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Signaling in Muscle Atrophy and Hypertrophy
Abstract
Muscle performance is influenced by turnover of contractile proteins. Production of new myofibrils and degradation of existing proteins is a delicate balance, which, depending on the condition, can promote muscle growth or loss. Protein synthesis and protein degradation are coordinately regulated by pathways that are influenced by mechanical stress, physical activity, availability of nutrients, and growth factors. Understanding the signaling that regulates muscle mass may provide potential therapeutic targets for the prevention and treatment of muscle wasting in metabolic and neuromuscular diseases.
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Citations
Cites
Identification of ubiquitin ligases required for skeletal muscle atrophy.
Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521
A central role for JNK in obesity and insulin resistance
Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359
Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012
Self-citationBodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752
Double muscling in cattle due to mutations in the myostatin gene
McPherron, A. C., & Lee, S.-J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12457 · Cited by 2,039
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953
Self-citationAbsence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
Um, S. H., Frigerio, F., Watanabe, M., Picard, F., Joaquin, M., Sticker, M., Fumagalli, S., Allegrini, P. R., Kozma, S. C., Auwerx, J., et al. (2004) · Nature · doi:10.1038/nature02866 · Cited by 1,677
Rommel, C., Bodine, S. C., Clarke, B. A., Rossman, R., Nunez, L., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1009 · Cited by 1,583
Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539
Zhao, J., Brault, J. J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.004 · Cited by 1,489
Self-citation
Cited by
Acute skeletal muscle wasting in critical illness
Puthucheary, Z. A., Rawal, J., McPhail, M., Connolly, B., Ratnayake, G., Chan, P., Hopkinson, N. S., Padhke, R., Dew, T., Sidhu, P. S., et al. (2013) · JAMA · doi:10.1001/jama.2013.278481 · Cited by 2,103
Exercise Metabolism and the Molecular Regulation of Skeletal Muscle Adaptation
Egan, B., & Zierath, J. R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2012.12.012 · Cited by 2,084
Mechanisms regulating skeletal muscle growth and atrophy
Schiaffino, S., Dyar, K. A., Ciciliot, S., Blaauw, B., & Sandri, M. (2013) · The FEBS Journal · doi:10.1111/febs.12253 · Cited by 1,492
Self-citationAutophagy is required to maintain muscle mass.
Masiero, E., Agatea, L., Mammucari, C., Blaauw, B., Loro, E., Komatsu, M., Metzger, D., Reggiani, C., Schiaffino, S., & Sandri, M. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.10.008 · Cited by 1,282
Self-citationMuscle wasting in disease: molecular mechanisms and promising therapies
Cohen, S., Nathan, J. A., & Goldberg, A. L. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4467 · Cited by 1,089
Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models
Schiaffino, S., & Mammucari, C. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-4 · Cited by 816
“Various aspects of the role of this pathway in skeletal muscle have been previously discussed [1-3].”
BackgroundTranscriptional mechanisms regulating skeletal muscle differentiation, growth and homeostasis
Braun, T., & Gautel, M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3118 · Cited by 713
Milan, G., Romanello, V., Pescatore, F., Armani, A., Paik, J.-H., Frasson, L., Seydel, A., Zhao, J., Abraham, R., Goldberg, A. L., et al. (2015) · Nature Communications · doi:10.1038/ncomms7670 · Cited by 709
Self-citationSchoenfeld, B. J., Ogborn, D., & Krieger, J. W. (2017) · Journal of Sports Sciences · doi:10.1080/02640414.2016.1210197 · Cited by 671
Mitochondrial fission and remodelling contributes to muscle atrophy
Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.60 · Cited by 596
Self-citationA review on the mechanisms of blood-flow restriction resistance training-induced muscle hypertrophy
Pearson, S. J., & Hussain, S. R. (2015) · Sports Medicine · doi:10.1007/s40279-014-0264-9 · Cited by 592
Smad2 and 3 transcription factors control muscle mass in adulthood
