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The molecular basis of skeletal muscle atrophy
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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“Various stimuli, such as aging, genetics, denervation, starvation, unhealthy lifestyle (i.e., sedentariness, high fat diet (HFD)), systemic pathologies (i.e., diabetes, inflammation, cancer), and long-term drug therapy (i.e., glucocorticoids) are known to further skeletal muscle loss and weakness [2,3,4].”
From Nutraceuticals in the Prevention and Treatment of the Muscle Atrophy (2021) · cites this paper as [3]
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“…Because of the highly disabling impact of muscle weakness and atrophy resulting from disuse, aging, or disease, the mechanisms of such weakness are the targets of intense research (Jackman and Kandarian, 2004; Marzetti et al., 2010; Weiss et al., 2010; Rüegg and Glass, 2011; Romanick et al., 2013).”
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“The early reversal of muscle inhibition during the early phases following surgery is essential for two main reasons: first, molecular and neural alterations lead to muscle atrophy following ACL injury injury (Konishi et al., 2002; Jackman and Kandarian, 2004), and the longer a muscle remains in an atrophy condition th…”
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“…inflammatory cytokines inhibit positive regulators (such as MyoD and IGFI) and induce negative regulators (TNFa and myostatin) of myogenesis (Carlson et al., 1999; Chakravarthy et al., 2000; Dasarathy et al., 2004; Jackman and Kandarian, 2004; Langen et al., 2004; Mourkioti and Rosenthal, 2005).”
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“Muscle atrophy induced by DEX begins with a decrease in myotube diameter, which is reflected by both a decrease in synthesis and an increase in protein degradation [12].”
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“Its major characteristics include the reduction of the myofibre cross-sectional area (CSA) and protein content of skeletal muscle and loss of muscle strength.(1,2) Skeletal muscle atrophy is a condition associated with chronic disease conditions, including neuromuscular diseases, cancer and cachexia.”
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“However, it is possible that the function of conventional shoes such as stabilization and supporting may protect/constraint feet excessively, resulting in the hypofunction or deterioration of the small extrinsic muscle groups in lower extremity (Jackman & Kandarian, 2004; Nigg, 2009).”
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Conditional Activation of MET in Differentiated Skeletal Muscle Induces Atrophy
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“Mechanistically, TNFα induces the generation of reactive oxygen species in the mitochondria and activates nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), signaling the breakdown of proteins in mature muscles, and finally, promotes muscle catabolism through the ubiquitin/proteasome pathway [11,1…”
BackgroundMitochondrial transplantation as a possible therapeutic option for sarcopenia
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“Atrophy begins with a decrease in muscle tension, which is associated with reduced protein synthesis and increased protein degradation (68).”
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“9-fold during fasting and decreased on re-feeding [42], indicating a role for calpain during extended starvation.”
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“Characteristic features of skeletal muscle atrophy include a decrease in fiber cross-sectional area, myofibrillar protein contents, and strength, and it leads to increased fragility and insulin resistance (23, 25, 31).”
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“Particularly, caspases have been identified to participate in muscle atrophy during the initial step by myofibrillar proteolysis and cleavage of actomyosin [34].”
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“Whilst the imbalance caused in all common forms of atrophy between protein synthesis and degradation is paramount in the aetiology of muscle atrophy (Jackman and Kandarian 2004; Lecker et al. 2004), the underpinning molecular mechanisms have yet to be fully defined.”
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“Many previous studies have indicated that protein degradation during unloading occurs principally through the ubiquitin-proteasome pathway [18, 29, 30]; with respect to the ubiquitin-proteasome pathway in the ES+ IM group, not only overexpression of MuRF-1 mRNA but also that of atrogin-1 was inhibited.”
BackgroundInfluentialEffects of toning shoes on lower extremity gait biomechanics
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“In consequence to the relationship of muscle atrophy and reduced muscle tension (Jackman and Kandarian, 2004), suggestions from several researchers have been raised that these shoe concepts may lead to an under-utilization of smaller extrinsic foot muscles and, in respect, cause weakness or even reduced strength if us…”
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“Skeletal muscle atrophy can be induced by a variety of conditions, including starvation, aging, denervation, cancer cachexia, microgravity, and immobilization that can lead to excessive protein degradation [1,2].”
