Mitochondrial fission and remodelling contributes to muscle atrophy
Open accessAbstract
Mitochondria are crucial organelles in the production of energy and in the control of signalling cascades. A machinery of pro-fusion and fission proteins regulates their morphology and subcellular localization. In muscle this results in an orderly pattern of intermyofibrillar and subsarcolemmal mitochondria. Muscular atrophy is a genetically controlled process involving the activation of the autophagy-lysosome and the ubiquitin-proteasome systems. Whether and how the mitochondria are involved in muscular atrophy is unknown. Here, we show that the mitochondria are removed through autophagy system and that changes in mitochondrial network occur in atrophying muscles. Expression of the fission machinery is per se sufficient to cause muscle wasting in adult animals, by triggering organelle dysfunction and AMPK activation. Conversely, inhibition of the mitochondrial fission inhibits muscle loss during fasting and after FoxO3 overexpression. Mitochondrial-dependent muscle atrophy requires AMPK activation as inhibition of AMPK restores muscle size in myofibres with altered mitochondria. Thus, disruption of the mitochondrial network is an essential amplificatory loop of the muscular atrophy programme.
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Co-transfecting mitochondria with DRP1 and FIS1 induces alterations in mitochondrial morphology and activates autophagy.
“Romanello et al. reported that co-transfecting mitochondria with DRP1 and FIS1 induces alterations in mitochondrial morphology and activates autophagy [50].”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [50]
Sustained DRP1/FIS1 contributes to a reduction in muscle fiber size and muscle atrophy.
“Over time, the sustained level of DRP1/FIS1 contributes to a reduction in muscle fiber size and muscle atrophy [50].”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [50]
Alterations in mitochondrial distribution, morphology, and function are present in atrophic muscles in aging, muscle disuse, burn injury, intensive care unit-acquired weakness, insulin resistance, chronic obstructive pulmonary disease, cancer cachexia, and different neuromuscular disorders.
“Alterations in mitochondrial distribution, morphology, and function are present in atrophic muscles in aging [148–150], muscle disuse [151, 152], burn injury [153], intensive care unit-acquired weakness [154], insulin resistance [155] chronic obstructive pulmonary disease (COPD) [156], cancer cachexia [157–159], and different neuromuscular disorders [160].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [152]
There is strong evidence in skeletal muscle supporting a causal link between dysregulation of mitochondrial fission and alterations in muscle maintenance.
“There is strong evidence in skeletal muscle that supports a causal link between the dysregulation of mitochondrial fission and alterations in muscle maintenance [152, 196, 197, 210, 211].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [152]
Acute overexpression of DRP1 is sufficient to activate mitochondrial dysfunction, mitophagy, and energy stress, which result in activation of an atrophy program via the AMPK-FoxO3 axis.
“Acute overexpression of DRP1 is sufficient to activate mitochondrial dysfunction, mitophagy, and energy stress, which result in the activation of an atrophy program via the AMPK–FoxO3 axis [152].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [152]
Activation of mitophagy triggered by transient overexpression of BNIP3 and BNIP3L induces muscle atrophy.
“The activation of mitophagy triggered by the transient overexpression of BNIP3 and BNIP3L induce muscle atrophy [15, 152].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [152]
Transient inhibition of BNIP3 in skeletal muscle partially protects from muscle loss induced by fasting, FoxO3, and FGF21 overexpression.
“In agreement, transient inhibition of BNIP3 in skeletal muscle partially protects from muscle loss induced by fasting, FoxO3, and FGF21 overexpression [15, 152, 212].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [152]
Overexpression of the fission proteins Drp1 and Fis1 in muscles causes muscle atrophy.
“On the other hand, the overexpression of the fission proteins Drp1 and Fis1 in muscles causes muscle atrophy [5,7].”
From Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles (2019) · cites this paper as [5]
Failure in mitochondrial-shaping processes has detrimental consequences for the maintenance of muscle mass and function.
“Accordingly, the failure in mitochondrial-shaping processes has detrimental consequences for the maintenance of muscle mass and function [4,5,6,7,8,13,29].”
From Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles (2019) · cites this paper as [5]
Overexpression of DRP1 is sufficient to activate an atrophy program via the AMPK-FoxO3 axis.
