Parkin is required for exercise-induced mitophagy in muscle: Impact of aging
Abstract
The maintenance of muscle health with advancing age is dependent on mitochondrial homeostasis. While reductions in mitochondrial biogenesis have been observed with age, less is known regarding organelle degradation. Parkin is an E3 ubiquitin ligase implicated in mitophagy, but few studies have examined Parkin’s contribution to mitochondrial turnover in muscle. Wild-type (WT) and Parkin knockout (KO) mice were used to delineate a role for Parkin-mediated mitochondrial degradation in aged muscle, in concurrence with exercise. Aged animals exhibited declines in muscle mass and mitochondrial content, paralleled by a nuclear environment endorsing the transcriptional repression of mitochondrial biogenesis. Mitophagic signaling was enhanced following acute endurance exercise in young WT mice but was abolished in the absence of Parkin. Basal mitophagy flux of the autophagosomal protein lipidated microtubule-associated protein 1A/1B-light chain 3 was augmented in aged animals but did not increase additionally with exercise when compared with young animals. In the absence of Parkin, exercise increased the nuclear localization of Parkin-interacting substrate, corresponding to a decrease in nuclear peroxisome proliferator gamma coactivator-1α. Remarkably, exercise enhanced mitochondrial ubiquitination in both young WT and KO animals. This suggested compensation of alternative ubiquitin ligases that were, however, unable to restore the diminished exercise-induced mitophagy in KO mice. Under basal conditions, we demonstrated that Parkin was required for mitochondrial mitofusin-2 ubiquitination. We also observed an abrogation of exercise-induced mitophagy in aged muscle. Our results demonstrate that acute exercise-induced mitophagy is dependent on Parkin and attenuated with age, which likely contributes to changes in mitochondrial content and quality in aging muscle.
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Mitophagy-related proteins are decreased in the skeletal muscle of old rodents, although conflicting data exist.
“Although conflicting data exist [54,145,146,147], several studies reported that mitophagy-related proteins are decreased in the skeletal muscle of old rodents [46,120,148,149,150,151,152].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [147]
Muscles of Parkin-deficient mice display impaired mitochondrial energetics.
“We and others have reported that muscles of Parkin-deficient mice display several aging-like features, including contractile dysfunction [154] and impaired mitochondrial energetics [147,153,154,155].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [147]
In the majority of studies that reported an increase in Parkin content in aged muscles, mitophagy was also reported to be impaired or insufficient in aged skeletal muscles.
“Importantly, the majority of studies that reported an increase in Parkin content in aged muscles also reported that mitophagy was impaired/insufficient in aged skeletal muscles [145,146,147].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [147]
Muscles from Parkin-deficient mice display lower mitophagy flux in response to acute exercise and endurance training.
“For instance, it has been reported that muscles from Parkin-deficient mice display lower mitophagy flux in response to acute exercise [147] and endurance training [153].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [147]
Under conditions of stress, injury or aging, mitochondrial kinase PINK1 gathers outside the membrane of dysfunctional mitochondria and translocates them into it selectively by phosphorylating and recruiting Parkin, and then ubiquitinates outer mitochondrial membrane proteins such as Mfn1/2 and Drp1 to participate in mitophagy.
“Under the conditions of stress, injury or aging, mitochondrial kinase PINK1 can gather outside the membrane of dysfunctional mitochondria and translocate them into it selectively by phosphorylating and recruiting Parkin, and then ubiquitinate outer mitochondrial membrane proteins such as mitochondrial fusion key proteins Mfn1/2 and fission key protein Drp1 to participate in mitophagy [48].”
