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Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.
Open accessAbstract
Skeletal muscle atrophy is a debilitating response to fasting, disuse, cancer, and other systemic diseases. In atrophying muscles, the ubiquitin ligase, atrogin-1 (MAFbx), is dramatically induced, and this response is necessary for rapid atrophy. Here, we show that in cultured myotubes undergoing atrophy, the activity of the PI3K/AKT pathway decreases, leading to activation of Foxo transcription factors and atrogin-1 induction. IGF-1 treatment or AKT overexpression inhibits Foxo and atrogin-1 expression. Moreover, constitutively active Foxo3 acts on the atrogin-1 promoter to cause atrogin-1 transcription and dramatic atrophy of myotubes and muscle fibers. When Foxo activation is blocked by a dominant-negative construct in myotubes or by RNAi in mouse muscles in vivo, atrogin-1 induction during starvation and atrophy of myotubes induced by glucocorticoids are prevented. Thus, forkhead factor(s) play a critical role in the development of muscle atrophy, and inhibition of Foxo factors is an attractive approach to combat muscle wasting.
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“Two muscle-specific E3 ubiquitin ligases, muscle RING finger 1 (MuRF1, also known as TRIM63) and muscle atrophy F-Box (MAFbx, also known as atrogin-1 or FBXO32), are thought to be key regulators of proteasomal proteolysis in skeletal muscle, especially under atrophy-inducing conditions (Cai et al., 2004; Sandri et al., 2004; Stitt et al., 2004).”
From Proteasome dysfunction induces muscle growth defects and protein aggregation (2014) · cites this paper as Sandri et al., 2004
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Two muscle-specific E3 ubiquitin ligases, MuRF1 and Atrogin1, are thought to be key regulators of proteasomal proteolysis in skeletal muscle, especially under atrophy-inducing conditions (Cai et al., 2004; Sandri et al., 2004).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Sandri et al., 2004
Experimental — accuracy not yet measuredIn the citing paper
“Atrogin-1 plays a key role in muscle atrophy as muscle specific ubiquitin ligase.”
From GLP-1RA Liraglutide and Semaglutide Improves Obesity-Induced Muscle Atrophy via SIRT1 Pathway (2023) · cites this paper as [48]
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“FoxO family of transcription factors (FoxO1, FoxO3, and FoxO4) are critical mediators of the catabolic response during atrophy [9, 15, 16].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [9]
In the citing paper
“The IGF1–AKT-–mTOR axis increases protein synthesis by stimulating the translational machinery and simultaneously blocks FoxOs transcription factors and protein degradation [9].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [9]
In the citing paper
“Alterations in mPTP function are undoubtedly contributing to the aging-related loss of muscle mass and function, since mPTP opening can trigger several atrophy-regulating pathways.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [17]
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Cites
Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor
Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 5,594
A System for Stable Expression of Short Interfering RNAs in Mammalian Cells
Brummelkamp, T. R., Bernards, R., & Agami, R. (2002) · Science · doi:10.1126/science.1068999 · Cited by 4,295
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
Bodine, 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
Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964
Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., & Goldberg, A. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251541198 · Cited by 1,774
Self-citationRommel, 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
Self-citationRubinson, D. A., Dillon, C. P., Kwiatkowski, A. V., Sievers, C., Yang, L., Kopinja, J. E., Rooney, D. L., Zhang, M., Ihrig, M. M., McManus, M. T., et al. (2003) · Nature Genetics · doi:10.1038/ng1117 · Cited by 1,499
Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction
Puigserver, P., Rhee, J., Donovan, J., Walkey, C. J., Yoon, J. C., Oriente, F., Kitamura, Y., Altomonte, J., Dong, H., Accili, D., et al. (2003) · Nature · doi:10.1038/nature01667 · Cited by 1,487
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Items 401–500 of 1,032
Tang, H., Inoki, K., Lee, M. C., Wright, E., Khuong, A., Khuong, A., Sugiarto, S., Garner, M. S., Paik, J., DePinho, R. A., et al. (2014) · Science Signaling · doi:10.1126/scisignal.2004809 · Cited by 145
