight subjects consumed water only. The other seven subjects, in a randomized-order crossover design, took either a 10 [3.6 g essential amino acids (EAA)] or 20 g (7.1 g EAA) solution of whey protein. Muscle biopsies from the vastus lateralis muscle were taken 30 min before and 1 h after resistance exercise. Phosphorylation of Akt (Ser473), mTOR (Ser2448), 4E-BP1 (Thr37/46), and S6K1 (Thr389) was measured by western blotting.
RESULTS: Concentric knee extension exercise alone did not increase phosphorylation of Akt and mTOR 1 h after exercise, but ingesting protein after exercise significantly increased the phosphorylation of Akt and mTOR in a dose-dependent manner (P < 0.05). 4E-BP1 phosphorylation significantly decreased after resistance exercise (P < 0.05), but subjects who took 10 or 20 g of protein after exercise showed increased 4E-BP1 from post-exercise dephosphorylation (P < 0.05). S6K1 phosphorylation significantly increased after resistance exercise (P < 0.05), and 20 g of protein further increased S6K1 phosphorylation compared with ingestion of 10 g (P < 0.05).
CONCLUSIONS: These findings suggest that whey protein intake after resistance exercise activates mTOR signaling in a dose-dependent manner in untrained men.

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MeSH Term

Adaptor Proteins, Signal Transducing
Administration, Oral
Amino Acids, Essential
Cell Cycle Proteins
Cross-Over Studies
Dose-Response Relationship, Drug
Humans
Knee
Male
Milk Proteins
Muscle, Skeletal
Phosphoproteins
Phosphorylation
Proto-Oncogene Proteins c-akt
Resistance Training
Ribosomal Protein S6 Kinases, 70-kDa
Signal Transduction
TOR Serine-Threonine Kinases
Whey Proteins
Young Adult

Chemicals

Adaptor Proteins, Signal Transducing
Amino Acids, Essential
Cell Cycle Proteins
EIF4EBP1 protein, human
Milk Proteins
Phosphoproteins
Whey Proteins
Proto-Oncogene Proteins c-akt
Ribosomal Protein S6 Kinases, 70-kDa
TOR Serine-Threonine Kinases
ribosomal protein S6 kinase, 70kD, polypeptide 1

Word Cloud

Created with Highcharts 10.0.0exerciseproteinresistancemTORgphosphorylationP<005muscledose-dependentmannersubjectsincreasedingestionsignaling10201Akt4E-BP1S6K1significantlyMPSkneetookEAAwheyhintakeactivatesPURPOSE:ProteinincreasessynthesisHowevermolecularmechanismsdose-dependencyremainsunclearstudyaimeddeterminedoseresponsemammaliantargetrapamycinMETHODS:FifteenmaleperformedfoursetssixunilateralisokineticconcentricextensionsImmediatelyeightconsumedwatersevenrandomized-ordercrossoverdesigneither[36essentialaminoacids]7solutionMusclebiopsiesvastuslateralistaken30minPhosphorylationSer473Ser2448Thr37/46Thr389measuredwesternblottingRESULTS:Concentricextensionaloneincreaseingestingdecreasedshowedpost-exercisedephosphorylationcomparedCONCLUSIONS:findingssuggestuntrainedmenWheyhumanskeletal

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