Sartori, R., Milan, G., Patron, M., Mammucari, C., Blaauw, B., Abraham, R., & Sandri, M. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00104.2009 · Cited by 517
Self-citationCrosstalk between Glucocorticoid Receptor and Nutritional Sensor mTOR in Skeletal Muscle
Shimizu, N., Yoshikawa, N., Ito, N., Maruyama, T., Suzuki, Y., Takeda, S.-I., Nakae, J., Tagata, Y., Nishitani, S., Takehana, K., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.01.001 · Cited by 498
BMP signaling controls muscle mass
Sartori, R., Schirwis, E., Blaauw, B., Bortolanza, S., Zhao, J., Enzo, E., Stantzou, A., Mouisel, E., Toniolo, L., Ferry, A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2772 · Cited by 467
Self-citationVaranita, 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
Self-citationSarcopenia, Cachexia and Aging: Diagnosis, Mechanisms and Therapeutic Options - A Mini-Review
Ali, S., & Garcia, J. M. (2014) · Gerontology · doi:10.1159/000356760 · Cited by 462
Sandri, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.056 · Cited by 451
Self-citationExercise Attenuates the Major Hallmarks of Aging
Garatachea, N., Pareja-Galeano, H., Sanchis-Gomar, F., Santos-Lozano, A., Fiuza-Luces, C., Morán, M., Emanuele, E., Joyner, M. J., & Lucia, A. (2015) · Rejuvenation Research · doi:10.1089/rej.2014.1623 · Cited by 413
Myostatin and the skeletal muscle atrophy and hypertrophy signaling pathways
Rodriguez, J., Vernus, B., Chelh, I., Cassar-Malek, I., Gabillard, J. C., Hadj Sassi, A., Seiliez, I., Picard, B., & Bonnieu, A. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1689-x · Cited by 397
Wohlgemuth, S. E., Seo, A. Y., Marzetti, E., Lees, H. A., & Leeuwenburgh, C. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2009.11.002 · Cited by 397
Myostatin/activin pathway antagonism: molecular basis and therapeutic potential
Han, H. Q., Zhou, X., Mitch, W. E., & Goldberg, A. L. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.019 · Cited by 314
The role of skeletal muscle mTOR in the regulation of mechanical load‐induced growth
Goodman, C. A., Frey, J. W., Mabrey, D. M., Jacobs, B. L., Lincoln, H. C., You, J., & Hornberger, T. A. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.218255 · Cited by 297
Sleep and muscle recovery: Endocrinological and molecular basis for a new and promising hypothesis
Dattilo, M., Antunes, H. K. M., Medeiros, A., Mônico Neto, M., Souza, H. S., Tufik, S., & de Mello, M. T. (2011) · Medical Hypotheses · doi:10.1016/j.mehy.2011.04.017 · Cited by 290
Skeletal muscle aging: influence of oxidative stress and physical exercise
Gomes, M. J., Martinez, P. F., Pagan, L. U., Damatto, R. L., Mariano Cezar, M. D., Ruiz Lima, A. R., Okoshi, K., & Okoshi, M. P. (2017) · Oncotarget · doi:10.18632/oncotarget.14670 · Cited by 285
The TWEAK–Fn14 system is a critical regulator of denervation-induced skeletal muscle atrophy in mice
Mittal, A., Bhatnagar, S., Kumar, A., Lach-Trifilieff, E., Wauters, S., Li, H., Makonchuk, D. Y., Glass, D. J., & Kumar, A. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200909117 · Cited by 250
Lee, D., & Goldberg, A. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.489716 · Cited by 211
Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle
Hornberger, T. A. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.05.007 · Cited by 170
“However, activation of PI3K/PKB can also induce signaling through a variety of mTORC1independent growth regulatory molecules including GSK3β and the FOXO transcription factors (Nader, 2005, Sandri, 2008, Frost and Lang, 2007).”
BackgroundModulation of autophagy and ubiquitin-proteasome pathways during ultra-endurance running
Jamart, C., Francaux, M., Millet, G. Y., Deldicque, L., Frère, D., & Féasson, L. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00952.2011 · Cited by 157
Differential response of skeletal muscles to mTORC1 signaling during atrophy and hypertrophy
Bentzinger, C. F., Lin, S., Romanino, K., Castets, P., Guridi, M., Summermatter, S., Handschin, C., Tintignac, L. A., Hall, M. N., & Rüegg, M. A. (2013) · Skeletal Muscle · doi:10.1186/2044-5040-3-6 · Cited by 153
Autophagy in health and disease. 3. Involvement of autophagy in muscle atrophy
Sandri, M. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00531.2009 · Cited by 152
Self-citationAnabolic and catabolic pathways regulating skeletal muscle mass
