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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“Muscle protein degradation is a complex process implicating four systems: the lysosomal proteases (cathepsins), the calcium-dependent proteases (calpains), the caspases and the ubiquitin–proteasome pathway (Jackman & Kandarian 2004).”
BackgroundMethod
Role of the ubiquitin-proteasome pathway in muscle atrophy in cachexia
Attaix, D., Combaret, L., Béchet, D., & Taillandier, D. (2008) · Current Opinion in Supportive and Palliative Care · doi:10.1097/spc.0b013e3283196ac2 · Cited by 56
CALPAIN activity is increased in skeletal muscle from gastric cancer patients with no or minimal weight loss
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“tion and proteasome-dependent degradation of the myofilaments.(13,14,30,31) Although the present results”
Result
Evidences of apoptosis during the early phases of soleus muscle atrophy in hindlimb suspended mice
Ferreira, R. M., Neuparth, M. J., Vitorino, R. M. P., Appell, H.-J., Amado, F. M. L., & Duarte, J. (2008) · Physiological Research · doi:10.33549/physiolres.931272 · Cited by 56
Reloading Functionally Ameliorates Disuse-Induced Muscle Atrophy by Reversing Mitochondrial Dysfunction, and Similar Benefits Are Gained by Administering a Combination of Mitochondrial Nutrients
Liu, J., Peng, Y., Feng, Z., Shi, W., Qu, L., Li, Y., Liu, J., & Long, J. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.01.003 · Cited by 55
“3 Introduction 1 Muscle atrophy is induced by an initial repression of protein synthesis, followed by a 2 constant induction of protein degradation (1-4).”
Background
Factors Limiting Exercise Tolerance in Chronic Lung Diseases
Vogiatzis, I., & Zakynthinos, S. (2012) · Comprehensive Physiology · doi:10.1002/cphy.c110015 · Cited by 77
“The interaction of Ik-B masks the nuclear localization sequence of the NF-kB complex, thereby preventing nuclear translocation and maintaining NF-kB in an inactive state in the cytoplasmic compartment (132, 161).”
The possible role of myostatin in skeletal muscle atrophy and cachexia
Jespersen, J., Kjær, M., & Schjerling, P. (2005) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2005.00498.x · Cited by 55
“…agents (e.g., tumor necrosis factor a, interleukins-1 and -6) is, however, beyond the scope of this short review, and interested readers may consult other references for details (Kotler, 2000; Anker & Sharma, 2002; Tisdale, 2002; Argiles et al., 2003; Jackman & Kandarian, 2004; Frost & Lang, 2005).”
Background
Cycle training induces muscle hypertrophy and strength gain: strategies and mechanisms
Ozaki, H., Loenneke, J. P., Thiebaud, R. S., & Abe, T. (2015) · Acta Physiologica Hungarica · doi:10.1556/aphysiol.102.2015.1.1 · Cited by 53
“Among these systems, UPS plays a prominent role in muscle protein breakdown (3, 38) through the elevated expressions of muscle-specific ubiquitin ligases: Atrogin-1 and muscle ring finger 1 (MuRF1) (6, 26).”
Background
Pathophysiology of exercise intolerance in pulmonary arterial hypertension
Tran, D., Lau, E., Celermajer, D. S., Davis, G. M., & Cordina, R. (2017) · Respirology · doi:10.1111/resp.13141 · Cited by 55
Conditional over-expression of PITX1 causes skeletal muscle dystrophy in mice
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“In addition to the myofiber atrophy that occurs in some inherited muscle diseases (Emery, 2002), skeletal muscle atrophy occurs when the muscle is disused, immobilized, denerved and during starvation (Andersen et al., 1999; Jagoe et al., 2002; Jackman and Kandarian, 2004).”
Changes in muscle fiber contractility and extracellular matrix production during skeletal muscle hypertrophy.
Mendias, C., Schwartz, A. J., Grekin, J. A., Gumucio, J., & Sugg, K. (2017) · Journal of applied physiology · doi:10.1152/japplphysiol.00719.2016 · Cited by 48
“The calpains, which are critical in the disassembly of mechanically damaged sarcomeres (19), and the E3 ubiquitin ligases atrogin-1, MuRF-1, and MuSA-1, which target damaged proteins to the 26S proteasome for proteolytic breakdown (35), were upregulated at the 3- and 7-day time points.”