BackgroundDeciphering the microRNA transcriptome of skeletal muscle during porcine development
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Kang, S., Kim, K., Noh, J.-Y., Jung, Y., Bae, O., Lim, K., & Chung, J. (2016) · Thrombosis and Haemostasis · doi:10.1160/th15-11-0858 · Cited by 22
Jang, J., Park, J., Chang, H., & Lim, K. (2016) · Applied Physiology Nutrition and Metabolism · doi:10.1139/apnm-2016-0094 · Cited by 22
“…of muscle atrophy include reduced muscle fiber size and weight and a general shift from slow twitch to fast twitch muscles, which lead to decreased muscle quality and fatigue resistance and can affect health and physical function (Cohen et al. 2009; Jackman and Kandarian 2004; Servais et al. 2007).”
BackgroundTFAM overexpression diminishes skeletal muscle atrophy after hindlimb suspension in mice
Theilen, N. T., Jeremic, N. S., Weber, G. J., & Tyagi, S. C. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.12.015 · Cited by 20
“During all of these scenarios, significant reductions in fiber contraction and mechanical stress on the muscle tissue occur, leading to potentially abrupt and reductive structural and molecular changes (16).”
BackgroundLim, S., Dunlap, K. R., Rosa‐Caldwell, M. E., Haynie, W. S., Jansen, L. T., Washington, T. A., & Greene, N. P. (2020) · Physiological Reports · doi:10.14814/phy2.14608 · Cited by 20
“Muscle atrophy is a pathological dysfunction in protein turnover where an imbalance in protein synthesis and degradation leads to an overall loss in muscle mass and function (Jackman & Kandarian, 2004).”
BackgroundAleman, M. R., & Nieto, J. E. (2010) · American Journal of Veterinary Research · doi:10.2460/ajvr.71.6.664 · Cited by 22
“…cysteine aspartate protease–dependent systems (caspases), lysosomal-dependent systems (cathepsins), non–lysosomal calcium protease–dependent systems (calpains), and ubiquitin-proteasome–dependent systems (ubiquitins) 10,12 These systems may be downregulated or upregulated by triggering signals .”
BackgroundEmerging Role for Linear and Circular Spermine Oxidase RNAs in Skeletal Muscle Physiopathology
Reinoso-Sánchez, J. F., Baroli, G., Duranti, G., Scaricamazza, S., Sabatini, S., Valle, C., Morlando, M., Casero, R. A., Bozzoni, I., Mariottini, P., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218227 · Cited by 24
“It has been reported that SMOX activity maintains basal SM gene expression; indeed a reduction in SMOX is sufficient to induce muscle fiber atrophy [8], that is the wasting or loss of muscle mass resulting in muscle weakness and general muscle fatigue [9,10].”
BackgroundP2Y2 promotes fibroblasts activation and skeletal muscle fibrosis through AKT, ERK, and PKC
Chen, M., Chen, H., Gu, Y., Sun, P., Sun, J., Yu, H., Zheng, H., & Chen, D. (2021) · BMC Musculoskeletal Disorders · doi:10.1186/s12891-021-04569-y · Cited by 21
Yeon, M., Choi, H., Chun, K., Lee, J. H., & Jun, H. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113406 · Cited by 21
Kobak, K. A., Kasztura, M., Dzięgała, M., Bania, J., Kapusniak, V., Banasiak, W., Ponikowski, P. P., & Jankowska, E. A. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3481 · Cited by 21
“Muscle atrophy reflects a systemic response to various chronic conditions, including heart failure (HF) (1,2). disease-associated decreases in the size of muscle tissue can occur as a result of various pathologies and one such reported causative factors is hypoxia (3‑5).”
BackgroundLing, T.-Y., Yi, F., Lü, T., Wang, X.-L., Sun, X., Willis, M. S., Wu, L.-Q., Shen, W.-K., Adelman, J. P., & Lee, H.-C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003837 · Cited by 21
“The UPS is a principal mechanism for cellular protein degradation (9, 10).”
BackgroundComparison between Neurectomy and Botulinum Toxin A Injection for Denervated Skeletal Muscle
Tsai, F., Hsieh, M., & Chou, C. (2010) · Journal of Neurotrauma · doi:10.1089/neu.2010.1320 · Cited by 21
“Neurectomy directly disrupts the continuity of the nerve itself, while BoNT-A denervates muscle by temporarily inhibiting the release of acetylcholine at the neuromuscular junction (NMJ) (Adhihetty et al., 2007; Jackman and Kandarian, 2004).”