“we and others have shown that overexpression of DRP1 is sufficient to activate an atrophy program via the AMPK-FoxO3 axis10,11.”
From DRP1-mediated mitochondrial shape controls calcium homeostasis and muscle mass (2019) · cites this paper as [10]
Bnip3 inhibition reduces autophagosome formation and protects against muscle loss during atrophy.
“we already demonstrated that Bnip3 inhibition reduces autophagosome formation and protects against muscle loss during atrophy,25, 38”
From Fibroblast growth factor 21 controls mitophagy and muscle mass (2019) · cites this paper as [25]
Inhibition of mitochondrial fission by genetic silencing of Fis1 and Drp1 in skeletal muscle protects against muscle wasting induced by starvation or by overexpression of FoxO3a.
“Inhibition of mitochondrial fission by genetic silencing of Fis1 and Drp1 in skeletal muscle has been shown to protect against muscle wasting induced by starvation or by overexpression of the atrophying transcription factor FoxO3a [41].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [41]
Mitochondrial fission is essential for skeletal muscle health.
“Taken altogether, the findings discussed above clearly indicate that mitochondrial fission is essential for skeletal muscle health.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [41]
Increased fission via overexpression of Drp1 and Fis1 leads to fragmented mitochondria and increased autophagy culminating in muscle atrophy.
“increased fission via overexpression of fission proteins Drp1 and Fis1 leads to fragmented mitochondria and increased autophagy culminating in muscle atrophy.(Romanello, Guadagnin, Gomes, Roder, Sandri, Petersen, Milan, Masiero, Del, Foretz, Scorrano, Rudolf, and Sandri 2010)”
From Successful aging: Advancing the science of physical independence in older adults (2015) · cites this paper as Romanello et al. 2010
AMPK activation and FOXO transcription factors regulate the UPS and the autophagy-lysosome system.
“AMPK activation (118) and the Forkhead box class O (FOXO) transcription factor family regulates the ubiquitin proteasome system (UPS), and the autophagy-lysosome system.”
From Mitochondria initiate and regulate sarcopenia (2017) · cites this paper as [118]
In mice with a muscle-specific deficiency in Fis1 and Drp, diminished mitochondrial fission was associated with reduced muscle atrophy and attenuated activation of atrophy-related genes during fasting.
“Furthermore, the role of mitochondrion-shaping proteins has recently been investigated in mice with a muscle-specific deficiency in Fis1 and Drp: diminished mitochondrial fission was associated with reduced muscle atrophy and attenuated activation of atrophy-related genes during fasting (Romanello et al., 2010).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Romanello et al., 2010
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Cites
1 retracted
Wenz, T., Rossi, S. G., Rotundo, R. L., Spiegelman, B. M., & Moraes, C. T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911570106 · Cited by 600 · see citing works
RetractedIdentification 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 · see citing works
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 · see citing works
Self-citationKoves, T. R., Ussher, J. R., Noland, R. C., Slentz, D., Mosedale, M., Ilkayeva, O., Bain, J., Stevens, R., Dyck, J. R. B., Newgard, C. B., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.013 · Cited by 1,990 · see citing works
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 · see citing works
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 · see citing works
Self-citationDynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationNix is a selective autophagy receptor for mitochondrial clearance
Novak, I., Kirkin, V., McEwan, D. G., Zhang, J., Wild, P., Rozenknop, A., Rogov, V., Löhr, F., Popovic, D., Occhipinti, A., et al. (2010) · The EMBO Reports · doi:10.1038/embor.2009.256 · Cited by 1,309 · see citing works
Autophagy 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 · see citing works
Self-citationProtein degradation by the ubiquitin-proteasome pathway in normal and disease states
Lecker, S. H., Goldberg, A. L., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010083 · Cited by 1,234 · see citing works
Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission.
Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., & Mihara, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607279200 · Cited by 1,226 · see citing works
Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974 · see citing works
Self-citationSignaling in Muscle Atrophy and Hypertrophy
Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 830 · see citing works
Self-citationGreer, E. L., Oskoui, P. R., Banko, M. R., Maniar, J. M., Gygi, M. P., Gygi, S. P., & Brunet, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705325200 · Cited by 820 · see citing works
Greer, E. L., Dowlatshahi, D., Banko, M. R., Villen, J., Hoang, K., Blanchard, D., Gygi, S. P., & Brunet, A. (2007) · Current Biology · doi:10.1016/j.cub.2007.08.047 · Cited by 801 · see citing works
Response to myocardial ischemia/reperfusion injury involves Bnip3 and autophagy
Hamacher-Brady, A., Brady, N. R., Logue, S. E., Sayen, M. R., Jinno, M., Kirshenbaum, L. A., Gottlieb, R. A., & Gustafsson, Å. B. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401936 · Cited by 609 · see citing works
Sacheck, J. M., Hyatt, J. K., Raffaello, A., Thomas Jagoe, R., Roy, R. R., Reggie Edgerton, V., Lecker, S. H., & Goldberg, A. L. (2007) · The FASEB Journal · doi:10.1096/fj.06-6604com · Cited by 585 · see citing works
Eyre, H., Kahn, R., Robertson, R. M., the ACS/ADA/AHA Collaborative Writing Committee, ACS/ADA/AHA Collaborative Writing Committee Members, Clark, N. G., Doyle, C., Hong, Y., Gansler, T., Glynn, T., et al. (2004) · Circulation · doi:10.1161/01.cir.0000133321.00456.00 · Cited by 542 · see citing works
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 · see citing works
Self-citationMitochondrial dysfunction and apoptosis in myopathic mice with collagen VI deficiency
Irwin, W., Bergamin, N., Sabatelli, P., Reggiani, C., Megighian, A., Merlini, L., Braghetta, P., Columbaro, M., Volpin, D., Bressan, G. M., et al. (2003) · Nature Genetics · doi:10.1038/ng1270 · Cited by 509 · see citing works
Ohanna, M., Sobering, A. K., Lapointe, T., Lorenzo, L., Praud, C., Petroulakis, E., Sonenberg, N., Kelly, P. A., Sotiropoulos, A., & Pende, M. (2005) · Nature Cell Biology · doi:10.1038/ncb1231 · Cited by 392 · see citing works
Resistance Exercise Reverses Aging in Human Skeletal Muscle
Melov, S., Tarnopolsky, M. A., Beckman, K. B., Felkey, K., & Hubbard, A. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000465 · Cited by 348 · see citing works
Soriano, F. X., Liesa, M., Bach, D., Chan, D. C., Palacín, M., & Zorzano, A. (2006) · Diabetes · doi:10.2337/db05-0509 · Cited by 343 · cited 1× · see citing works
“…| All Rights Reserved 0261-4189/10 www.embojournal.org The EMBO Journal VOL 29 | NO 10 | 2010 &2010 European Molecular Biology Organization EMBO THE JOURNAL 1774 implicated in apoptosis as well as in the regulation of muscle metabolism (Soriano et al, 2006) or of cell cycle (Taguchi et al, 2007).”
BackgroundEyre, H. J., Kahn, R., Robertson, R. M., Clark, N. G., Doyle, C., Gansler, T. S., Glynn, T., Hong, Y., Smith, R. A., Taubert, K. A., et al. (2004) · CA A Cancer Journal for Clinicians · doi:10.3322/canjclin.54.4.190 · Cited by 328 · see citing works
The muscle-specific ubiquitin ligase atrogin-1/MAFbx mediates statin-induced muscle toxicity
Hanai, J., Cao, P., Tanksale, P., Imamura, S., Koshimizu, E., Zhao, J., Kishi, S., Yamashita, M., Phillips, P. S., Sukhatme, V. P., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32741 · Cited by 281 · see citing works
Nakashima, K., & Yakabe, Y. (2007) · Bioscience, biotechnology and biochemistry · doi:10.1271/bbb.70057 · Cited by 224 · see citing works
Bnip3 mediates mitochondrial dysfunction and cell death through Bax and Bak
Kubli, D. A., Ycaza, J. E., & Gustafsson, Å. B. (2007) · Biochemical Journal · doi:10.1042/bj20070319 · Cited by 208 · see citing works
In vivo monitoring of Ca2 + uptake into mitochondria of mouse skeletal muscle during contraction
Rudolf, R., Mongillo, M., Magalhães, P. J., & Pozzan, T. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403102 · Cited by 193 · see citing works
Self-citationAguilar, V. M., Alliouachene, S., Sotiropoulos, A., Sobering, A. K., Athéa, Y., Djouadi, F., Miraux, S., Thiaudière, E., Foretz, M., Viollet, B., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.05.006 · Cited by 182 · see citing works
Self-citationTherapeutic approaches for muscle wasting disorders
Lynch, G. S., Schertzer, J. D., & Ryall, J. G. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2006.11.004 · Cited by 152 · see citing works
(De)constructing Mitochondria: What For?
