Cited by 7Muscle Physiology and DisordersMuscle metabolism and nutritionSpaceflight effects on biology

Protein Supplementation Enhances the Effects of Intermittent Loading on Skeletal Muscles by Activating the mTORC1 Signaling Pathway in a Rat Model of Disuse Atrophy

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Miyatake, Sho, Hino, Kazuo, Natsui, Yuko, Ebisu, Goro, Fujita, Satoshi·2020·Nutrients

Abstract

Inactivity leads to skeletal muscle atrophy, whereas intermittent loading (IL) during hind limb unloading (HU) attenuates muscle atrophy. However, the combined effects of IL and protein supplementation on disuse muscle atrophy are unclear. Therefore, we investigated the effects of IL and a high-protein oral nutritional supplement (HP) during HU on skeletal muscle mass and protein synthesis/breakdown. Male F344 rats were assigned to the control (CON), 14-day HU (HU), IL during HU (HU + IL), and IL during HU followed by HP administration (2.6 g protein/kg/day; HU + IL + HP) groups. Soleus and gastrocnemius muscles were sampled 30 min after the last IL and HP supplementation. HU decreased relative soleus and gastrocnemius muscle masses. Relative muscle masses and p70 ribosomal protein S6 kinase/ribosomal protein S6 phosphorylation in soleus and gastrocnemius muscles were higher in the HU + IL group than the HU group and further higher in the HU + IL + HP group than the HU + IL group in gastrocnemius muscle. Therefore, protein administration plus IL effectively prevented skeletal muscle atrophy induced by disuse, potentially via enhanced activation of targets downstream of mammalian target of rapamycin complex 1 (mTORC1) signaling pathway.

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Crossref · 10.3390/nu12092729

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  • Oral administration of a high protein liquid nutritional supplement (milk protein, whey protein, leucine, and citrulline) inhibits intermittent loading-induced muscle atrophy and increases muscle mass by activating mTORC1 signaling.

    “Oral administration of a high protein liquid nutritional supplement (milk protein, whey protein, leucine, and citrulline) inhibits intermittent loading-induced muscle atrophy and increases muscle mass by activating the mTORC1 signaling pathway (Ribosomal protein S6 kinase (p70S6K) and ribosomal protein S6 (rpS6)) [20].”

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Authors
Miyatake, S., Hino, K., Natsui, Y., Ebisu, G., & Fujita, S.
Affiliations
  • Otsuka (Japan) (JP)
  • Ritsumeikan University (JP)
Corresponding author
Fujita, Satoshi
Venue
Nutrients
Publisher
MDPI AG
Published
2020-09-07
Volume
12
Issue
9
Pages
2729
ISSN
2072-6643 (ISSN-L)
OpenAlex
W3083349290
Cited by
7
References
44
Citations by year
2026: 2 · 2025: 1 · 2024: 1 · 2023: 1 · 2021: 2
FWCI
0.24
Type
journal article
Language
en
Open access
Locations
  • Nutrients (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Japan Society for the Promotion of Science (17H02183)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
  • Health Sciences › Medicine › Physiology › Spaceflight effects on biology
Keywords
protein supplementation, intermittent loading, disuse atrophy, hindlimb unloading, mTORC1 signaling, skeletal muscle mass, muscle protein synthesis, muscle protein degradation, S6 phosphorylation, soleus muscle, gastrocnemius
MeSH terms
Mechanistic Target of Rapamycin Complex 1, Amino Acids, Animals, Dietary Proteins, Disease Models, Animal, Male, Muscular Atrophy, Phosphorylation, Proteins, Rats, Inbred F344, Signal Transduction, Muscle, Skeletal, Hindlimb Suspension, Dietary Supplements, Muscular Disorders, Atrophic, Ribosomal Protein S6 Kinases, 70-kDa, Rats

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