title: Resistance exercise with whey protein ingestion affects mTOR signaling pathway and myostatin in men.
abstract: Signaling pathways sense local and systemic signals and regulate muscle hypertrophy. The effects of whey protein ingestion on acute and long-term signaling responses of resistance exercise are not well known. Previously untrained young men were randomized into protein (n = 9), placebo (n = 9), and control (n = 11) groups. Vastus lateralis (VL) muscle biopsies were taken before and 1 h and 48 h after a leg press of 5 x 10 repetitions [resistance exercise (RE)] and after 21 wk (2 times per week) of resistance training (RT). Protein (15 g of whey) or nonenergetic placebo was ingested before and after a single RE bout and each RE workout throughout the RT. The protein group increased its body mass and VL muscle thickness (measured by ultrasonography) already at week 10.5 (P < 0.05). At week 21, the protein and placebo groups had similarly increased their myofiber size. No changes were observed in the nonexercised controls. However, the phosphorylation of p70(S6K) and ribosomal protein S6 (rpS6) were increased at 1 h post-RE measured by Western blotting, the former being the greatest with protein ingestion. Mammalian target of rapamycin (mTOR) phosphorylation was increased after the RE bout and RT only in the protein group, whereas the protein ingestion prevented the post-RE decrease in phosphorylated eukaryotic initiation factor 4E binding protein 1 (p-4E-BP1). Akt phosphorylation decreased after RT, whereas no change was observed in phosphorylated eukaryotic elongation factor 2. A post-RE decrease in muscle myostatin protein occurred only in the placebo group. The results indicate that resistance exercise rapidly increases mTOR signaling and may decrease myostatin protein expression in muscle and that whey protein increases and prolongs the mTOR signaling response.
authors.affiliation: Dept. of Biology of Physical Activity, Univ. of Jyväskylä, P.O. Box 35, 40014 Jyväskylä, Finland. juha.hulmi@sport.jyu.fi
authors.forename: Juha J
authors.initials: JJ
authors.lastname: Hulmi
authors.forename: Jörgen
authors.initials: J
authors.lastname: Tannerstedt
authors.forename: Harri
authors.initials: H
authors.lastname: Selänne
authors.forename: Heikki
authors.initials: H
authors.lastname: Kainulainen
authors.forename: Vuokko
authors.initials: V
authors.lastname: Kovanen
authors.forename: Antti A
authors.initials: AA
authors.lastname: Mero
mesh_terms: D004044:Dietary Proteins; D015444:Exercise / Q000502:physiology*; D006801:Humans; D008297:Male; D008894:Milk Proteins / Q000008:administration & dosage*; D018485:Muscle Fibers, Skeletal / Q000166:cytology / Q000378:metabolism; D055435:Myostatin / Q000378:metabolism*; D051058:Oncogene Protein v-akt / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D038601:Ribosomal Protein S6 / Q000378:metabolism; D038762:Ribosomal Protein S6 Kinases, 70-kDa / Q000378:metabolism; D015398:Signal Transduction; D058570:TOR Serine-Threonine Kinases; D000067816:Whey Proteins
chemical_list: D004044:Dietary Proteins; D008894:Milk Proteins; D055435:Myostatin; D038601:Ribosomal Protein S6; D000067816:Whey Proteins; D011494:Protein Kinases; C546842:MTOR protein, human; D051058:Oncogene Protein v-akt; D038762:Ribosomal Protein S6 Kinases, 70-kDa; D058570:TOR Serine-Threonine Kinases