Chien, K. R., & Karsenty, G. (2005) · Cell · doi:10.1016/j.cell.2005.02.006 · Cited by 143
Sarcopenia and cachexia: the adaptations of negative regulators of skeletal muscle mass
Sakuma, K., & Yamaguchi, A. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0052-4 · Cited by 137
Mechanisms of muscle growth and atrophy in mammals and Drosophila
Piccirillo, R., Demontis, F., Perrimon, N., & Goldberg, A. L. (2013) · Developmental Dynamics · doi:10.1002/dvdy.24036 · Cited by 147
Self-citationA novel ubiquitin‐binding protein ZNF216 functioning in muscle atrophy
Hishiya, A., Iemura, S., Natsume, T., Takayama, S.-I. J., Ikeda, K., & Watanabe, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600945 · Cited by 142
Smad3 Induces Atrogin-1, Inhibits mTOR and Protein Synthesis, and Promotes Muscle Atrophy In Vivo
Goodman, C. A., McNally, R. M., Hoffmann, F. M., & Hornberger, T. A. (2013) · Molecular Endocrinology · doi:10.1210/me.2013-1194 · Cited by 152
Intermittent glucocorticoid steroid dosing enhances muscle repair without eliciting muscle atrophy
Quattrocelli, M., Barefield, D. Y., Warner, J. L., Vo, A. H., Hadhazy, M., Earley, J. U., Demonbreun, A. R., & McNally, E. M. (2017) · Journal of Clinical Investigation · doi:10.1172/jci91445 · Cited by 143
Calpain activity and muscle wasting in sepsis
Smith, I. J., Lecker, S. H., & Hasselgren, P.-O. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90226.2008 · Cited by 142
Self-citationMcClung, J. M., Kavazis, A. N., Whidden, M. A., DeRuisseau, K. C., Falk, D. J., Criswell, D. S., & Powers, S. K. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.141119 · Cited by 141
Sato, A. Y., Richardson, D., Cregor, M. D., Davis, H. M., Au, E. D., McAndrews, K., Zimmers, T. A., Organ, J. M., Peacock, M., Plotkin, L. I., et al. (2017) · Endocrinology · doi:10.1210/en.2016-1779 · Cited by 144
Hickmann, C., Castanares‐Zapatero, D., Deldicque, L., den Bergh, P. Y. K. V., Caty, G. D., Robert, A. R., Roeseler, J., Francaux, M., & Laterre, P. (2018) · Critical Care Medicine · doi:10.1097/ccm.0000000000003263 · Cited by 145
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-citationJaitovich, A., Angulo, M., Lecuona, E., Dada, L. A., Welch, L. C., Cheng, Y., Gusarova, G., Ceco, E., Liu, C., Shigemura, M., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.625715 · Cited by 137
Computational reconstruction of the human skeletal muscle secretome
Bortoluzzi, S., Scannapieco, P., Cestaro, A., Danieli, G. A., & Schiaffino, S. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20803 · Cited by 136
Self-citationAtrophy and hypertrophy of skeletal muscles: structural and functional aspects
Boonyarom, O., & Inui, K. (2006) · Acta Physiologica · doi:10.1111/j.1748-1716.2006.01613.x · Cited by 144
NF-κB Signaling in the Aging Process
Salminen, A., & Kaarniranta, K. (2009) · Journal of Clinical Immunology · doi:10.1007/s10875-009-9296-6 · Cited by 140
Regulation of IRS1/Akt insulin signaling by microRNA-128a during myogenesis
Motohashi, N., Alexander, M. S., Shimizu‐Motohashi, Y., Myers, J. A., Kawahara, G., & Kunkel, L. M. (2013) · Journal of Cell Science · doi:10.1242/jcs.119966 · Cited by 140
C/EBPβ mediates tumour‐induced ubiquitin ligase atrogin1/MAFbx upregulation and muscle wasting
Zhang, G., Jin, B., & Li, Y. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.292 · Cited by 144
Sáinz, N., Rodríguez, A., Catalán, V., Becerril, S., Ramírez, B., Gómez-Ambrosi, J., & Frühbeck, G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006808 · Cited by 135
Mikura, M., Yamaoka, I., Doi, M., Kawano, Y., Nakayama, M., Nakao, R., Hirasaka, K., Okumura, Y., & Nikawa, T. (2008) · Anesthesiology · doi:10.1097/aln.0b013e318190b6c1 · Cited by 135
Almeida, M. (2012) · BoneKEy Reports · doi:10.1038/bonekey.2012.102 · Cited by 141
Protein breakdown in cancer cachexia
Sandri, M. (2016) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.11.002 · Cited by 134
Self-citationMetabolic control through glucocorticoid hormones: An update
Rose, A. J., & Herzig, S. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.03.007 · Cited by 136
microRNA-378 promotes autophagy and inhibits apoptosis in skeletal muscle
Li, Y., Jiang, J., Liu, W., Wang, H., Zhao, L., Liu, S., Li, P., Zhang, S., Sun, C., Wu, Y., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803377115 · Cited by 137
Skeletal muscle fibre plasticity in response to selected environmental and physiological stimuli.
