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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.
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“acute increases in mTOR signaling markers following one bout of resistance exercise are associated with muscle hypertrophy following weeks of resistance training (Terzis et al., 2008; Hulmi et al., 2009; Mayhew et al., 2009; Mitchell et al., 2013)”
From Skeletal Muscle Ribosome and Mitochondrial Biogenesis in Response to Different Exercise Training Modalities (2021) · cites this paper as Hulmi et al., 2009
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Metadata
- Authors
- Hulmi, J. J., Tannerstedt, J., Selänne, H., Kainulainen, H., Kovanen, V., & Mero, A. A.
- Affiliations
- University of Jyväskylä (FI)
- Venue
- Journal of Applied Physiology
- Publisher
- American Physiological Society
- Published
- 2009-05
- Volume
- 106
- Issue
- 5
- Pages
- 1720-1729
- ISSN
- 0161-7567 (ISSN-L)
- 8750-7587
- 1522-1601
- OpenAlex
- W2095678778
- Cited by
- 163
- References
- 59
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 7 · 2023: 5 · 2022: 7 · 2021: 4 · 2020: 5 · 2019: 8 · 2018: 8 · 2017: 12 · 2016: 5 · 2015: 16 · 2014: 13 · 2013: 12 · 2012: 22
- FWCI
- 7.12
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Applied Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ellen ja Artturi Nyyssösen Säätiö
- Kela
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Orthopedics and Sports Medicine › Sports Performance and Training
- Keywords
- resistance training, mTOR signaling, myostatin, muscle hypertrophy, p70S6K phosphorylation, ribosomal protein S6, 4E-BP1, Akt phosphorylation, elongation factor 2, vastus lateralis, muscle fiber size, protein supplementation
- MeSH terms
- Whey Proteins, Dietary Proteins, Humans, Male, Milk Proteins, Phosphorylation, Protein Kinases, Signal Transduction, Exercise, Muscle Fibers, Skeletal, Ribosomal Protein S6, Ribosomal Protein S6 Kinases, 70-kDa, Oncogene Protein v-akt, Myostatin, TOR Serine-Threonine Kinases
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