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Oxidative stress and disuse muscle atrophy
Abstract
Skeletal muscle inactivity is associated with a loss of muscle protein and reduced force-generating capacity. This disuse-induced muscle atrophy results from both increased proteolysis and decreased protein synthesis. Investigations of the cell signaling pathways that regulate disuse muscle atrophy have increased our understanding of this complex process. Emerging evidence implicates oxidative stress as a key regulator of cell signaling pathways, leading to increased proteolysis and muscle atrophy during periods of prolonged disuse. This review will discuss the role of reactive oxygen species in the regulation of inactivity-induced skeletal muscle atrophy. The specific objectives of this article are to provide an overview of muscle proteases, outline intracellular sources of reactive oxygen species, and summarize the evidence that connects oxidative stress to signaling pathways contributing to disuse muscle atrophy. Moreover, this review will also discuss the specific role that oxidative stress plays in signaling pathways responsible for muscle proteolysis and myonuclear apoptosis and highlight gaps in our knowledge of disuse muscle atrophy. By presenting unresolved issues and suggesting topics for future research, it is hoped that this review will serve as a stimulus for the expansion of knowledge in this exciting field.
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Essentials of Mechanical Ventilation
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Degradation of sarcomeric and cytoskeletal proteins in cultured skeletal muscle cells
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Role of iron in oxidative stress in skeletal muscle atrophied by immobilization
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Interplay of stress and physical inactivity on muscle loss: nutritional countermeasures
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Apoptotic signaling in skeletal muscle fibers during atrophy
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Increased antioxidant capacity does not attenuate muscle atrophy caused by unweighting
Koesterer, T. J., DODD, S. L., & Powers, S. K. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00511.2002 · Cited by 71
Self-citationClenbuterol antagonizes glucocorticoid‐induced atrophy and fibre type transformation in mice
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Antioxidant enzyme systems in skeletal muscle atrophied by immobilization
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Hydroxyl radical generation in skeletal muscle atrophied by immobilization
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Denervation-induced changes in myosin heavy chain expression in the rat diaphragm muscle
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Inhibition of protein synthesis in cortical neurons during exposure to hydrogen peroxide
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Allopurinol mitigates muscle contractile dysfunction caused by hindlimb unloading in mice.
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Influence of corticosteroids on myonuclear domain size in the rat diaphragm muscle
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9 Ubiquitin-Proteasome Pathway of Intracellular Protein Degradation
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Diaphragmatic nitric oxide synthase is not induced during mechanical ventilation
Gammeren, D. V., Falk, D. J., Deering, M. A., DeRuisseau, K. C., & Powers, S. K. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00043.2006 · Cited by 21
Self-citationHeme oxygenase-1: a key step in counteracting cellular dysfunction.
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PROTEIN SYNTHESIS AND MYOSIN HEAVY CHAIN mRNA IN THE RAT DIAPHRAGM DURING MECHANICAL VENTILATION
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Cited by
Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production
Powers, S. K., & Jackson, M. J. (2008) · Physiological Reviews · doi:10.1152/physrev.00031.2007 · Cited by 2,459
Self-citationExercise is the real polypill.
Fiuza-Luces, C., Garatachea, N., Berger, N. A., & Lucia, A. (2013) · Physiology · doi:10.1152/physiol.00019.2013 · Cited by 791
Skeletal muscle: A review of molecular structure and function, in health and disease
Mukund, K., & Subramaniam, S. (2020) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1462 · Cited by 664
Varanita, T., Soriano, M. E., Romanello, V., Zaglia, T., Quintana-Cabrera, R., Semenzato, M., Menabò, R., Costa, V., Civiletto, G., Pesce, P., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.007 · Cited by 460
Reactive Oxygen Species Are Signalling Molecules for Skeletal Muscle Adaptation
Powers, S. K., Duarte, J., Kavazis, A. N., & Talbert, E. E. (2010) · Experimental Physiology · doi:10.1113/expphysiol.2009.050526 · Cited by 440
Self-citation
Metadata
- Authors
- Powers, S. K., Kavazis, A. N., & McClung, J. M.
- Venue
- Journal of Applied Physiology
- Publisher
- American Physiological Society
- Published
- 2007-06
- Volume
- 102
- Issue
- 6
- Pages
- 2389-2397
- ISSN
- 0161-7567 (ISSN-L)
- 8750-7587
- 1522-1601
- OpenAlex
- W2156251255
- Cited by
- 472
- References
- 127
- FWCI
- 12.21
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