Dimmer, K. S., & Scorrano, L. (2006) · Physiology · doi:10.1152/physiol.00010.2006 · Cited by 151 · see citing works
Self-citationRudolf, R., Magalhães, P. J., & Pozzan, T. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601160 · Cited by 141 · see citing works
Self-citationThe changing shape of mitochondrial apoptosis
Wasilewski, M., & Scorrano, L. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.03.007 · Cited by 129 · see citing works
Self-citationAlirol, E., James, D. I., Huber, D., Marchetto, A., Vergani, L., Martinou, J., & Scorrano, L. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-05-0377 · Cited by 128 · see citing works
Self-citationThe role of mitochondria in aging of skeletal muscle
Figueiredo, P. A., Mota, M. P., Appell, H. J., & Duarte, J. A. (2008) · Biogerontology · doi:10.1007/s10522-007-9121-7 · Cited by 109 · see citing works
Burn injury causes mitochondrial dysfunction in skeletal muscle
Padfield, K. E., Astrakas, L. G., Zhang, Q., Gopalan, S., Dai, G., Mindrinos, M. N., Tompkins, R. G., Rahme, L. G., & Tzika, A. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501211102 · Cited by 101 · see citing works
Raffaello, A., Laveder, P., Romualdi, C., Bean, C., Toniolo, L., Germinario, E., Megighian, A., Danieli‐Betto, D., Reggiani, C., & Lanfranchi, G. (2005) · Physiological Genomics · doi:10.1152/physiolgenomics.00051.2005 · Cited by 73 · see citing works
Adams, V. (2007) · Frontiers in bioscience · doi:10.2741/2680 · Cited by 44 · see citing works
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Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797 · see citing works
Self-citationMechanisms 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 · see citing works
Self-citationCellular and molecular mechanisms of muscle atrophy
Bonaldo, P., & Sandri, M. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.010389 · Cited by 1,284 · see citing works
Self-citationAutophagy‐based unconventional secretory pathway for extracellular delivery of IL‐1β
Dupont, N., Jiang, S., Pilli, M., Ornatowski, W., Bhattacharya, D., & Deretic, V. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.398 · Cited by 967 · see citing works
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Sandri, M. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.04.023 · Cited by 689 · see citing works
Self-citationMitochondrial dysfunction and sarcopenia of aging: from signaling pathways to clinical trials
Marzetti, E., Calvani, R., Cesari, M., Buford, T. W., Lorenzi, M., Behnke, B. J., & Leeuwenburgh, C. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.024 · Cited by 627 · see citing works
A 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 · see citing works
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Hood, D. A., Memme, J. M., Oliveira, A. N., & Triolo, M. (2019) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114310 · Cited by 567 · see citing works
Grumati, P., Coletto, L., Sabatelli, P., Cescon, M., Angelin, A., Bertaggia, E., Blaauw, B., Urciuolo, A., Tiepolo, T., Merlini, L., et al. (2010) · Nature Medicine · doi:10.1038/nm.2247 · Cited by 540 · see citing works
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Seo, A. Y., Joseph, A.-M., Dutta, D., Hwang, J. C. Y., Aris, J. P., & Leeuwenburgh, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.070490 · Cited by 522 · see citing works
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Cartee, G. D., Hepple, R. T., Bamman, M. M., & Zierath, J. R. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.007 · Cited by 483 · see citing works
