Cited by 52Muscle Physiology and DisordersMuscle metabolism and nutritionNutrition and Health in Aging

Soluble Whey Protein Hydrolysate Ameliorates Muscle Atrophy Induced by Immobilization via Regulating the PI3K/Akt Pathway in C57BL/6 Mice

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Shin, Ji Eun, Park, Seok Jun, Ahn, Seung Il, Choung, Se-Young·2020·Nutrients

Abstract

Sarcopenia, a loss of skeletal muscle mass and function, is prevalent in older people and associated with functional decline and mortality. Protein supplementation is necessary to maintain skeletal muscle mass and whey protein hydrolysates have the best nutrient quality among food proteins. In the first study, C57BL/6 mice were subjected to immobilization for 1 week to induce muscle atrophy. Then, mice were administered with four different whey protein hydrolysates for 2 weeks with continuous immobilization. Among them, soluble whey protein hydrolysate (WP-S) had the greatest increase in grip strength, muscle weight, and cross-sectional area of muscle fiber than other whey protein hydrolysates. To investigate the molecular mechanism, we conducted another experiment with the same experimental design. WP-S significantly promoted the phosphoinositide 3-kinase (PI3K)/protein kinase B (Akt)/mammalian target of rapamycin (mTOR) pathway and inhibited the PI3K/Akt/forkhead box O (FoxO) pathway. In addition, it increased myosin heavy chain (MyHC) expression in both the soleus and quadriceps and changed MyHC isoform expressions. In conclusion, WP-S attenuated muscle atrophy induced by immobilization by enhancing the net protein content regulating muscle protein synthesis and degradation. Thus, it is a necessary and probable candidate for developing functional food to prevent sarcopenia.

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  • Soluble whey protein hydrolysate increases grip strength, muscle mass, and cross-sectional area of muscle fiber and ameliorates immobilization-induced C57BL/6 mice muscle atrophy via regulating PI3K/Akt pathway.

    “Shin et al. reported that soluble whey protein hydrolysate increases grip strength, muscle mass, and cross-sectional area of muscle fiber and meliorates immobilization-induced C57BL/6 mice muscle atrophy via regulating the PI3K/Akt pathway [21].”

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Authors
Shin, J. E., Park, S. J., Ahn, S. I., & Choung, S.-Y.
Affiliations
  • Department of Life and Nanopharmaceutical Sciences, Graduate School, Kyung Hee University, Seoul 02447, Korea
  • Health & Nutrition R&D Group, Maeil Dairies Co., Ltd., Gyeonggi 17714, Korea
  • Neocremar R&D Center, 211, Jungdae-ro, Songpa-gu, Seoul 05702, Korea
  • Kyung Hee University (KR)
Corresponding author
Choung, Se-Young
Venue
Nutrients
Publisher
MDPI AG
Published
2020-11-01
Volume
12
Issue
11
Pages
3362
ISSN
2072-6643 (ISSN-L)
OpenAlex
W3095171489
Cited by
52
References
49
Citations by year
2026: 8 · 2025: 13 · 2024: 9 · 2023: 11 · 2022: 7 · 2021: 4
FWCI
1.78
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
Ministry of Science & ICT (2018M3A9F3081447)
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 › Nutrition and Health in Aging
Keywords
muscle atrophy, immobilization, sarcopenia, PI3K/AKT/mTOR pathway, FoxO signaling, myosin heavy chain isoforms, muscle protein synthesis, muscle protein degradation, grip strength, functional foods
MeSH terms
Whey Proteins, Animals, Mice, Inbred C57BL, Muscle Proteins, Muscular Atrophy, Protein Hydrolysates, Protein Biosynthesis, Signal Transduction, Muscle, Skeletal, Hindlimb Suspension, Proto-Oncogene Proteins c-akt, Mice, Forkhead Transcription Factors, Sarcopenia, Phosphatidylinositol 3-Kinase, TOR Serine-Threonine Kinases, Proteolysis

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