Cited by 70Muscle Physiology and DisordersMuscle metabolism and nutritionNutrition and Health in Aging

Urolithin B, a Newly Identified Regulator of Skeletal Muscle Mass

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Rodriguez, Julie, Pierre, Nicolas, Naslain, Damien, Bontemps, Françoise, Ferreira, Daneel, Priem, Fabian, Deldicque, Louise, Francaux, Marc·2017·Journal of Cachexia Sarcopenia and Muscle

Abstract

BACKGROUND: The control of muscle size is an essential feature of health. Indeed, skeletal muscle atrophy leads to reduced strength, poor quality of life, and metabolic disturbances. Consequently, strategies aiming to attenuate muscle wasting and to promote muscle growth during various (pathological) physiological states like sarcopenia, immobilization, malnutrition, or cachexia are needed to address this extensive health issue. In this study, we tested the effects of urolithin B, an ellagitannin-derived metabolite, on skeletal muscle growth. METHODS: C2C12 myotubes were treated with 15 μM of urolithin B for 24 h. For in vivo experiments, mice were implanted with mini-osmotic pumps delivering continuously 10 μg/day of urolithin B during 28 days. Muscle atrophy was studied in mice with a sciatic nerve denervation receiving urolithin B by the same way. RESULTS: Our experiments reveal that urolithin B enhances the growth and differentiation of C2C12 myotubes by increasing protein synthesis and repressing the ubiquitin-proteasome pathway. Genetic and pharmacological arguments support an implication of the androgen receptor. Signalling analyses suggest a crosstalk between the androgen receptor and the mTORC1 pathway, possibly via AMPK. In vivo experiments confirm that urolithin B induces muscle hypertrophy in mice and reduces muscle atrophy after the sciatic nerve section. CONCLUSIONS: This study highlights the potential usefulness of urolithin B for the treatment of muscle mass loss associated with various (pathological) physiological states.

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Crossref · 10.1002/jcsm.12190

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  • Urolithin B increases C2C12 myotubes protein synthesis by activating mTORC1 signaling.

    “Urolithin B increases C2C12 myotubes protein synthesis by activating mTORC1 signaling.”
  • In vivo, urolithin B reduces muscle weight loss induced by denervation and inhibits protein degradation by downregulating FoxO1, FoxO3a, MAFbx, and MuRF1.

    “In vivo, urolithin B reduces muscle weight loss induced by denervation and inhibit protein degradation by downregulating the mRNA expression of atrophy-related genes, such as FoxO1, FoxO3a, MAFbx and MuRF1 [96].”

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Authors
Rodriguez, J., Pierre, N., Naslain, D., Bontemps, F., Ferreira, D., Priem, F., Deldicque, L., & Francaux, M.
Affiliations
  • UCLouvain (BE)
  • de Duve Institute (BE)
  • University of Mississippi (US)
  • PROCELL nutrition sprl 2 Rue Jean Burgers 7850 Enghien Belgium
Corresponding author
Francaux, Marc
Venue
Journal of Cachexia Sarcopenia and Muscle
Publisher
Wiley
Published
2017-03
Volume
8
Issue
4
Pages
583-597
ISSN
  • 2190-5991 (ISSN-L)
  • 2190-6009
OpenAlex
W2593660669
Cited by
70
References
54
Citations by year
2026: 9 · 2025: 7 · 2024: 4 · 2023: 9 · 2022: 9 · 2021: 11 · 2020: 10 · 2019: 3 · 2018: 8
FWCI
2.34
Type
journal article
Language
en
Open access
Locations
  • Journal of Cachexia Sarcopenia and Muscle (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • ORBi (University of Liège) (submittedVersion, other-oa)
  • Digital Access to Libraries (Université catholique de Louvain (UCL), l'Université de Namur (UNamur) and the Université Saint-Louis (USL-B)) (submittedVersion, other-oa)
Funders
  • U.S. Department of Agriculture (58‐6408‐2‐0009)
  • Waalse Gewest
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
urolithin B, ellagitannins, skeletal muscle hypertrophy, muscle atrophy, androgen receptor, mTORC1, AMPK, ubiquitin-proteasome system, protein synthesis, sciatic nerve denervation, C2C12 myotubes, cachexia, sarcopenia
MeSH terms
Animals, Cell Differentiation, Cells, Cultured, Coumarins, Female, Male, Mice, Inbred C57BL, Muscle Proteins, Muscular Atrophy, Receptors, Androgen, Signal Transduction, Muscle, Skeletal, Muscle Fibers, Skeletal, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Mice

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