From Lifelong Aerobic Exercise Alleviates Sarcopenia by Activating Autophagy and Inhibiting Protein Degradation via the AMPK/PGC-1α Signaling Pathway (2021) · cites this paper as [48]
Cites
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578 · see citing works
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026 · see citing works
Mitochondrial Fission, Fusion, and Stress
Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · see citing works
TFEB Links Autophagy to Lysosomal Biogenesis
Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365 · see citing works
Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276 · see citing works
Janssen, I., Heymsfield, S. B., & Ross, R. (2002) · Journal of the American Geriatrics Society · doi:10.1046/j.1532-5415.2002.50216.x · Cited by 3,139 · see citing works
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082 · see citing works
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944 · see citing works
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835 · see citing works
A Gene Network Regulating Lysosomal Biogenesis and Function
Sardiello, M., Palmieri, M., di Ronza, A., Medina, D. L., Valenza, M., Gennarino, V. A., Di Malta, C., Donaudy, F., Embrione, V., Polishchuk, R. S., et al. (2009) · Science · doi:10.1126/science.1174447 · Cited by 2,543 · see citing works
Ubiquitin is phosphorylated by PINK1 to activate parkin
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477 · see citing works
Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375 · see citing works
PINK1-Phosphorylated Mitofusin 2 Is a Parkin Receptor for Culling Damaged Mitochondria
Chen, Y., & Dorn, G. W. (2013) · Science · doi:10.1126/science.1231031 · Cited by 1,323 · see citing works
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298 · 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
Mitochondrial pathology and apoptotic muscle degeneration in <i>Drosophila parkin</i> mutants
Greene, J. C., Whitworth, A. J., Kuo, I., Andrews, L. A., Feany, M. B., & Pallanck, L. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0737556100 · Cited by 1,203 · see citing works
Exercise-induced BCL2-regulated autophagy is required for muscle glucose homeostasis
He, C., Bassik, M. C., Moresi, V., Sun, K., Wei, Y., Zou, Z., An, Z., Loh, J., Fisher, J., Sun, Q., et al. (2012) · Nature · doi:10.1038/nature10758 · Cited by 1,136 · see citing works
Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
Sarraf, S. A., Raman, M., Guarani, V., Sowa, M. E., Huttlin, E. L., Gygi, S. P., & Harper, J. W. (2013) · Nature · doi:10.1038/nature12043 · Cited by 1,020 · see citing works
Mitochondrial Dysfunction and Oxidative Damage in parkin-deficient Mice
Palacino, J. J., Sagi, D., Goldberg, M. S., Krauss, S., Motz, C., Wacker, M., Klose, J., & Shen, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401135200 · Cited by 995 · see citing works
PARIS (ZNF746) Repression of PGC-1α Contributes to Neurodegeneration in Parkinson's Disease
Shin, J.-H., Ko, H. S., Kang, H., Lee, Y., Lee, Y.-I., Pletinkova, O., Troconso, J. C., Dawson, V. L., & Dawson, T. M. (2011) · Cell · doi:10.1016/j.cell.2011.02.010 · Cited by 953 · see citing works
Parkin-deficient Mice Exhibit Nigrostriatal Deficits but Not Loss of Dopaminergic Neurons
Goldberg, M. S., Fleming, S. M., Palacino, J. J., Cepeda, C., Lam, H. A., Bhatnagar, A., Meloni, E. G., Wu, N., Ackerson, L. C., Klapstein, G. J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308947200 · Cited by 913 · see citing works
Gegg, M. E., Cooper, J. M., Chau, K.-Y., Rojo, M., Schapira, A. H. V., & Taanman, J.-W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq419 · Cited by 910 · see citing works
The PINK1/Parkin pathway regulates mitochondrial morphology
Poole, A. C., Thomas, R. E., Andrews, L. A., McBride, H. M., Whitworth, A. J., & Pallanck, L. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709336105 · Cited by 885 · see citing works
The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy
Bingol, B., Tea, J. S., Phu, L., Reichelt, M., Bakalarski, C. E., Song, Q., Foreman, O., Kirkpatrick, D. S., & Sheng, M. (2014) · Nature · doi:10.1038/nature13418 · Cited by 855 · see citing works
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65
Kazlauskaite, A., Kondapalli, C., Gourlay, R., Campbell, D. G., Ritorto, M. S., Hofmann, K., Alessi, D. R., Knebel, A., Trost, M., & Muqit, M. M. K. (2014) · Biochemical Journal · doi:10.1042/bj20140334 · Cited by 806 · see citing works
The mitochondrial‐lysosomal axis theory of aging
Brunk, U. T., & Terman, A. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02869.x · Cited by 729 · see citing works
Invited Review: Contractile activity-induced mitochondrial biogenesis in skeletal muscle
Hood, D. A. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.90.3.1137 · Cited by 692 · see citing works
Self-citationLazarou, M., Jin, S. M., Kane, L. A., & Youle, R. J. (2012) · Developmental Cell · doi:10.1016/j.devcel.2011.12.014 · Cited by 670 · see citing works
Hoshino, A., Mita, Y., Okawa, Y., Ariyoshi, M., Iwai-Kanai, E., Ueyama, T., Ikeda, K., Ogata, T., & Matoba, S. (2013) · Nature Communications · doi:10.1038/ncomms3308 · Cited by 536 · see citing works
The metabolic footprint of aging in mice
Houtkooper, R. H., Argmann, C., Houten, S. M., Cantó, C., Jeninga, E. H., Andreux, P. A., Thomas, C., Doenlen, R., Schoonjans, K., & Auwerx, J. (2011) · Scientific Reports · doi:10.1038/srep00134 · Cited by 528 · see citing works
Exercise-induced mitochondrial biogenesis begins before the increase in muscle PGC-1α expression.
