Cited by 1,008Muscle Physiology and DisordersMuscle metabolism and nutritionNutrition and Health in Aging

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The molecular basis of skeletal muscle atrophy

Jackman, Robert W., Kandarian, Susan C.·2004·American Journal of Physiology-Cell Physiology

DOI 10.1152/ajpcell.00579.2003

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Abstract

Skeletal muscle atrophy attributable to muscular inactivity has significant adverse functional consequences. While the initiating physiological event leading to atrophy seems to be the loss of muscle tension and a good deal of the physiology of muscle atrophy has been characterized, little is known about the triggers or the molecular signaling events underlying this process. Decreases in protein synthesis and increases in protein degradation both have been shown to contribute to muscle protein loss due to disuse, and recent work has delineated elements of both synthetic and proteolytic processes underlying muscle atrophy. It is also becoming evident that interactions among known proteolytic pathways (ubiquitin-proteasome, lysosomal, and calpain) are involved in muscle proteolysis during atrophy. Factors such as TNF-alpha, glucocorticoids, myostatin, and reactive oxygen species can induce muscle protein loss under specified conditions. Also, it is now apparent that the transcription factor NF-kappaB is a key intracellular signal transducer in disuse atrophy. Transcriptional profiles of atrophying muscle show both up- and downregulation of various genes over time, thus providing further evidence that there are multiple concurrent processes involved in muscle atrophy. The purpose of this review is to synthesize our current understanding of the molecular regulation of muscle atrophy. We also discuss how ongoing work should uncover more about the molecular underpinnings of muscle wasting, particularly that due to disuse.

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Cai, W., Zhang, Y., Chang, T., Wang, Z., Zhu, B., Chen, Y., Gao, X., Xu, L., Zhang, L., Gao, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26588436
Additional file 1 of The eQTL colocalization and transcriptome-wide association study identify potentially causal genes responsible for economic traits in Simmental beef cattle
Cai, W., Zhang, Y., Chang, T., Wang, Z., Zhu, B., Chen, Y., Gao, X., Xu, L., Zhang, L., Gao, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26588403
Additional file 19 of The eQTL colocalization and transcriptome-wide association study identify potentially causal genes responsible for economic traits in Simmental beef cattle
Cai, W., Zhang, Y., Chang, T., Wang, Z., Zhu, B., Chen, Y., Gao, X., Xu, L., Zhang, L., Gao, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26588457
Additional file 15 of The eQTL colocalization and transcriptome-wide association study identify potentially causal genes responsible for economic traits in Simmental beef cattle
Cai, W., Zhang, Y., Chang, T., Wang, Z., Zhu, B., Chen, Y., Gao, X., Xu, L., Zhang, L., Gao, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26588445
Additional file 1 of The role of proteasome in muscle wasting of experimental arthritis
Teixeira, V. O. N., Bartikoski, B. J., do Espirito Santo, R. C., Alabarse, P. V. G., Ghannan, K., Silva, J. M. S., Filippin, L. I., Visioli, F., Martinez-Gamboa, L., Feist, E., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26576804
Additional file 5 of The eQTL colocalization and transcriptome-wide association study identify potentially causal genes responsible for economic traits in Simmental beef cattle
Cai, W., Zhang, Y., Chang, T., Wang, Z., Zhu, B., Chen, Y., Gao, X., Xu, L., Zhang, L., Gao, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26588415
Additional file 17 of The eQTL colocalization and transcriptome-wide association study identify potentially causal genes responsible for economic traits in Simmental beef cattle
Cai, W., Zhang, Y., Chang, T., Wang, Z., Zhu, B., Chen, Y., Gao, X., Xu, L., Zhang, L., Gao, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26588451
Additional file 4 of The eQTL colocalization and transcriptome-wide association study identify potentially causal genes responsible for economic traits in Simmental beef cattle
Cai, W., Zhang, Y., Chang, T., Wang, Z., Zhu, B., Chen, Y., Gao, X., Xu, L., Zhang, L., Gao, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26588412
Additional file 7 of The eQTL colocalization and transcriptome-wide association study identify potentially causal genes responsible for economic traits in Simmental beef cattle
Cai, W., Zhang, Y., Chang, T., Wang, Z., Zhu, B., Chen, Y., Gao, X., Xu, L., Zhang, L., Gao, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26588421
Additional file 6 of The eQTL colocalization and transcriptome-wide association study identify potentially causal genes responsible for economic traits in Simmental beef cattle
Cai, W., Zhang, Y., Chang, T., Wang, Z., Zhu, B., Chen, Y., Gao, X., Xu, L., Zhang, L., Gao, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26588418
Additional file 26 of The eQTL colocalization and transcriptome-wide association study identify potentially causal genes responsible for economic traits in Simmental beef cattle
Cai, W., Zhang, Y., Chang, T., Wang, Z., Zhu, B., Chen, Y., Gao, X., Xu, L., Zhang, L., Gao, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26588478
Additional file 9 of The eQTL colocalization and transcriptome-wide association study identify potentially causal genes responsible for economic traits in Simmental beef cattle
Cai, W., Zhang, Y., Chang, T., Wang, Z., Zhu, B., Chen, Y., Gao, X., Xu, L., Zhang, L., Gao, H., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26588427
Morphological and Functional Evaluation of Rat Leg Muscles under the Influence of Hindlimb Unloading, Tenotomy, and Denervation
Sabirova, D. E., Shadrina, A. A., Eremeev, A. A., Khairullin, A. E., & Baltina, T. (2026) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747825700606
“In addition, age-related changes, malnutrition, and hormonal imbalances can lead to muscle atrophy [6–8].”
Gait analysis for functional evaluation in a surgical hindlimb suspension model of muscle atrophy
Xu, Y., Zhang, Z., Chen, P., Kellon, N., He, A., Alizai, U., Lee, S., Sathish, K., Yan, Z., Zhou, X., et al. (2026) · The Journal of Physiology · doi:10.1113/jp289401
“Muscle mass loss can occur rapidly during periods of unloading, with older individuals being particularly vulnerable to functional deterioration and incomplete recovery (Jackman & Kandarian, 2004; Mitchell et al., 2012; Mulavara et al., 2018).”
Exercise as an epigenetic modulator: Remodeling DNA methylation and gene expression in skeletal muscle
Nalli, R., Elumalai, S., Raavi, V., & Likhit, M. (2026) · Gene Reports · doi:10.1016/j.genrep.2026.102464
Burn injury dysregulates protein signaling in type 1 and type 2 muscles in rats
Dombrecht, D., Daele, U. V., Asbroeck, B. V., Schieffelers, D. R., Guns, P., & van Breda, E. (2026) · Burns · doi:10.1016/j.burns.2026.107948
Obestatin: canonical and unexpected functions
Santos‐Zas, I., Gurriarán‐Rodríguez, U., Cid-Diaz, T., Leal‐López, S., Casanueva, F. F., Pazos-Randulfe, Y., & Camiña, J. P. (2026) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-026-10021-0
“Muscle atrophy is the wasting or thinning of muscle mass [95, 96].”
Implication des céramides dans l'atrophie musculaire
Larichaudy, J. D. (2012) · theses.fr (ABES) · doi:10.70675/b97ff403z6fa7z464fzb67czaa56e3753d9e
Atrophie musculaire et récupération : homéostasie calcique, stress oxydant, apoptose et protéolyse musculaire
Andrianjafiniony, T. (2010) · theses.fr (ABES) · doi:10.70675/e8e80863z024fz49b2z87c6zd4ee4c88a3d6
Role of p53 in muscle wasting
de Abreu, P. A. (2016) · theses.fr (ABES) · doi:10.70675/a49b7f77z1189z425fz86b8z8ee9f8fa327a
Déconditionnement et régénération du muscle strié squelettique : rôle du niveau d’activité contractile sur le développement d’infiltrations graisseuses
Pagano, A. F. (2016) · theses.fr (ABES) · doi:10.70675/b2e8ea4ez5cd3z43a4zae84z3a8e6d8c661f
Étude des modifications sub-cellulaires associées au vieillissement musculaire chez Caenorhabditis elegans-Rôle du facteur de transcription UNC-120/SRF
Lamarche, A. M. D. (2016) · theses.fr (ABES) · doi:10.70675/9ce6267dz94c3z4e2ez8a69z5f6b5ac9b808
Le métabolisme lipidique dans les altérations mitochondriales induites par l’absence de myostatine : impact de l’entrainement en endurance
Baati, N. (2018) · theses.fr (ABES) · doi:10.70675/59794f12z6d4ez48dbz9978zef6be22f62d2