Matsakas, A., & Patel, K. (2009) · PubMed · doi:10.14670/hh-24.611 · Cited by 133
Liu, J., Peng, Y., Wang, X., Fan, Y., Qin, C., Shi, L., Tang, Y., Cao, K., Li, H., Long, J., et al. (2016) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.5b00516 · Cited by 133
Schulze, P. C., Fang, J. S., Kassik, K. A., Gannon, J., Cupesi, M., MacGillivray, C., Lee, R. T., & Rosenthal, N. A. (2005) · Circulation Research · doi:10.1161/01.res.0000179580.72375.c2 · Cited by 136
Choi, S., Jeong, H.-J., Kim, H., Choi, D., Cho, S.-C., Seong, J. K., Koo, S.-H., & Kang, J.-S. (2019) · Autophagy · doi:10.1080/15548627.2019.1569931 · Cited by 132
Effects of 3 days unloading on molecular regulators of muscle size in humans
Gustafsson, T. P., Österlund, T., Flanagan, J. N., von Walden, F., Trappe, T. A., Linnehan, R. M., & Tesch, P. A. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00110.2009 · Cited by 135
Wollersheim, T., Woehlecke, J., Krebs, M., Hamati, J., Lodka, D., Luther-Schroeder, A., Langhans, C., Haas, K., Radtke, T., Kleber, C., et al. (2014) · Intensive Care Medicine · doi:10.1007/s00134-014-3224-9 · Cited by 143
A centronuclear myopathy-dynamin 2 mutation impairs skeletal muscle structure and function in mice
Durieux, A., Vignaud, A., Prudhon, B., Bui, M. T., Beuvin, M., Vassilopoulos, S., Fraysse, B., Ferry, A., Lainé, J., Romero, N. B., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq413 · Cited by 143
Fenofibrate prevents skeletal muscle loss in mice with lung cancer
Goncalves, M. D., Hwang, S., Pauli, C., Murphy, C. J., Cheng, Z., Hopkins, B. D., Wu, D., Loughran, R. M., Emerling, B. M., Zhang, G., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1714703115 · Cited by 133
Forkhead transcription factors in immunology
Jonsson, A. H., & Peng, S. L. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4365-8 · Cited by 132
Ros‐mediated activation of NF‐κB and Foxo during muscle disuse
Dodd, S. L., Gagnon, B. J., Senf, S. M., Hain, B. A., & Judge, A. R. (2010) · Muscle & Nerve · doi:10.1002/mus.21526 · Cited by 131
Current understanding of sarcopenia: possible candidates modulating muscle mass
Sakuma, K., Aoi, W., & Yamaguchi, A. (2014) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1527-x · Cited by 133
Muscle wasting and aging: Experimental models, fatty infiltrations, and prevention
Brioche, T., Pagano, A. F., Py, G., & Chopard, A. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.04.006 · Cited by 129
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
The possible role of the Akt signaling pathway in schizophrenia
Zheng, W., Wang, H., Zeng, Z., Lin, J., Little, P. J., Srivastava, L. K., & Quirion, R. (2012) · Brain Research · doi:10.1016/j.brainres.2012.06.032 · Cited by 130
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Conte, E., Bresciani, E., Rizzi, L., Cappellari, O., Luca, A. D., Torsello, A., & Liantonio, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041242 · Cited by 136
Wang, X. H., Du, J., Klein, J. D., Bailey, J. L., & Mitch, W. E. (2009) · Kidney International · doi:10.1038/ki.2009.260 · Cited by 130
HDAC1 activates FoxO and is both sufficient and required for skeletal muscle atrophy
Beharry, A. W., Sandesara, P. B., Roberts, B. M., Ferreira, L. F., Senf, S. M., & Judge, A. R. (2014) · Journal of Cell Science · doi:10.1242/jcs.136390 · Cited by 128
Chalkiadaki, A., Igarashi, M., Nasamu, A. S., Knezevic, J., & Guarente, L. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004490 · Cited by 126
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Noone, J., Mucinski, J. M., DeLany, J. P., Sparks, L. M., & Goodpaster, B. H. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2023.12.025 · Cited by 128
The Functional Role of Calcineurin in Hypertrophy, Regeneration, and Disorders of Skeletal Muscle
Sakuma, K., & Yamaguchi, A. (2010) · BioMed Research International · doi:10.1155/2010/721219 · Cited by 132
Recent advances in the biology and therapy of muscle wasting
Glass, D. J., & Roubenoff, R. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05809.x · Cited by 130