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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 · see citing works
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 · see citing works
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Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434 · see citing works
Self-citationLira, V. A., Okutsu, M., Zhang, M., Greene, N. P., Laker, R. C., Breen, D. S., Hoehn, K. L., & Yan, Z. (2013) · The FASEB Journal · doi:10.1096/fj.13-228486 · Cited by 432 · see citing works
Mitochondria and ageing: Role in heart, skeletal muscle and adipose tissue
Boengler, K., Kosiol, M., Mayr, M., Schulz, R., & Rohrbach, S. (2017) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12178 · Cited by 421 · see citing works
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Carnio, S., LoVerso, F., Baraibar, M. A., Longa, E., Khan, M. M., Maffei, M., Reischl, M., Canepari, M., Loefler, S., Kern, H., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.061 · Cited by 423 · see citing works
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Leidal, A. M., Levine, B., & Debnath, J. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0235-8 · Cited by 424 · see citing works
Sebastián, D., Sorianello, E., Segalés, J., Irazoki, A., Ruiz‐Bonilla, V., Sala, D., Planet, E., Berenguer‐Llergo, A., Muñoz, J. P., Sánchez‐Feutrie, M., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593084 · Cited by 396 · see citing works
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Favaro, G., Romanello, V., Varanita, T., Andrea Desbats, M., Morbidoni, V., Tezze, C., Albiero, M., Canato, M., Gherardi, G., De Stefani, D., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10226-9 · Cited by 398 · see citing works
Self-citationSandri, M., Barberi, L., Bijlsma, A. Y., Blaauw, B., Dyar, K. A., Milan, G., Mammucari, C., Meskers, C. G. M., Pallafacchina, G., Paoli, A., et al. (2013) · Biogerontology · doi:10.1007/s10522-013-9432-9 · Cited by 340 · see citing works
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Calvani, R., Joseph, A.-M., Adhihetty, P. J., Miccheli, A., Bossola, M., Leeuwenburgh, C., Bernabei, R., & Marzetti, E. (2013) · bchm · doi:10.1515/hsz-2012-0247 · Cited by 328 · see citing works
Successful aging: Advancing the science of physical independence in older adults
Anton, S. D., Woods, A. J., Ashizawa, T., Barb, D., Buford, T. W., Carter, C. S., Clark, D. J., Cohen, R. A., Corbett, D. B., Cruz-Almeida, Y., et al. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.09.005 · Cited by 292 · see citing works
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Leduc-Gaudet, J.-P., Picard, M., Pelletier, F. S.-J., Sgarioto, N., Auger, M.-J., Vallée, J., Robitaille, R., St-Pierre, D. H., & Gouspillou, G. (2015) · Oncotarget · doi:10.18632/oncotarget.4235 · Cited by 273 · see citing works
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“Inhibition of mitochondrial fission by genetic silencing of Fis1 and Drp1 in skeletal muscle has been shown to protect against muscle wasting induced by starvation or by overexpression of the atrophying transcription factor FoxO3a [41].”
BackgroundThe Role of AMPK in the Regulation of Skeletal Muscle Size, Hypertrophy, and Regeneration
Thomson, D. M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103125 · Cited by 267 · see citing works
White, J. P., Baynes, J. W., Welle, S. L., Kostek, M. C., Matesic, L. E., Sato, S., & Carson, J. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024650 · Cited by 260 · see citing works
“both atrogin1 and MuRF1 expression in muscle [77,78].”