McCarthy, J. J., & Esser, K. A. (2010) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e32833781b5 · Cited by 148
Regulation of muscle atrophy in aging and disease
Vinciguerra, M., Musaro, A., & Rosenthal, N. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_15 · Cited by 149
YAP-Mediated Mechanotransduction in Skeletal Muscle
Fischer, M., Rikeit, P., Knaus, P., & Coirault, C. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00041 · Cited by 145
Ogasawara, R., Kobayashi, K., Tsutaki, A., Lee, K., Abe, T., Fujita, S., Nakazato, K., & Ishii, N. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01161.2012 · Cited by 138
Role of mTORC1 in mechanically induced increases in translation and skeletal muscle mass
Goodman, C. A. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01011.2018 · Cited by 133
Mtor is necessary for proper satellite cell activity and skeletal muscle regeneration
Zhang, P., Liang, X., Shan, T., Jiang, Q., Deng, C., Zheng, R., & Kuang, S. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.05.032 · Cited by 133
Philp, A., Hamilton, D. L., & Baar, K. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00941.2010 · Cited by 131
The Transcription Factor ATF4 Promotes Skeletal Myofiber Atrophy during Fasting
Ebert, S. M., Monteys, A. M., Fox, D. K., Bongers, K. S., Shields, B. E., Malmberg, S. E., Davidson, B. L., Suneja, M., & Adams, C. M. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0345 · Cited by 130
Sarcopenia: Molecular Pathways and Potential Targets for Intervention
Pascual-Fernández, J., Fernández-Montero, A., Córdova-Martínez, A., Pastor, D., Martínez-Rodríguez, A., & Roche, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228844 · Cited by 125
Favier, F. B., Costes, F., Defour, A., Bonnefoy, R., Lefai, E., Baugé, S., Peinnequin, A., Benoit, H., & Freyssenet, D. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00550.2009 · Cited by 127
Muscle activation during low- versus high-load resistance training in well-trained men
Schoenfeld, B. J., Contreras, B., Willardson, J. M., Fontana, F., & Tiryaki-Sonmez, G. (2014) · European Journal of Applied Physiology · doi:10.1007/s00421-014-2976-9 · Cited by 121
Posttranslational modifications control FoxO3 activity during denervation
Bertaggia, E., Coletto, L., & Sandri, M. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00142.2011 · Cited by 114
Self-citationVissing, K., McGee, S. L., Farup, J., Kjølhede, T., Vendelbo, M. H., & Jessen, N. (2013) · Scandinavian Journal of Medicine & Science in Sports · doi:10.1111/j.1600-0838.2011.01395.x · Cited by 111
Autophagic response to exercise training in skeletal muscle with age
Kim, Y. A., Kim, Y. S., Oh, S. L., Kim, H.-J., & Song, W. (2013) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-013-0246-7 · Cited by 108
Brocca, L., Toniolo, L., Reggiani, C., Bottinelli, R., Sandri, M., & Pellegrino, M. A. (2017) · The Journal of Physiology · doi:10.1113/jp273097 · Cited by 93
Self-citationAguilar‐Agon, K. W., Capel, A. J., Martin, N. R. W., Player, D. J., & Lewis, M. P. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28923 · Cited by 84
Angiotensin-(1-7) attenuates disuse skeletal muscle atrophy via the Mas receptor
Morales, M. G., Abrigo, J., Acuña, M. J., Santos, R. A., Bader, M., Brandan, E., Simon, F., Olguin, H., Cabrera, D., & Cabello-Verrugio, C. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.023390 · Cited by 77
Liang, J., Zhang, H., Zeng, Z., Wu, L., Zhang, Y., Guo, Y., Lv, J., Wang, C., Fan, J., & Chen, N. (2021) · Metabolites · doi:10.3390/metabo11050323 · Cited by 84
Nutritional strategies to counteract muscle atrophy caused by disuse and to improve recovery
Magne, H., Savary-Auzeloux, I., Rémond, D., & Dardevet, D. (2013) · Nutrition Research Reviews · doi:10.1017/s0954422413000115 · Cited by 78
Role of PGC-1α in sarcopenia: Etiology and potential intervention—A mini-review
Ji, L. L., & Kang, C. (2015) · Gerontology · doi:10.1159/000365947 · Cited by 77
Schoenfeld, B. J. (2013) · Journal of Strength and Conditioning Research · doi:10.1519/jsc.0b013e31828ddd53 · Cited by 74
Anderson, L. J., Tamayose, J. M., & Garcia, J. M. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.06.010 · Cited by 70
Chen, M.-C., Hsu, W.-L., Hwang, P.-A., Chen, Y.-L., & Chou, T.-C. (2016) · Oncotarget · doi:10.18632/oncotarget.9958 · Cited by 69