Wright, D. C., Han, D.-H., Garcia-Roves, P. M., Geiger, P. C., Jones, T. E., & Holloszy, J. O. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m606116200 · Cited by 488 · see citing works
Parkin-mediated mitophagy directs perinatal cardiac metabolic maturation in mice
Gong, G., Song, M., Csordás, G., Kelly, D. P., Matkovich, S. J., & Dorn, G. W. (2015) · Science · doi:10.1126/science.aad2459 · Cited by 441 · see citing works
Mitochondrial function and apoptotic susceptibility in aging skeletal muscle
Chabi, B., Ljubicic, V., Menzies, K. J., Huang, J. H., Saleem, A., & Hood, D. A. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2007.00347.x · Cited by 437 · see citing works
Self-citationSebastián, 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
Decline with age of the respiratory chain activity in human skeletal muscle
Boffoli, D., Scacco, S. C., Vergari, R., Solarino, G., Santacroce, G., & Papa, S. (1994) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(94)90061-2 · Cited by 341 · see citing works
Cooper, J. A. D., Mann, V. M., & Schapira, A. H. V. (1992) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(92)90270-u · Cited by 335 · see citing works
Rana, A., Rera, M., & Walker, D. W. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216197110 · Cited by 335 · see citing works
Yun, J., Puri, R., Yang, H. M., Lizzio, M. A., Wu, C., Sheng, Z., & Guo, M. (2014) · eLife · doi:10.7554/elife.01958 · Cited by 325 · see citing works
Transcription Factor EB Controls Metabolic Flexibility during Exercise
Mansueto, G., Armani, A., Viscomi, C., D’Orsi, L., De Cegli, R., Polishchuk, E. V., Lamperti, C., Di Meo, I., Romanello, V., Marchet, S., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.11.003 · Cited by 314 · see citing works
MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5
Nezich, C. L., Wang, C., Fogel, A. I., & Youle, R. J. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201501002 · Cited by 309 · see citing works
Mitochondrial E3 ligase MARCH5 regulates FUNDC1 to fine‐tune hypoxic mitophagy
Chen, Z., Liu, L., Cheng, Q., Li, Y., Wu, H., Zhang, W., Wang, Y., Sehgal, S. A., Siraj, S., Wang, X., et al. (2017) · EMBO Reports · doi:10.15252/embr.201643309 · Cited by 295 · see citing works
Cogswell, A. M., Stevens, R. J., & Hood, D. A. (1993) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1993.264.2.c383 · Cited by 286 · see citing works
Self-citationShimura, H., Hattori, N., Kubo, S., Yoshikawa, M., Kitada, T., Matsumine, H., Asakawa, S., Minoshima, S., Yamamura, Y., Shimizu, N., et al. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199905)45:5 · Cited by 282 · see citing works
Role of PGC-1α during acute exercise-induced autophagy and mitophagy in skeletal muscle
Vainshtein, A., Tryon, L. D., Pauly, M., & Hood, D. A. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00380.2014 · Cited by 273 · see citing works
Self-citationGrumati, P., Coletto, L., Schiavinato, A., Castagnaro, S., Bertaggia, E., Sandri, M., & Bonaldo, P. (2011) · Autophagy · doi:10.4161/auto.7.12.17877 · Cited by 267 · see citing works
Parkin loss leads to PARIS-dependent declines in mitochondrial mass and respiration
Stevens, D. A., Lee, Y., Kang, H. C., Lee, B. D., Lee, Y.-I., Bower, A., Jiang, H., Kang, S.-U., Andrabi, S. A., Dawson, V. L., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500624112 · Cited by 257 · see citing works
Quantitation of "autophagic flux" in mature skeletal muscle
Ju, J.-S., Varadhachary, A. S., Miller, S. E., & Weihl, C. C. (2010) · Autophagy · doi:10.4161/auto.6.7.12785 · Cited by 229 · see citing works
Deubiquitinating enzymes regulate PARK2-mediated mitophagy
Wang, Y., Serricchio, M., Jauregui, M., Shanbhag, R., Stoltz, T., Paolo, C. T. D., Kim, P. K., & McQuibban, G. A. (2015) · Autophagy · doi:10.1080/15548627.2015.1034408 · Cited by 220 · see citing works
PINK1 Primes Parkin-Mediated Ubiquitination of PARIS in Dopaminergic Neuronal Survival