Picard, M., Ritchie, D., Wright, K. J., Romestaing, C., Thomas, M. M., Rowan, S. L., Taivassalo, T., & Hepple, R. T. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00628.x · Cited by 238 · see citing works
Fibroblast growth factor 21 controls mitophagy and muscle mass
Oost, L. J., Kustermann, M., Armani, A., Blaauw, B., & Romanello, V. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12409 · Cited by 231 · see citing works
Self-citationSkeletal muscle aging and the mitochondrion
Johnson, M. L., Robinson, M. M., & Nair, K. S. (2013) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.12.003 · Cited by 233 · see citing works
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
Self-citationQuantitative 3D Mapping of the Human Skeletal Muscle Mitochondrial Network
Vincent, A. E., White, K., Davey, T., Philips, J., Ogden, R. T., Lawless, C., Warren, C., Hall, M. G., Ng, Y. S., Falkous, G., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.010 · Cited by 195 · see citing works
Skeletal muscle autophagy: a new metabolic regulator
Neel, B. A., Lin, Y., & Pessin, J. E. (2013) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.09.004 · Cited by 178 · see citing works
FoxO Transcription Factors Are Critical Regulators of Diabetes-Related Muscle Atrophy
O’Neill, B. T., Bhardwaj, G., Penniman, C. M., Krumpoch, M. T., Suarez Beltran, P. A., Klaus, K., Poro, K., Li, M., Pan, H., Dreyfuss, J. M., et al. (2019) · Diabetes · doi:10.2337/db18-0416 · Cited by 167 · see citing works
Cannavino, J., Brocca, L., Sandri, M., Grassi, B., Bottinelli, R., & Pellegrino, M. A. (2015) · The Journal of Physiology · doi:10.1113/jphysiol.2014.286740 · Cited by 166 · see citing works
Self-citationHuang, Y., Zhu, X., Chen, K., Lang, H., Zhang, Y., Hou, P., Ran, L., Zhou, M., Zheng, J., Yi, L., et al. (2019) · Aging · doi:10.18632/aging.101910 · Cited by 167 · see citing works
Unravelling the mechanisms regulating muscle mitochondrial biogenesis
Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159 · see citing works
JunB transcription factor maintains skeletal muscle mass and promotes hypertrophy
Raffaello, A., Milan, G., Masiero, E., Carnio, S., Lee, D., Lanfranchi, G., Goldberg, A. L., & Sandri, M. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201001136 · Cited by 156 · see citing works
Self-citationJoseph, A.-M., Adhihetty, P. J., Wawrzyniak, N. R., Wohlgemuth, S. E., Picca, A., Kujoth, G. C., Prolla, T. A., & Leeuwenburgh, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069327 · Cited by 161 · see citing works
Modulation 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 · see citing works
Mitochondria initiate and regulate sarcopenia
Alway, S. E., Mohamed, J. S., & Myers, M. J. (2017) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000101 · Cited by 153 · see citing works
“AMP-activated protein kinase (AMPK) and Sirtuin 1 (SIRT1) trigger the destruction of dysfunctional fragmented mitochondria through FoxO3-dependent autophagy (mitophagy) (94,118).”
BackgroundLokireddy, S., Wijesoma, I. W., Teng, S., Bonala, S., Gluckman, P. D., McFarlane, C., Sharma, M., & Kambadur, R. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.005 · Cited by 154 · see citing works
RetractedLo Verso, F., Carnio, S., Vainshtein, A., & Sandri, M. (2014) · Autophagy · doi:10.4161/auto.32154 · Cited by 146 · see citing works
Self-citationMuscle-specific Drp1 overexpression impairs skeletal muscle growth via translational attenuation
Touvier, T., De Palma, C., Rigamonti, E., Scagliola, A., Incerti, E., Mazelin, L., Thomas, J.-L., D'Antonio, M., Politi, L., Schaeffer, L., et al. (2015) · Cell Death & Disease · doi:10.1038/cddis.2014.595 · Cited by 140 · see citing works
Impaired Mitochondrial Dynamics and Bioenergetics in Diabetic Skeletal Muscle
Liu, R., Jin, P., LiqunYu, Wang, Y., Han, L., Shi, T., & Li, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092810 · Cited by 146 · see citing works
Protein breakdown in cancer cachexia
Sandri, M. (2016) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.11.002 · Cited by 134 · see citing works
Self-citationLiu, 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 · see citing works
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 · see citing works
Update on mitochondria and muscle aging: All wrong roads lead to sarcopenia