Background
Reactive nitrogen species induce nuclear factor-κB-mediated protein degradation in skeletal muscle cells
Bar‐Shai, M., & Reznick, A. Z. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.02.009 · Cited by 53
NF-κB activation by depolarization of skeletal muscle cells depends on ryanodine and IP3 receptor-mediated calcium signals
Valdés, J. A., Hidalgo, J., Galaz, J. L., Puentes, N., Silva, M. G., Jaimovich, E., & Carrasco, M. A. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00320.2006 · Cited by 53
“activation of this factor is seen in response to muscle disuse and in cachexia (28, 35).”
BackgroundMethod
Depressed mitochondrial biogenesis and dynamic remodeling in mouse tibialis anterior and gastrocnemius induced by 4‐week hindlimb unloading
Liu, J., Peng, Y., Cui, Z., Wu, Z., Qian, A., Shang, P., Qu, L., Li, Y., Liu, J., & Long, J. (2012) · IUBMB Life · doi:10.1002/iub.1087 · Cited by 54
“Muscle atrophy is frequently observed in diseases, fasting, and disuse conditions such as limb immobilization, hindlimb unloading (HU), denervated conditions, chronic bed rest, and space flight (1, 2).”
Background
Effect of flywheel-based resistance exercise on processes contributing to muscle atrophy during unloading in adult rats
Dupont‐Versteegden, E. E., Fluckey, J. D., Knox, M., Gaddy, D., & Peterson, C. A. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01540.2005 · Cited by 53
“Other changes that occur during disuse atrophy that play an important role in the loss of muscle mass include 1) an increase in protein degradation, 2) an elevation of apoptosis, and 3) a decrease in cell proliferation (1, 10, 13, 19, 29).”
TRAF6 Inhibition Rescues Dexamethasone-Induced Muscle Atrophy
Sun, H., Gong, Y., Qiu, J., Chen, Y., Ding, F., & Zhao, Q. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150611126 · Cited by 52
“biochemical process occurring under various pathophysiological conditions, such as aging, disuse, starvation, severe injury, sepsis, cancer and other cachectic diseases [1–4].”
Background
Skeletal muscle atrophy increases cell proliferation in mice gastrocnemius during the first week of hindlimb suspension
Ferreira, R. M., Neuparth, M. J., Ascensão, A. A. M. R., Magalhães, J., Vitorino, R. M. P., Duarte, J. A., & Amado, F. M. L. (2006) · European Journal of Applied Physiology · doi:10.1007/s00421-006-0197-6 · Cited by 52
“These include hindlimb suspension, spaceXight, bed rest, denervation, and spinal cord transsection (Mitchell and Pavlath 2001; Jackman and Kandarian 2004).”
Background
Microarray analysis of the temporal response of skeletal muscle to methylprednisolone: comparative analysis of two dosing regimens
Almon, R. R., DuBois, D. C., Yao, Z., Hoffman, E. P., Ghimbovschi, S. D., & Jusko, W. J. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00242.2006 · Cited by 52
IL-6 and the dysregulation of immune, bone, muscle, and metabolic homeostasis during spaceflight
Smith, J. K. (2018) · npj Microgravity · doi:10.1038/s41526-018-0057-9 · Cited by 56
Sabinene Prevents Skeletal Muscle Atrophy by Inhibiting the MAPK–MuRF-1 Pathway in Rats
Ryu, Y., Lee, D., Jung, S. H., Lee, K.-J., Jin, H., Kim, S. J., Lee, H. M., Kim, B., & Won, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194955 · Cited by 53
“The ubiquitin–proteasome system is the major regulatory mechanism of muscle protein breakdown associated with skeletal muscle atrophy [6,7].”
Background
Trophic action of sphingosine 1-phosphate in denervated rat soleus muscle
Zanin, M., Germinario, E., Libera, L. D., Sandonà, D., Sabbadini, R. A., Betto, R., & Danieli‐Betto, D. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00164.2007 · Cited by 51
“Muscle atrophy is characterized by accelerated proteolysis, mainly via the ubiquitin-proteasome pathway (28), leading to progressive and severe reduction of muscle mass and alteration of contractile properties (21, 37).”