Matsushima, Y., Nanri, H., Nara, S., Okufuji, T., Ohta, M., Hachisuka, K., & Ikeda, M. (2006) · Free Radical Research · doi:10.1080/10715760600580488 · Cited by 21
“The direct oxidation and/or oxidative modifications of cellular proteins, however, has been reported to render proteins susceptible to degradation by cellular proteolytic pathways [1,9,11], which may possibly facilitate the muscle breakdown in the late phase of muscle atrophy.”
BackgroundInfluentialEffects of unstable footwear on gait characteristic: A systematic review
Farzadi, M., Nemati, Z., Jalali, M., Doulagh, R. S., & Kamali, M. (2017) · The Foot · doi:10.1016/j.foot.2017.04.005 · Cited by 21
Goswami, A., Jesse, C. M., Chandrasekar, A., Bushuven, E., Vollrath, J. T., Dreser, A., Katona, I., Beyer, C., Johann, S., Feller, A. C., et al. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12164 · Cited by 20
Muscle Disuse Atrophy Caused by Discord of Intracellular Signaling
Ji, L. L., Yeo, D., & Kang, C. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8072 · Cited by 21
“However, recent research reveals that cellular mechanism for each type of atrophy may be different, although a common core pathway may exist (45, 48).”
Muscle ring finger-3 protects against diabetic cardiomyopathy induced by a high fat diet
Quintana, M. T., He, J., Sullivan, J., Grevengoed, T. J., Schisler, J. C., Han, Y., Hill, J. A., Yates, C. C., Stansfield, W. E., Mapanga, R. F., et al. (2015) · BMC Endocrine Disorders · doi:10.1186/s12902-015-0028-z · Cited by 19
“, mono- and di-ubiquitination) substrates [65–67], MuRF3 does not lead to PPAR degradation in the physiological conditions.”
BackgroundMorphological, physiological and behavioural evaluation of a ‘Mice in Space’ housing system
Blottner, D., Serradj, N., Salanova, M., Touma, C., Palme, R., Silva, M., Aerts, J., Berckmans, D., Vico, L., Liu, Y., et al. (2009) · Journal of Comparative Physiology B · doi:10.1007/s00360-008-0330-4 · Cited by 20
Effect of Gonadal Hormones on the Cross‐Sectional Area of Pubococcygeus Muscle Fibers in Male Rat
Alvarado-Olivarez, M., Cuevas‐Romero, E., Lara‐García, M., Camacho, M. Á. M., Carrillo, P., Hudson, R., & Pacheco, P. (2008) · The Anatomical Record · doi:10.1002/ar.20694 · Cited by 20
“The CSA of muscle fibers can change because of a change in the number of myofibrils composing them, a process directly related to protein synthesis in the muscle (Jackman and Kandarian, 2004).”
BackgroundBaumann, C. W., Liu, H. M., & Thompson, L. V. (2016) · PLoS ONE · doi:10.1371/journal.pone.0160839 · Cited by 22
“, proteolysis) exceeding protein synthesis [5, 6].”
Liu, X., Harlow, L., Graham, Z., Bauman, W. A., & Cardozo, C. P. (2016) · Journal of Neurotrauma · doi:10.1089/neu.2016.4763 · Cited by 20
Li, L., Liu, Y.-Y., Chen, N., Chen, Y.-H., Huang, C.-C., Kao, K., Chang, C.-H., Chuang, L., & Chiu, L. (2018) · Laboratory Investigation · doi:10.1038/s41374-018-0081-0 · Cited by 20
Bochud, M., Ponte, B., Pruijm, M. T., Ackermann, D., Guessous, I., Ehret, G., Escher, G., Groessl, M., Younes, S. E., d’Uscio, C. H., et al. (2019) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2018-01942 · Cited by 21
In Utero LPS Exposure Impairs Preterm Diaphragm Contractility
Song, Y., Karisnan, K., Noble, P. B., Berry, C. A., Lavin, T., Moss, T. J. M., Bakker, A. J., Pinniger, G. J., & Pillow, J. J. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2013-0107oc · Cited by 20
Razeghi, P., Wang, M., Youker, K. A., Golfman, L. S., Stepkowski, S. M., & Taegtmeyer, H. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.12.021 · Cited by 20
“P105/p50 has a central role in muscle atrophy because it forms either homodimers during disuse atrophy or heterodimers (with p65) during cachexia-induced atrophy [9].”
