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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Koncarevic A , Jackman RW, and Kandarian SC. Upregulation of ubiquitin-protein ligase Nedd4 in skeletal muscle disuse atrophy. FASEB Summer Research Conference on “Skeletal Muscle Satellite and Stem Cells.” Tucson, AZ, July 26–30, 2003.

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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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