Salmonid genomes have a remarkably expanded akirin family, coexpressed with genes from conserved pathways governing skeletal muscle growth and catabolism
Macqueen, D. J., Kristjánsson, B. K., & Johnston, I. A. (2010) · Physiological Genomics · doi:10.1152/physiolgenomics.00045.2010 · Cited by 51
The effect of calorie restriction on mouse skeletal muscle is sex, strain and time-dependent
Boldrin, L., Ross, J. A., Whitmore, C. L., Doreste, B., Beaver, C., Eddaoudi, A., Pearce, D. J., & Morgan, J. E. (2017) · Scientific Reports · doi:10.1038/s41598-017-04896-y · Cited by 51
The role of mitochondria in redox signaling of muscle homeostasis
Ji, L. L., Yeo, D., Kang, C., & Zhang, T. (2020) · Journal of sport and health science/Journal of Sport and Health Science · doi:10.1016/j.jshs.2020.01.001 · Cited by 51
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. (2023) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-023-00876-7 · Cited by 53
USP19-deubiquitinating enzyme regulates levels of major myofibrillar proteins in L6 muscle cells
Sundaram, P., Pang, Z., Miao, M., Yu, L., & Wing, S. S. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00409.2009 · Cited by 50
TGF-β requires the activation of canonical and non-canonical signalling pathways to induce skeletal muscle atrophy
Ábrigo, J., Campos, F., Simón, F., Riedel, C. A., Cabrera, D., Vilos, C., & Cabello‐Verrugio, C. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0217 · Cited by 50
“Skeletal muscle atrophy is a pathological condition characterised by a loss of strength and muscle mass with concomitant degradative pathway activation and anabolic pathway inhibition, which produces weakness (Jackman and Kandarian, 2004; Glass, 2005).”
Background
Effect of branched-chain amino acid supplementation during unloading on regulatory components of protein synthesis in atrophied soleus muscles
Bajotto, G., Sato, Y., Kitaura, Y., & Shimomura, Y. (2011) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1825-8 · Cited by 50
“Conversely, the ATP-dependent ubiquitin– proteasome pathway is constitutively active in muscle fibers and, during muscle inactivity, predominantly deals with degradation of cleaved myofibrillar proteins (Jackman and Kandarian 2004; Taillandier et al. 1996).”
Background
Sarcopenia or muscle modifications in neurologic diseases: a lexical or patophysiological difference?
Carda, S., Cisari, C., & Invernizzi, M. (2013) · PubMed · Cited by 49
Expression of Atrophy mRNA Relates to Tendon Tear Size in Supraspinatus Muscle
Schmutz, S., Fuchs, T. J., Regenfelder, F., Steinmann, P., Zumstein, M. A., & Fuchs, B. (2008) · Clinical Orthopaedics and Related Research · doi:10.1007/s11999-008-0565-0 · Cited by 49
“This signaling orchestrates three known proteolytic systems working together in muscle atrophy, ie, the calcium-dependent calpain system, the lysosomal protease system (cathepsins), and the ubiquitin-proteasome system [21].”
BackgroundInfluential
Protective effects of exercise preconditioning on hindlimb unloading‐induced atrophy of rat soleus muscle
Fujino, H., Ishihara, A., Murakami, S., Yasuhara, T., Kondo, H., Mohri, S., Takeda, I., & Roy, R. R. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01984.x · Cited by 49
“…disuse, such as HU, have been shown to be associated with decreased protein synthesis and/or increased protein degradation rates involving at least three proteolytic pathways, i.e. cathepsins, calpains and an ATP-ubiquitin-proteasome-dependent system (Roy et al. 1996, Jackman & Kandarian 2004).”
Background
Characterisation and expression analysis of cathepsins and ubiquitin-proteasome genes in gilthead sea bream (Sparus aurata) skeletal muscle
Salmerón, C., Navarro, I., Johnston, I. A., Gutiérrez, J., & Capilla, E. (2015) · BMC Research Notes · doi:10.1186/s13104-015-1121-0 · Cited by 49
“In vertebrates, four catabolic systems are known to be involved in muscle proteolysis: a) the Ca-dependent proteinases (calpains), b) the autophagy-lysosome system (cathepsins), c) the ATPdependent ubiquitin-proteasome (UbP) pathway and, d) the apoptosis protease system (caspases) [13-16].”