Gruet, M., Troosters, T., & Vergès, S. (2017) · Journal of Cystic Fibrosis · doi:10.1016/j.jcf.2017.02.007 · Cited by 131
Frost, R. A., Nystrom, G. J., Jefferson, L. S., & Lang, C. H. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00359.2006 · Cited by 136
Ottenheijm, C. A. C., Heunks, L. M. A., Li, Y.-P., Jin, B., Minnaard, R., van Hees, H. W. H., & Dekhuijzen, P. N. R. (2006) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200605-721oc · Cited by 127
Calpain-1 is required for hydrogen peroxide-induced myotube atrophy
McClung, J. M., Judge, A. R., Talbert, E. E., & Powers, S. K. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00497.2008 · Cited by 137
Murdoch, J. D., Rostosky, C. M., Gowrisankaran, S., Arora, A. S., Soukup, S., Vidal, R. O., Capece, V., Freytag, S., Fischer, A., Verstreken, P., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.058 · Cited by 124
Role of Pro-inflammatory Cytokines in Regulation of Skeletal Muscle Metabolism: A Systematic Review
Sharma, B., & Dabur, R. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867326666181129095309 · Cited by 129
Mitochondrial dysfunction and skeletal muscle atrophy: Causes, mechanisms, and treatment strategies
Kubat, G. B., Bouhamida, E., Ülger, Ö., Türkel, İ., Pedriali, G., Ramaccini, D., Ekinci, Ö., Özerkliğ, B., Atalay, Ö., Patergnani, S., et al. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.07.003 · Cited by 134
Muscle wasting and interleukin-6-induced atrogin-I expression in the cachectic Apc Min/+ mouse
Baltgalvis, K. A., Berger, F. G., Peña, M. M. O., Davis, J. M., White, J. P., & Carson, J. A. (2008) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-008-0574-6 · Cited by 129
Judge, S. M., Howard, T. M., Ahn, B., Ferreira, L. F., & Judge, A. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062687 · Cited by 127
The Role of Autophagy in Skeletal Muscle Diseases
Xia, Q., Huang, X., Huang, J., Zheng, Y., March, M., Li, J., & Wei, Y. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.638983 · Cited by 137
Forkhead Box O Signaling Pathway in Skeletal Muscle Atrophy
Chen, K., Gao, P., Li, Z., Dai, A., Yang, M. W. O., Chen, S., Su, J., Deng, Z., & Li, L. (2022) · American Journal Of Pathology · doi:10.1016/j.ajpath.2022.09.003 · Cited by 129
The epigenetic network regulating muscle development and regeneration
Palacios, D., & Puri, P. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20489 · Cited by 128
Luo, J., Sobkiw, C. L., Hirshman, M. F., Logsdon, M. N., Li, T. Q., Goodyear, L. J., & Cantley, L. C. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.04.003 · Cited by 123
Identification of atrogin-1-targeted proteins during the myostatin-induced skeletal muscle wasting
Lokireddy, S., Wijesoma, I. W., Sze, S. K., McFarlane, C., Kambadur, R., & Sharma, M. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00402.2011 · Cited by 135
Cancer Cachexia Signaling Pathways Continue to Emerge Yet Much Still Points to the Proteasome
Acharyya, S., & Guttridge, D. C. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2307 · Cited by 127
Insulin Regulation of Proteostasis and Clinical Implications
James, H. A., O'Neill, B. T., & Nair, K. S. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.06.010 · Cited by 121
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Tsai, S., Sitzmann, J. M., Dastidar, S. G., Rodriguez, A. A., Vu, S. L., McDonald, C. E., Academia, E. C., O’Leary, M. N., Ashe, T. D., La Spada, A. R., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci77361 · Cited by 126
Interdependence of Muscle Atrophy and Bone Loss Induced by Mechanical Unloading
Lloyd, S. A. J., Lang, C. H., Zhang, Y., Paul, E. M., Laufenberg, L. J., Lewis, G. S., & Donahue, H. J. (2013) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2113 · Cited by 129
Watson, M. L., Baehr, L. M., Reichardt, H. M., Tuckermann, J. P., Bodine, S. C., & Furlow, J. D. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00512.2011 · Cited by 122