Lewis, A., Lee, J. Y., Donaldson, A. V., Natanek, S. A., Vaidyanathan, S., Man, W. D. ‐., Hopkinson, N. S., Sayer, A. A., Patel, H. P., Cooper, C., et al. (2016) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12078 · Cited by 68
PGC-1α and Myokines in the Aging Muscle – A Mini-Review
Arnold, A.-S., Egger, A., & Handschin, C. (2011) · Gerontology · doi:10.1159/000281883 · Cited by 65
Mirzoev, T. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217940 · Cited by 65
Contribution of the Mitochondria to Locomotor Muscle Dysfunction in Patients with COPD
Taivassalo, T., & Hussain, S. N. A. (2016) · Chest · doi:10.1016/j.chest.2015.11.021 · Cited by 59
Influence of Oral Contraceptive Use on Adaptations to Resistance Training
Dalgaard, L. B., Dalgas, U., Andersen, J. L., Rossen, N. B., Møller, A. B., Stødkilde-Jørgensen, H., Jørgensen, J. O., Kovanen, V., Couppé, C., Langberg, H., et al. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00824 · Cited by 58
Bohnert, K. R., Goli, P., Roy, A., Sharma, A. K., Xiong, G., Gallot, Y. S., & Kumar, A. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00184-19 · Cited by 52
Girven, M., Dugdale, H. F., Owens, D. J., Hughes, D. C., Stewart, C. E., & Sharples, A. P. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25380 · Cited by 48
Chen, M.-C., Chen, Y.-L., Lee, C.-F., Hung, C.-H., & Chou, T.-C. (2015) · PLOS ONE · doi:10.1371/journal.pone.0143594 · Cited by 45
Inflammation and metabolism: the role of adiposity in sarcopenic obesity
Lynch, G. M., Murphy, C. H., Castro, E. D. M., & Roche, H. M. (2020) · Proceedings of the Nutrition Society · doi:10.1017/s0029665120007119 · Cited by 41
Zhao, F., Yu, Y., Liu, W., Zhang, J., Liu, X., Liu, L., & Yin, H. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b05387 · Cited by 41
Muscle wasting in collagen-induced arthritis and disuse atrophy
de Oliveira Nunes Teixeira, V., Filippin, L. I., Viacava, P. R., de Oliveira, P. G., & Xavier, R. M. (2013) · Experimental Biology and Medicine · doi:10.1177/1535370213505961 · Cited by 40
Pottecher, J., Adamopoulos, C., Lejay, A., Bouitbir, J., Charles, A.-L., Meyer, A., Singer, M., Wolff, V., Diemunsch, P., Laverny, G., et al. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00579 · Cited by 33
Eftestøl, E., Egner, I. M., Lunde, I. G., Ellefsen, S., Andersen, T., Sjåland, C., Gundersen, K., & Bruusgaard, J. C. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00016.2016 · Cited by 36
New roles for Smad signaling and phosphatidic acid in the regulation of skeletal muscle mass
Goodman, C. A., & Hornberger, T. A. (2014) · F1000Prime Reports · doi:10.12703/p6-20 · Cited by 30
Current opinion on dietary advice in order to preserve fat-free mass during a low-calorie diet
Rondanelli, M., Faliva, M. A., Gasparri, C., Peroni, G., Spadaccini, D., Maugeri, R., Nichetti, M., Infantino, V., & Perna, S. (2020) · Nutrition · doi:10.1016/j.nut.2019.110667 · Cited by 29
Late-onset caloric restriction alters skeletal muscle metabolism by modulating pyruvate metabolism
Chen, C.-N. (., Lin, S.-Y., Liao, Y.-H., Li, Z.-J., & Wong, A. M.-K. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00508.2014 · Cited by 27
Seok, Y. M., Yoo, J.-M., Nam, Y., Kim, J., Kim, J. S., Son, J.-H., & Kim, H. J. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.113557 · Cited by 27
Anabolic Activity of a Soy Extract and Three Major Isoflavones in C2C12 Myotubes
Zheng, W., Hemker, M., Xie, M., Soukup, S., & Diel, P. (2018) · Planta Medica · doi:10.1055/a-0598-4812 · Cited by 23
Taurine Rescues Cisplatin-Induced Muscle Atrophy in Vitro: A Morphological Study
Stacchiotti, A., Rovetta, F., Ferroni, M., Corsetti, G., Lavazza, A., Sberveglieri, G., & Aleo, M. F. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/840951 · Cited by 21
Effect of 20-hydroxyecdysone on proteolytic regulation in skeletal muscle atrophy
HIRUNSAI, M., YIMLAMAI, T., & SUKSAMRARN, A. (2016) · In Vivo · doi:10.21873/invivo.11007 · Cited by 13
Metadata
- Authors
- Sandri, M.
- Venue
- Physiology
- Publisher
- American Physiological Society
- Published
- 2008-06
- Volume
- 23
- Issue
- 3
- Pages
- 160-170
- ISSN
- 0886-1714 (ISSN-L)
- 1548-9213
- 1548-9221
- OpenAlex
- W2165370562
- Cited by
- 827
- References
- 25
- FWCI
- 16.01
- Type
- journal article
- Language
- en
- Open access
- closed
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