Background
A new pathway encompassing calpain 3 and its newly identified substrate cardiac ankyrin repeat protein is involved in the regulation of the nuclear factor‐κB pathway in skeletal muscle
Laure, L., Danièle, N., Suel, L., Marchand, S., Aubert, S., Bourg, N., Roudaut, C., Duguez, S., Bartoli, M., & Richard, I. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07820.x · Cited by 47
Morphological effects of two protocols of passive stretch over the immobilized rat soleus muscle
Gomes, A. R. S., Cornachione, A. S., Salvini, T. F., & Mattiello‐Sverzut, A. C. (2007) · Journal of Anatomy · doi:10.1111/j.1469-7580.2007.00697.x · Cited by 48
“Immobilization generates type I and type II fibers atrophy, which seems to be associated with an increase in proteolysis more than a decrease in protein synthesis (Jackman & Kandarian, 2004).”
Background
Overexpression of inducible 70-kDa heat shock protein in mouse improves structural and functional recovery of skeletal muscles from atrophy
Miyabara, E. H., Nascimento, T. L., Rodrigues, D. C., Moriscot, A. S., Davila, W. F., Mou, Y. A., de Tombe, P. P., & Mestril, R. (2012) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-012-1087-x · Cited by 48
“Loss of skeletal muscle mass and function are important clinical consequences of certain diseases, immobilization/ reduced activity, poor nutrition, use of specific medications, and aging [3, 17].”
Protective effect of L-arginine administration on proteins of unloaded m. soleus
Lomonosova, Y. N., Kalamkarov, G. R., Бугрова, А. Е., Shevchenko, T. F., Kartashkina, N. L., Lysenko, E. A., Швец, В. И., & Nemirovskaya, T. L. (2011) · Biochemistry (Moscow) · doi:10.1134/s0006297911050075 · Cited by 48
Role of altered proteostasis network in chronic hypobaric hypoxia induced skeletal muscle atrophy
Agrawal, A., Rathor, R., Kumar, R. S., Suryakumar, G., & Ganju, L. (2018) · PLoS ONE · doi:10.1371/journal.pone.0204283 · Cited by 48
“Activated UPS and calpain pathways account for removal of misfolded/oxidized proteins and activation of apoptotic signalling cascade in the cell.”
BackgroundInfluential
Proteomic analysis of altered protein expression in skeletal muscle of rats in a hypermetabolic state induced by burn sepsis
Duan, X., Francois Berthiaume, B., Yarmush, D. M., & Yarmush, M. L. (2006) · Biochemical Journal · doi:10.1042/bj20051710 · Cited by 48
Melanocortin antagonism ameliorates muscle wasting and inflammation in chronic kidney disease
Cheung, W. W., & Mak, R. H. (2012) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00341.2012 · Cited by 47
DIGE analysis of rat skeletal muscle proteins using nonionic detergent phase extraction of young adult versus aged gastrocnemius tissue
Donoghue, P. M., Staunton, L., Mullen, E., Manning, G., & Ohlendieck, K. (2010) · Journal of Proteomics · doi:10.1016/j.jprot.2010.01.014 · Cited by 48
“metabolic alterations [43], (iii) mitochondrial disturbances and an increased susceptibility to apoptosis [44], (iv) a decreased regenerative capacity [45], (v) disturbed luminal ion binding and cycling [46], (vi) excitation–contraction uncoupling [47], (vii) oxidative stress [48], (viii) a blunted cellular stress res…”
Background
The metabolic modulator trimetazidine triggers autophagy and counteracts stress‐induced atrophy in skeletal muscle myotubes
Ferraro, E., Giammarioli, A. M., Caldarola, S., Lista, P., Feraco, A., Tinari, A., Salvatore, A. M., Malorni, W., Berghella, L., & Rosano, G. M. C. (2013) · FEBS Journal · doi:10.1111/febs.12484 · Cited by 49
Correlated mRNAs and miRNAs from co-expression and regulatory networks affect porcine muscle and finally meat properties
Ponsuksili, S., Du, Y., Hadlich, F., Siengdee, P., Muráni, E., Schwerin, M., & Wimmers, K. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-533 · Cited by 48

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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