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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“The loss of protein is due to an increase in protein degradation and to a decrease in protein synthesis (Jackman and Kandarian, 2004).”
Background
Improving In Vitro Myogenesis and Force Production in Engineered Skeletal Muscle Tissues
Syverud, B. C. (2017) · Deep Blue (University of Michigan)
Molecular assessment of muscle health and function : The effect of age, nutrition and physical activity on the human muscle transcriptome and metabolom
Hangelbroek, R. (2017) · doi:10.18174/425481
Efeito do treinamento físico na modulação autonômica cardiovascular e no tecido muscular esquelético em pacientes com cardiopatia chagásica e função sistólica preservada
Cruz, A. S. D. O. (2017) · doi:10.11606/t.5.2017.tde-29112017-080615
Efeito do tratamento quimioterápico sobre a ação da proteína quinase dependente de RNA (PKR) nos sistemas nociceptivo e muscular
Carvalho, A. M. (2018) · doi:10.11606/d.47.2018.tde-18042018-103029
Efeito agudo da hipóxia intermitente no metabolismo de proteínas em músculos esqueléticos de ratos: papel dos glicocorticóides
Przygodda, F. (2017) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.17.2017.tde-12012017-135613
Investigation of ERK inhibition and Hedgehog signaling in myogenesis and cancer-associated muscle wasting
Liu, J. (2018) · IUScholarWorks (Indiana University) · doi:10.7912/c2/2350
Vias de síntese e degradação de proteínas no músculo esquelético após atrofia por desuso: modulação por ácidos graxos ômega-3.
Marzuca-Nassr, G. N. (2017) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.42.2017.tde-10052017-105538
Exercise preconditioning and TFAM overexpression diminish skeletal muscle atrophy.
Theilen, N. T. (2018) · ThinkIR: The University of Louisville's Institutional Repository (University of Louisville) · doi:10.18297/etd/2986 · Cited by 1
“mechanical stress on the muscle tissue occur, leading to potentially abrupt and reductive structural and molecular changes (55).”
Background
Effect of chronic hypoxia on protein metabolism in human skeletal muscle
D’Hulst, G., Ferri, A., Naslain, D., Billaut, F., Marquet, N., Bertrand, L., Horman, S., Francaux, M., Bishop, D. J., & Deldicque, L. (2015)

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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