Smith, G. I., Yoshino, J., Reeds, D. N., Bradley, D., Burrows, R. E., Heisey, H. D., Moseley, A. C., & Mittendorfer, B. (2014) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2013-2835 · Cited by 124
Mechanisms of skeletal muscle atrophy
Ventadour, S., & Attaix, D. (2006) · Current Opinion in Rheumatology · doi:10.1097/01.bor.0000245731.25383.de · Cited by 128
Krawiec, B. J., Nystrom, G. J., Frost, R. A., Jefferson, L. S., & Lang, C. H. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00622.2006 · Cited by 125
MicroRNA-23a and MicroRNA-27a Mimic Exercise by Ameliorating CKD-Induced Muscle Atrophy
Wang, B., Zhang, C., Zhang, A., Cai, H., Price, S. R., & Wang, X. H. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016111213 · Cited by 123
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Konopka, A. R., Douglass, M. D., Kaminsky, L. A., Jemioło, B., Trappe, T. A., Trappe, S. W., & Harber, M. P. (2010) · The Journals of Gerontology Series A · doi:10.1093/gerona/glq109 · Cited by 134
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Wilson, E. M., & Rotwein, P. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605445200 · Cited by 125
Csibi, A., Cornille, K., Leibovitch, M.-P., Poupon, A., Tintignac, L. A. J., Sanchez, A. M. J., & Leibovitch, S. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008994 · Cited by 130
Kukreti, H., Amuthavalli, K., Harikumar, A., Sathiyamoorthy, S., Feng, P. Z., Anantharaj, R., Tan, S. L. K., Lokireddy, S., Bonala, S., Sriram, S., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.390369 · Cited by 124
Lokireddy, S., Mouly, V., Butler-Browne, G. S., Gluckman, P. D., Sharma, M., Kambadur, R., & McFarlane, C. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00114.2011 · Cited by 126
Lipocalin 2 mediates appetite suppression during pancreatic cancer cachexia
Olson, B. G., Zhu, X., Norgard, M. A., Levasseur, P. R., Butler, J. T., Buenafe, A. C., Burfeind, K. G., Michaelis, K. A., Pelz, K. R., Mendez, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22361-3 · Cited by 127
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Méjat, A., Decostre, V., Li, J., Renou, L., Kesari, A., Hantaı̈, D., Stewart, C. L., Xiao, X., Hoffman, E. P., Bonne, G., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200811035 · Cited by 121
Baehr, L. M., West, D. W. D., Marshall, A. G., Marcotte, G. R., Baar, K., & Bodine, S. C. (2017) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00703.2016 · Cited by 123
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Goldbraikh, D., Neufeld, D., Eid‐Mutlak, Y., Lasry, I., Gilda, J. E., Parnis, A., & Cohen, S. (2020) · EMBO Reports · doi:10.15252/embr.201948791 · Cited by 126
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Sato, R., Vatic, M., da Fonseca, G. W. P., Anker, S. D., & von Haehling, S. (2024) · Cardiovascular Research · doi:10.1093/cvr/cvae073 · Cited by 130
Mallinson, J. E., Constantin‐Teodosiu, D., Sidaway, J. E., Westwood, F. R., & Greenhaff, P. L. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.164699 · Cited by 119
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Wang, X., Su, H., & Ranek, M. J. (2008) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2008.03.025 · Cited by 120
Dupont‐Versteegden, E. E., Strotman, B. A., Gurley, C. M., Gaddy, D., Knox, M., Fluckey, J. D., & Peterson, C. A. (2006) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00176.2006 · Cited by 122
Yoshida, T., Semprun‐Prieto, L., Sukhanov, S., & Delafontaine, P. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00146.2010 · Cited by 123
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
Smith, I. J., & DODD, S. L. (2007) · Experimental Physiology · doi:10.1113/expphysiol.2006.035790 · Cited by 123
Salminen, A., Ojala, J. O., Huuskonen, J., Kauppinen, A., Suuronen, T., & Kaarniranta, K. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7461-3 · Cited by 120
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Wilson, E. M., & Rotwein, P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c600315200 · Cited by 118