Authors: Jackman, R. W., & Kandarian, S. C.
Affiliations: Boston University (US)
Venue: American Journal of Physiology-Cell Physiology
Publisher: American Physiological Society
Published: 2004-10
Volume: 287
Issue: 4
Pages: C834-C843
ISSN: 0363-6143 (ISSN-L)
1522-1563
DOI: 10.1152/ajpcell.00579.2003
OpenAlex: W2127808488
Cited by: 1,008
References: 118
Citations by year: 2026: 18 · 2025: 21 · 2024: 53 · 2023: 34 · 2022: 33 · 2021: 35 · 2020: 45 · 2019: 50 · 2018: 38 · 2017: 41 · 2016: 52 · 2015: 59 · 2014: 49 · 2013: 64 · 2012: 49
FWCI: 3.83
Type: journal article
Language: en
Open access: closed
Locations: American Journal of Physiology-Cell Physiology (publishedVersion)
PubMed (publishedVersion)
Funders: National Space Biomedical Research Institute
National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01 AR-41705, R01AR041705)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Health Sciences › Medicine › Physiology (medical) › Nutrition and Health in Aging
Keywords: skeletal muscle atrophy, disuse atrophy, muscle protein degradation, muscle protein synthesis, ubiquitin-proteasome system, lysosomal proteolysis, calpain, TNF-α, glucocorticoids, myostatin, reactive oxygen species, NF-κB, transcriptional regulation, muscle atrophy
MeSH terms: Muscle Proteins, Muscular Atrophy, Transcription, Genetic, Signal Transduction, Gene Expression, NF-kappa B, Muscle, Skeletal, Muscular Disorders, Atrophic

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The molecular basis of skeletal muscle atrophy

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