Picca, A., Calvani, R., Bossola, M., Allocca, E., Menghi, A., Pesce, V., Lezza, A. M. S., Bernabei, R., Landi, F., & Marzetti, E. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0331 · Cited by 116 · see citing works
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 · see citing works
Self-citationBori, Z., Zhao, Z., Koltai, E., Fatouros, I. G., Jamurtas, A. Z., Douroudos, I. I., Terzis, G., Chatzinikolaou, A., Sovatzidis, A., Draganidis, D., et al. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.03.004 · Cited by 108 · see citing works
Wang, D., Sun, H., Song, G., Yang, Y., Zou, X., Han, P., & Li, S. (2018) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201700941 · Cited by 102 · see citing works
The Interplay between Mitochondrial Morphology and Myomitokines in Aging Sarcopenia
Romanello, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010091 · Cited by 101 · see citing works
Self-citationDefective Autophagy and mTORC1 Signaling in Myotubularin Null Mice
Fetalvero, K. M., Yu, Y., Goetschkes, M., Liang, G., Valdez, R. A., Gould, T., Triantafellow, E., Bergling, S., Loureiro, J., Eash, J., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01075-12 · Cited by 96 · see citing works
Dulac, M., Leduc‐Gaudet, J., Reynaud, O., Ayoub, M., Guérin, A., Finkelchtein, M., Hussain, S. N., & Gouspillou, G. (2020) · The Journal of Physiology · doi:10.1113/jp279802 · Cited by 90 · see citing works
Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles
Romanello, V., Scalabrin, M., Albiero, M., Blaauw, B., Scorrano, L., & Sandri, M. (2019) · Cells · doi:10.3390/cells8060597 · Cited by 91 · see citing works
Self-citationGreene, N. P., Lee, D. E., Brown, J. L., Rosa, M. E., Brown, L. A., Perry, R. A., Henry, J. N., & Washington, T. A. (2015) · Physiological Reports · doi:10.14814/phy2.12470 · Cited by 89 · see citing works
Avellaneda, J., Rodier, C., Daian, F., Brouilly, N., Rival, T., Luis, N. M., & Schnorrer, F. (2021) · Nature Communications · doi:10.1038/s41467-021-22058-7 · Cited by 92 · see citing works
Mitochondrial dynamics in cancer-induced cachexia
van der Ende, M., Grefte, S., Plas, R., Meijerink, J., Witkamp, R. F., Keijer, J., & van Norren, K. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.07.008 · Cited by 87 · see citing works
Mitochondrial Dysfunction in Skeletal Muscle Pathologies
Abrigo, J., Simon, F., Cabrera, D., Vilos, C., & Cabello-Verrugio, C. (2019) · Current Protein & Peptide Science · doi:10.2174/1389203720666190402100902 · Cited by 88 · see citing works
Halling, J. F., Ringholm, S., Olesen, J., Prats, C., & Pilegaard, H. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.05.020 · Cited by 86 · see citing works
Sarcopenic obesity: satellite cells in the aging muscle
Thornell, L.-E. (2011) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e3283412260 · Cited by 86 · see citing works
Pgc-1α overexpression Via local transfection attenuates mitophagy pathway in muscle disuse atrophy
Kang, C., & Ji, L. L. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.032 · Cited by 83 · see citing works
Protective Effects of Ghrelin on Fasting-Induced Muscle Atrophy in Aging Mice
Wu, C.-S., Wei, Q., Wang, H., Kim, D. M., Balderas, M., Wu, G., Lawler, J., Safe, S., Guo, S., Devaraj, S., et al. (2020) · The Journals of Gerontology: Series A · doi:10.1093/gerona/gly256 · Cited by 81 · see citing works
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 · see citing works
Kravic, B., Harbauer, A. B., Romanello, V., Simeone, L., Vögtle, F.-N., Kaiser, T., Straubinger, M., Huraskin, D., Böttcher, M., Cerqua, C., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1403716 · Cited by 75 · see citing works
Self-citationRole of Autophagy in COPD Skeletal Muscle Dysfunction
Hussain, S. N. A., & Sandri, M. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00893.2012 · Cited by 77 · see citing works
Self-citationMitochondrial adaptations in skeletal muscle to hindlimb unloading
Wagatsuma, A., Kotake, N., Kawachi, T., Shiozuka, M., Yamada, S., & Matsuda, R. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0677-1 · Cited by 70 · see citing works
Loss of <i>Parkin</i> impairs mitochondrial function and leads to muscle atrophy
Peker, N., Donipadi, V., Sharma, M., McFarlane, C., & Kambadur, R. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00064.2017 · Cited by 68 · see citing works
Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3