BackgroundInfluentialCurto período de imobilização provoca alterações morfométricas e mecânicas no músculo de rato
Lima, S., Caierão, Q. M., Durigan, J. L. Q., Schwarzenbeck, A., Silva, C., Minamoto, V. B., & Guirro, R. (2007) · Brazilian Journal of Physical Therapy · doi:10.1590/s1413-35552007000400009 · Cited by 19
Khayyat, S. G. A., Falsetti, P., Conticini, E., D'Alessandro, R., Bellisai, F., Gentileschi, S., Baldi, C., Bardelli, M., Cantarini, L., & Frediani, B. (2021) · Reumatologia/Rheumatology · doi:10.5114/reum.2021.108430 · Cited by 19
“Although the deleterious effects of GCs on bone [11] and muscle tissues [12] are known, a paper [13] demonstrated that a high dose GC pulse therapy did not lower BMD of RA patients during 18 months of follow-up.”
BackgroundMuscle atrophy in immobilization and senescence in humans
Murton, A. J., & Greenhaff, P. L. (2009) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32832f15e1 · Cited by 19
Changes to Metabolism and Cell Physiology that Enable Mammalian Hibernation
Klug, B. J., & Brigham, R. M. (2015) · Springer Science Reviews · doi:10.1007/s40362-015-0030-x · Cited by 19
“sion of myostatin, a protein that inhibits growth and differentiation of muscle tissue, causing muscle atrophy [115].”
BackgroundProteomic profiling of skeletal muscle plasticity.
Ohlendieck, K. (2011) · Europe PMC (PubMed Central) · Cited by 19
Electrical stimulation delays reinnervation in denervated rat muscle
Pinheiro-Dardis, C. M., Erbereli, B. T., Gigo‐Benato, D., Castro, P. A. T. D. S., & Russo, T. L. (2017) · Muscle & Nerve · doi:10.1002/mus.25589 · Cited by 19
“Furthermore, with regard to muscle protein synthesis and degradation, there is a reduction in the synthesis and increase in protein degradation following PNI, leading to muscle mass loss.(24) The expression of muscle-specific genes involved in the ubiquitin-proteasome pathway, such as MuRF1 and MAFBx (atrogin-1), is i…”
BackgroundKanazashi, M., Tanaka, M., Nakanishi, R., Maeshige, N., & Fujino, H. (2019) · The Journal of Physiological Sciences · doi:10.1007/s12576-019-00692-7 · Cited by 20
Skeletal Muscle Aging Atrophy: Assessment and Exercise-Based Treatment
Marzuca-Nassr, G. N., SanMartín-Calísto, Y., Guerra-Vega, P., Artigas-Arias, M., Alegría, A., & Curi, R. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-42667-5_6 · Cited by 20
H19X‐encoded miR‐322(424)/miR‐503 regulates muscle mass by targeting translation initiation factors
Liang, R., Shen, X., Wang, F., Wang, X., DesJarlais, A., Syed, A., Saba, R., Tan, Z., Yu, F., Ji, X., et al. (2021) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12827 · Cited by 19
“Muscle loss also contributes to decreased quality of life in ageing.(1,2) Muscle atrophy results from a reduced rate of protein synthesis, accelerated protein degradation, or both.”
BackgroundNishimura, M., Mikura, M., Hirasaka, K., Okumura, Y., Nikawa, T., Kawano, Y., Nakayama, M., & Ikeda, M. (2008) · The Journal of Biochemistry · doi:10.1093/jb/mvn126 · Cited by 19
Exercise preconditioning attenuates atrophic mediators and preserves muscle mass in acute sepsis
Al‐Nassan, S., & Fujino, H. (2018) · General Physiology and Biophysics · doi:10.4149/gpb_2018001 · Cited by 19
“LPS administration induces a number of catabolic factors in sepsis, including tumor necrosis factoralpha (TNF-α), which promotes muscle wasting in diseased states (Ahmad et al. 1994; Jackman and Kandarian 2004).”
BackgroundRegulation of cell proliferation and differentiation in the kidney
Neil, I. A. (2009) · Frontiers in bioscience · doi:10.2741/3582 · Cited by 19
“Moreover, TNF could also partially explain the wasting phenotype (62-63).”
BackgroundRoberston, M. J., Raghunathan, S., Potaman, V. N., Zhang, F., Stewart, M. D., McConnell, B. K., & Schwartz, R. J. (2019) · The FASEB Journal · doi:10.1096/fj.201901107rr · Cited by 18
“IGF1Eb ATCTACCAACAAGAACACG NM_001111285 (1)”
Influential
Metadata
- 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
- 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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