Lee, Y., Stevens, D. A., Kang, S.-U., Jiang, H., Lee, Y.-I., Ko, H. S., Scarffe, L. A., Umanah, G. K. E., Kang, H., Ham, S., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2016.12.090 · Cited by 207 · see citing works
Regulation of mitophagy by the Gp78 E3 ubiquitin ligase
Fu, M., St-Pierre, P., Shankar, J., Wang, P. T. C., Joshi, B., & Nabi, I. R. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-08-0607 · Cited by 204 · see citing works
Mitochondria, Muscle Health, and Exercise with Advancing Age
Carter, H. N., Chen, C. C. W., & Hood, D. A. (2015) · Physiology · doi:10.1152/physiol.00039.2014 · Cited by 191 · see citing works
Self-citationIqbal, S., Ostojic, O., Singh, K., Joseph, A., & Hood, D. A. (2013) · Muscle & Nerve · doi:10.1002/mus.23838 · Cited by 169 · see citing works
Self-citationSirtuin 1-mediated Effects of Exercise and Resveratrol on Mitochondrial Biogenesis
Menzies, K. J., Singh, K., Saleem, A., & Hood, D. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.431155 · Cited by 167 · see citing works
Self-citationAdaptive plasticity of autophagic proteins to denervation in aging skeletal muscle
O'Leary, M. F., Vainshtein, A., Iqbal, S., Ostojic, O., & Hood, D. A. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00240.2012 · Cited by 165 · see citing works
Self-citationAcute endurance exercise increases the nuclear abundance of PGC-1α in trained human skeletal muscle
Little, J. P., Safdar, A., Cermak, N. M., Tarnopolsky, M. A., & Gibala, M. J. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00409.2009 · Cited by 163 · 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
Self-citationPicard, M. A., Ritchie, D., Thomas, M. M., Wright, K. J., & Hepple, R. T. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00745.x · Cited by 145 · see citing works
Molecular basis for an attenuated mitochondrial adaptive plasticity in aged skeletal muscle
Ljubicic, V., Joseph, A.-M., Adhihetty, P. J., Huang, J. H., Saleem, A., Uguccioni, G., & Hood, D. A. (2009) · Aging · doi:10.18632/aging.100083 · Cited by 98 · see citing works
Self-citationLjubicic, V., & Hood, D. A. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00483.x · Cited by 87 · see citing works
Self-citationParkin Protects against Mitochondrial Toxins and β-Amyloid Accumulation in Skeletal Muscle Cells
Rosen, K. M., Veereshwarayya, V., Moussa, C., Fu, Q., Goldberg, M. S., Schlossmacher, M. G., Shen, J., & Querfurth, H. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512649200 · Cited by 84 · see citing works
Nabben, M., Joris Hoeks, J., Briedé, J. J., Glatz, J. F. C., Moonen‐Kornips, E., Hesselink, M. K. C., & Schrauwen, P. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.11.016 · Cited by 84 · see citing works
Age modifies respiratory complex I and protein homeostasis in a muscle type‐specific manner
Kruse, S. E., Karunadharma, P. P., Basisty, N., Johnson, R. S., Beyer, R. P., MacCoss, M. J., Rabinovitch, P. S., & Marcinek, D. J. (2015) · Aging Cell · doi:10.1111/acel.12412 · Cited by 73 · see citing works
Saleem, A., Carter, H. N., & Hood, D. A. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00270.2013 · Cited by 71 · see citing works
Self-citationRegulation of the autophagy system during chronic contractile activity-induced muscle adaptations
Kim, Y., & Hood, D. A. (2017) · Physiological Reports · doi:10.14814/phy2.13307 · Cited by 40 · see citing works
Self-citationEffect of p53 on mitochondrial morphology, import, and assembly in skeletal muscle
Saleem, A., Iqbal, S., Zhang, Y., & Hood, D. A. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00253.2014 · Cited by 39 · see citing works
Self-citationSiddiqui, A., Rane, A., Rajagopalan, S., Chinta, S. J., & Andersen, J. K. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.05.009 · Cited by 35 · see citing works
Zhang, Y., Iqbal, S., O′Leary, M. F. N., Menzies, K. J., Saleem, A., Ding, S., & Hood, D. A. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00058.2013 · Cited by 27 · see citing works