Lin, L., Chen, K., Khalek, W. A., Ward, J. L., Yang, H., Chabi, B., Wrutniak-Cabello, C., & Tong, Q. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085636 · Cited by 67 · see citing works
Huang, Y., Chen, K., Ren, Q., Yi, L., Zhu, J., Zhang, Q., & Mi, M. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000493040 · Cited by 64 · see citing works
Zhang, X., Trevino, M. B., Wang, M., Gardell, S. J., Ayala, J. E., Han, X., Kelly, D. P., Goodpaster, B. H., Vega, R. B., & Coen, P. M. (2018) · The Journals of Gerontology: Series A · doi:10.1093/gerona/gly051 · Cited by 58 · see citing works
Marzetti, E., Calvani, R., Lorenzi, M., Tanganelli, F., Picca, A., Bossola, M., Menghi, A., Bernabei, R., & Landi, F. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.04.003 · Cited by 58 · see citing works
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 · see citing works
Kitaoka, Y., Ogasawara, R., Tamura, Y., Fujita, S., & Hatta, H. (2015) · Applied Physiology Nutrition and Metabolism · doi:10.1139/apnm-2015-0184 · Cited by 54 · see citing works
Castets, P., Frank, S., Sinnreich, M., & Rüegg, M. A. (2016) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-160153 · Cited by 49 · see citing works
Mitochondrial dynamics in aging and disease
Bereiter-Hahn, J. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394625-6.00004-0 · Cited by 48 · see citing works
Sun, L., Miyaji, N., Yang, M., Mills, E. M., Taniyama, S., Uchida, T., Nikawa, T., Li, J., Shi, J., Tachibana, K., et al. (2021) · Nutrients · doi:10.3390/nu13020379 · Cited by 45 · see citing works
Lee, H., Lim, J.-Y., & Choi, S.-J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2739721 · Cited by 43 · see citing works
Facts and controversies in our understanding of how caloric restriction impacts the mitochondrion
Gouspillou, G., & Hepple, R. T. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.03.004 · Cited by 42 · see citing works
Lee, S.-J., Bae, J. H., Lee, H., Lee, H., Park, J., Kang, J.-S., & Bae, G.-U. (2019) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2019.112054 · Cited by 38 · see citing works
Regulatory role of exercise-induced autophagy for sarcopenia
Liang, J., Zeng, Z., Zhang, Y., & Chen, N. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2019.110789 · Cited by 33 · see citing works
Picca, A., Calvani, R., Lorenzi, M., Menghi, A., Galli, M., Vitiello, R., Randisi, F., Bernabei, R., Landi, F., & Marzetti, E. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.06.005 · Cited by 32 · see citing works
Jun, L., Tao, Y.-X., Geetha, T., & Babu, J. R. (2024) · Current Nutrition Reports · doi:10.1007/s13668-024-00555-7 · Cited by 27 · see citing works
Arneson‐Wissink, P. C., Hogan, K. A., Ducharme, A. M., Samani, A., Jatoi, A., & Doles, J. D. (2020) · JCSM Rapid Communications · doi:10.1002/rco2.14 · Cited by 21 · see citing works
- Authors
- Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., Scorrano, L., Rudolf, R., & Sandri, M.
- Affiliations
- Veneto Institute of Molecular Medicine (IT)
- Karlsruhe Institute of Technology (DE)
- Centre National de la Recherche Scientifique (FR)
- University of Padua (IT)
- Corresponding author
- Sandri, Marco
- Venue
- The EMBO Journal
- Published
- 2010-04-16
- Volume
- 29
- Issue
- 10
- Pages
- 1774-1785
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2876965
- OpenAlex
- W2114063620
- Cited by
- 596
- References
- 41
- Citations by year
- 2026: 11 · 2025: 32 · 2024: 27 · 2023: 27 · 2022: 41 · 2021: 45 · 2020: 32 · 2019: 42 · 2018: 44 · 2017: 39 · 2016: 35 · 2015: 41 · 2014: 41 · 2013: 47 · 2012: 47
- FWCI
- 17.99
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- European Commission (223576)
- Deutsche Forschungsgemeinschaft
- Ministero dell’Istruzione, dell’Università e della Ricerca (PRIN2007)
- Associazione Italiana per la Ricerca sul Cancro (PRIN 2007)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial fission, mitochondrial remodeling, muscle atrophy, AMPK activation, autophagy, FOXO3, fasting, mitochondrial network, ubiquitin-proteasome system
- MeSH terms
- Animals, Autophagy, Cell Line, Humans, Microscopy, Fluorescence, Mitochondria, Models, Biological, Muscular Atrophy, Time Factors, Transfection, Signal Transduction, Muscle, Skeletal, RNA Interference, Mice, AMP-Activated Protein Kinases
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