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Romanello, V., & Sandri, M. (2010) · Current Hypertension Reports · doi:10.1007/s11906-010-0157-8 · Cited by 123
Self-citationWhite, Z. R., Terrill, J. R., White, R. B., McMahon, C., Sheard, P., Grounds, M. D., & Shavlakadze, T. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0117-3 · Cited by 125
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Cao, P., Hanai, J., Tanksale, P., Imamura, S., Sukhatme, V. P., & Lecker, S. H. (2009) · The FASEB Journal · doi:10.1096/fj.08-128843 · Cited by 117
Self-citationFoxO3 induces reversible cardiac atrophy and autophagy in a transgenic mouse model
Schips, T. G., Wietelmann, A., Höhn, K., Schimanski, S., Walther, P., Braun, T. W., Wirth, T., & Maier, H. J. (2011) · Cardiovascular Research · doi:10.1093/cvr/cvr144 · Cited by 119
Myogenic and proteolytic mRNA expression following blood flow restricted exercise
Manini, T. M., Vincent, K. R., Leeuwenburgh, C., Lees, H. A., Kavazis, A. N., Borst, S. E., & Clark, B. C. (2010) · Acta Physiologica · doi:10.1111/j.1748-1716.2010.02172.x · Cited by 117
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Gallot, Y. S., Durieux, A., Castells, J., Desgeorges, M. M., Vernus, B., Plantureux, L., Rémond, D., Jahnke, V. E., Lefai, É., Dardevet, D. P., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0057 · Cited by 123
Molecular mechanisms of skeletal muscle development, regeneration, and osteogenic conversion
Endo, T. (2015) · Bone · doi:10.1016/j.bone.2015.02.028 · Cited by 117
Metabolic benefits of resistance training and fast glycolytic skeletal muscle
LeBrasseur, N. K., Walsh, K. X., & Arany, Z. P. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00512.2010 · Cited by 123
Self-citationLokireddy, S., McFarlane, C., Ge, X., Zhang, H., Sze, S. K., Sharma, M., & Kambadur, R. (2011) · Molecular Endocrinology · doi:10.1210/me.2011-1124 · Cited by 122
RetractedSanchez, A. M. J., Candau, R. B., Csibi, A., Pagano, A. F., Raibon, A., & Bernardi, H. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00125.2012 · Cited by 122
Metadata
- Authors
- Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L.
- Affiliations
- Harvard University (US)
- Veneto Institute of Molecular Medicine (IT)
- Beth Israel Deaconess Medical Center (US)
- Boston University (US)
- Corresponding author
- Lecker, Stewart H
- Goldberg, Alfred L
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2004-04
- Volume
- 117
- Issue
- 3
- Pages
- 399-412
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3619734
- OpenAlex
- W2033797333
- Cited by
- 3,012
- References
- 41
- Citations by year
- 2026: 129 · 2025: 122 · 2024: 121 · 2023: 118 · 2022: 141 · 2021: 153 · 2020: 165 · 2019: 159 · 2018: 151 · 2017: 117 · 2016: 134 · 2015: 171 · 2014: 176 · 2013: 177 · 2012: 150
- FWCI
- 33.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- National Space Biomedical Research Institute
- European Commission (QLRT-2000-00530)
- National Institutes of Health (DK02707, DK62307)
- Ministero dell’Istruzione, dell’Università e della Ricerca
- Agenzia Spaziale Italiana
- Muscular Dystrophy Association
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › FOXO transcription factor regulation
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- FOXO transcription factors, atrogin-1, skeletal muscle atrophy, ubiquitin ligase, PI3K/Akt signaling, insulin-like growth factor I, FOXO3, forkhead transcription factor, starvation, glucocorticoids, myotubes, muscle atrophy, transcriptional regulation
- MeSH terms
- Adenoviridae, Animals, Cells, Cultured, Cloning, Molecular, Fasting, Gene Expression Regulation, Genetic Vectors, Glucocorticoids, Insulin-Like Growth Factor I, Ligases, Models, Biological, Muscle Proteins, Muscular Atrophy, Promoter Regions, Genetic, Proto-Oncogene Proteins, Transcription Factors, Signal Transduction, Protein Serine-Threonine Kinases, Muscle, Skeletal, Phosphatidylinositol 3-Kinases, Muscle Cells, RNA Interference, Ubiquitin-Protein Ligases, SKP Cullin F-Box Protein Ligases, Proto-Oncogene Proteins c-akt, Mice
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