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Maintenance of Skeletal Muscle Mitochondria in Health, Exercise, and Aging
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
Self-citationMitophagy curtails cytosolic mtDNA-dependent activation of cGAS/STING inflammation during aging
Jiménez‐Loygorri, J. I., Villarejo‐Zori, B., Viedma-Poyatos, Á., Zapata‐Muñoz, J., Benítez‐Fernández, R., Frutos-Lisón, M. D., Tomás-Barberán, F. A., Espı́n, J. C., Área-Gómez, E., Gómez-Durán, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45044-1 · Cited by 381 · see citing works
Exercise and mitochondrial health
Memme, J. M., Erlich, A. T., Phukan, G., & Hood, D. A. (2021) · The Journal of Physiology · doi:10.1113/jp278853 · Cited by 343 · see citing works
Self-citationSkeletal muscle mitochondrial remodeling in exercise and diseases
Gan, Z., Fu, T., Kelly, D. P., & Vega, R. B. (2018) · Cell Research · doi:10.1038/s41422-018-0078-7 · Cited by 287 · see citing works
Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging
Leduc-Gaudet, J.-P., Hussain, S. N. A., Barreiro, E., & Gouspillou, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158179 · Cited by 268 · see citing works
“For instance, it has been reported that muscles from Parkin-deficient mice display lower mitophagy flux in response to acute exercise [147] and endurance traini g [153].”
BackgroundMitophagy pathways in health and disease
Killackey, S. A., Philpott, D. J., & Girardin, S. E. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202004029 · Cited by 236 · see citing works
Role of Age-Related Mitochondrial Dysfunction in Sarcopenia
Ferri, E., Marzetti, E., Calvani, R., Picca, A., Cesari, M., & Arosio, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155236 · Cited by 224 · see citing works
Physical Exercise: A Novel Tool to Protect Mitochondrial Health
Sorriento, D., Di Vaia, E., & Iaccarino, G. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.660068 · Cited by 118 · see citing works
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Stacchiotti, A., Favero, G., & Rodella, L. F. (2020) · Cells · doi:10.3390/cells9020288 · Cited by 115 · see citing works
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The clinical impact and biological mechanisms of skeletal muscle aging
Aversa, Z., Zhang, X., Fielding, R. A., Lanza, I. R., & LeBrasseur, N. K. (2019) · Bone · doi:10.1016/j.bone.2019.05.021 · Cited by 104 · see citing works
Lei, Y., Gan, M., Qiu, Y., Chen, Q., Wang, X., Liao, T., Zhao, M., Chen, L., Zhang, S., Zhao, Y., et al. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00572-y · Cited by 100 · see citing works
Mitochondrial Impairment in Sarcopenia
Bellanti, F., Buglio, A. L., & Vendemiale, G. (2021) · Biology · doi:10.3390/biology10010031 · Cited by 99 · see citing works
Mitochondrial Properties in Skeletal Muscle Fiber
Dong, H., & Tsai, S. (2023) · Cells · doi:10.3390/cells12172183 · Cited by 95 · see citing works
Ubiquitin Ligases at the Heart of Skeletal Muscle Atrophy Control
Peris-Moreno, D., Cussonneau, L., Combaret, L., Polge, C., & Taillandier, D. (2021) · Molecules · doi:10.3390/molecules26020407 · Cited by 87 · see citing works
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 · see citing works
Mitochondrial Mechanisms of Neuromuscular Junction Degeneration with Aging
Anagnostou, M., & Hepple, R. T. (2020) · Cells · doi:10.3390/cells9010197 · Cited by 81 · see citing works
Exercise-Induced Mitophagy in Skeletal Muscle and Heart
Guan, Y., Drake, J. C., & Yan, Z. (2019) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000192 · Cited by 79 · see citing works
Triolo, M., Oliveira, A. N., Kumari, R., & Hood, D. A. (2022) · Skeletal Muscle · doi:10.1186/s13395-022-00296-7 · Cited by 75 · see citing works
“We have previously reported that basal mitophagy flux is enhanced in aged muscle [22, 24] but in contrast to young muscle, that it is unresponsive to the stress of acute exercise.”
