Cited by 46Muscle Physiology and DisordersExercise and Physiological ResponsesNutrition and Health in Aging

Astaxanthin intake attenuates muscle atrophy caused by immobilization in rats

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Shibaguchi, Tsubasa, Yamaguchi, Yusuke, Miyaji, Nobuyuki, Yoshihara, Toshinori, Naito, Hisashi, Goto, Katsumasa, Ohmori, Daijiro, Yoshioka, Toshitada +1 more·2016·Physiological Reports

Abstract

Astaxanthin is a carotenoid pigment and has been shown to be an effective inhibitor of oxidative damage. We tested the hypothesis that astaxanthin intake would attenuate immobilization-induced muscle atrophy in rats. Male Wistar rats (14-week old) were fed for 24 days with either astaxanthin or placebo diet. After 14 days of each experimental diet intake, the hindlimb muscles of one leg were immobilized in plantar flexion position using a plaster cast. Following 10 days of immobilization, both the atrophic and the contralateral plantaris muscles were removed and analyzed to determine the level of muscle atrophy along with measurement of the protein levels of CuZn-superoxide dismutase (CuZn-SOD) and selected proteases. Compared with placebo diet animals, the degree of muscle atrophy in response to immobilization was significantly reduced in astaxanthin diet animals. Further, astaxanthin supplementation significantly prevented the immobilization-induced increase in the expression of CuZn-SOD, cathepsin L, calpain, and ubiquitin in the atrophied muscle. These results support the postulate that dietary astaxanthin intake attenuates the rate of disuse muscle atrophy by inhibiting oxidative stress and proteolysis via three major proteolytic pathways.

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  • Dietary astaxanthin intake attenuates immobilization-induced muscle atrophy in Wistar rats by inhibiting oxidative stress and proteolysis via lysosomal proteases, calpains, and ubiquitin-proteasome system.

    “Dietary astaxanthin intake attenuates muscle atrophy caused by immobilization in Wistar mice rats by inhibiting oxidative stress and proteolysis via three major proteolytic pathways, including lysosomal proteases, calpains, and the ubiquitin–proteasome system [102].”

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Authors
Shibaguchi, T., Yamaguchi, Y., Miyaji, N., Yoshihara, T., Naito, H., Goto, K., Ohmori, D., Yoshioka, T., & Sugiura, T.
Affiliations
  • Frontier Science and Social Co-creation Initiative, Kanazawa University (JP)
  • Yamaguchi University (JP)
  • Toyo Koso Kagaku Co. Ltd. Urayasu City Chiba Japan
  • Juntendo University (JP)
  • Graduate School of Health and Sports Science Juntendo University Inzai City Chiba Japan
  • Toyohashi SOZO University (JP)
  • Hirosaki Gakuin University (JP)
Corresponding author
Sugiura, Takao
Venue
Physiological Reports
Publisher
Wiley
Published
2016-08
Volume
4
Issue
15
ISSN
2051-817X (ISSN-L)
OpenAlex
W2481215024
Cited by
46
References
39
Citations by year
2026: 1 · 2025: 4 · 2024: 5 · 2023: 6 · 2022: 4 · 2021: 5 · 2020: 8 · 2019: 4 · 2018: 5 · 2017: 3 · 2016: 1
FWCI
2.25
Type
journal article
Language
en
Open access
Locations
  • Physiological Reports (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Health Sciences › Medicine › Rehabilitation › Exercise and Physiological Responses
  • Health Sciences › Medicine › Physiology › Nutrition and Health in Aging
Keywords
astaxanthin, muscle atrophy, immobilization, disuse atrophy, oxidative stress, proteolysis, Cu/Zn superoxide dismutase, cathepsin L, calpain, ubiquitin, plantaris muscle, carotenoid supplementation, hindlimb muscles
MeSH terms
Animals, Antioxidants, Male, Muscular Atrophy, Restraint, Physical, Rats, Wistar, Reactive Oxygen Species, Oxidative Stress, Muscle, Skeletal, Xanthophylls, Rats

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