BackgroundSelf-citationAt the heart of mitochondrial quality control: many roads to the top
Gottlieb, R. A., Piplani, H., Sin, J., Sawaged, S., Hamid, S. M., TAYLOR, D. J., & Germano, J. D. F. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03772-3 · Cited by 67 · see citing works
Drake, J. C., Laker, R. C., Wilson, R. J., Zhang, M., & Yan, Z. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1559556 · Cited by 65 · see citing works
Mitochondrial dynamics in exercise physiology
Tanaka, T., Nishimura, A., Nishiyama, K., Goto, T., Numaga‐Tomita, T., & Nishida, M. (2019) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-019-02258-3 · Cited by 66 · see citing works
Ito, A., Hashimoto, M., Tanihata, J., Matsubayashi, S., Sasaki, R., Fujimoto, S., Kawamoto, H., Hosaka, Y., Ichikawa, A., Kadota, T., et al. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12988 · Cited by 62 · see citing works
Exercise Alleviates Cardiovascular Diseases by Improving Mitochondrial Homeostasis
Zhang, H., Zhang, Y., Zhang, J., & Jia, D. (2024) · Journal of the American Heart Association · doi:10.1161/jaha.124.036555 · Cited by 64 · see citing works
Ageing of skeletal muscle extracellular matrix and mitochondria: finding a potential link
Cai, L., Shi, L., Peng, Z., Sun, Y., & Chen, J. (2023) · Annals of Medicine · doi:10.1080/07853890.2023.2240707 · Cited by 60 · see citing works
The influence of aerobic exercise on mitochondrial quality control in skeletal muscle
Philp, A. M., Saner, N. J., Lazarou, M., Ganley, I. G., & Philp, A. (2020) · The Journal of Physiology · doi:10.1113/jp279411 · Cited by 58 · see citing works
Manifestations of Age on Autophagy, Mitophagy and Lysosomes in Skeletal Muscle
Triolo, M., & Hood, D. A. (2021) · Cells · doi:10.3390/cells10051054 · Cited by 57 · see citing works
Self-citationMitophagy Regulates Neurodegenerative Diseases
Cen, X., Zhang, M., Zhou, M., Ye, L., & Xia, H. (2021) · Cells · doi:10.3390/cells10081876 · Cited by 58 · see citing works
Redox Signaling and Sarcopenia: Searching for the Primary Suspect
Foreman, N. A., Hesse, A. S., & Ji, L. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22169045 · Cited by 52 · see citing works
Exercise improves vascular health: Role of mitochondria
Zhang, X., & Gao, F. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.11.002 · Cited by 52 · see citing works
Li, J., Wang, Z., Li, C., Song, Y., Wang, Y., Hai, B., & Zhang, Y. (2022) · Cells · doi:10.3390/cells11132086 · Cited by 52 · see citing works
The Role of Mitophagy in Skeletal Muscle Damage and Regeneration
Chatzinikita, E., Maridaki, M. D., Palikaras, K., Koutsilieris, M., & Philippou, Α. (2023) · Cells · doi:10.3390/cells12050716 · Cited by 53 · see citing works
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 · see citing works
Mitochondrial quality control in cardiac fibrosis: Epigenetic mechanisms and therapeutic strategies
Lin, L.-C., Tu, B., Song, K., Liu, Z., Sun, H., Zhou, Y., Sha, J.-M., Yang, J., Ye, Z., Zhao, J., et al. (2023) · Metabolism · doi:10.1016/j.metabol.2023.155626 · Cited by 51 · see citing works
Sligar, J., Debruin, D. A., Saner, N. J., Philp, A. M., & Philp, A. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00388.2021 · Cited by 49 · see citing works
Ubiquitin Ligases in Longevity and Aging Skeletal Muscle
Hughes, D. C., Baehr, L. M., Waddell, D. S., Sharples, A. P., & Bodine, S. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147602 · Cited by 45 · see citing works
McKendry, J., Coletta, G., Nunes, E. A., Lim, C., & Phillips, S. M. (2024) · Experimental Physiology · doi:10.1113/ep091937 · Cited by 43 · see citing works
Targeting mitochondrial quality control for treating sarcopenia: lessons from physical exercise
Picca, A., Calvani, R., Leeuwenburgh, C., Coelho‐Júnior, H. J., Bernabei, R., Landi, F., & Marzetti, E. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2019.1559827 · Cited by 42 · see citing works
Regulatory Roles of PINK1-Parkin and AMPK in Ubiquitin-Dependent Skeletal Muscle Mitophagy
Seabright, A. P., & Lai, Y. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.608474 · Cited by 41 · see citing works
Regulatory networks coordinating mitochondrial quality control in skeletal muscle
Slavin, M. B., Memme, J. M., Oliveira, A. N., Moradi, N., & Hood, D. A. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00065.2022 · Cited by 40 · see citing works
Self-citationCurcumin as a Therapeutic Agent for Sarcopenia
Gany, S. L. S., Chin, K., Tan, J. K., Aminuddin, A., & Makpol, S. (2023) · Nutrients · doi:10.3390/nu15112526 · Cited by 41 · see citing works
Mitochondrial breakdown in skeletal muscle and the emerging role of the lysosomes
Triolo, M., & Hood, D. A. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.11.004 · Cited by 39 · see citing works
Self-citationThe intersection of exercise and aging on mitochondrial protein quality control
Zhang, Y., Oliveira, A. N., & Hood, D. A. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2019.110824 · Cited by 37 · see citing works
Self-citationExercise is mitochondrial medicine for muscle
Oliveira, A. N., & Hood, D. A. (2019) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2019.08.008 · Cited by 34 · see citing works
Self-citationMitochondrial-derived vesicles in skeletal muscle remodeling and adaptation
Picca, A., Guerra, F., Calvani, R., Romanò, R., Coelho‐Júnior, H. J., Bucci, C., Leeuwenburgh, C., & Marzetti, E. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.023 · Cited by 28 · see citing works
Exercise is muscle mitochondrial medicine
Oliveira, A. N., Richards, B. J., Slavin, M., & Hood, D. A. (2021) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000250 · Cited by 26 · see citing works
Self-citationWang, Y., Li, J., Zhang, Z., Wang, R., Hai, B., & Zhang, Y. (2023) · Life · doi:10.3390/life13041006 · Cited by 28 · see citing works
Perspectives on mitochondrial dysfunction in the regeneration of aging skeletal muscle
Wang, K., Gan, M., Lei, Y., Liao, T., Li, J., Niu, L., Zhao, Y., Chen, L., Wang, Y., Zhu, L., et al. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00771-1 · Cited by 33 · see citing works
Loss of Parkin Results in Altered Muscle Stem Cell Differentiation during Regeneration
Esteca, M. V., Severino, M. B., Silvestre, J. G., dos Santos, G. P., Tamborlin, L., Luchessi, A. D., Moriscot, A. S., Gustafsson, Å. B., & Baptista, I. L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218007 · Cited by 25 · see citing works
Acute exercise rapidly activates hepatic mitophagic flux
McCoin, C. S., Franczak, E., Deng, F., Pei, D., Ding, W., & Thyfault, J. P. (2022) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00704.2021 · Cited by 24 · see citing works
Rissardo, J. P., McGarry, A. J., Shi, Y., Caprara, A. L. F., & Kannarkat, G. T. (2025) · Brain Sciences · doi:10.3390/brainsci15121260 · Cited by 35 · see citing works
Bellanti, F., Buglio, A. L., & Vendemiale, G. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14122588 · Cited by 24 · see citing works
Polyamines and Physical Activity in Musculoskeletal Diseases: A Potential Therapeutic Challenge
Galasso, L., Cappella, A., Mulè, A., Castelli, L., Ciorciari, A. M., Stacchiotti, A., & Montaruli, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24129798 · Cited by 23 · see citing works
Gudiksen, A., Qoqaj, A., Ringholm, S., Wojtaszewski, J. F. P., Plomgaard, P., & Pilegaard, H. (2021) · The Journals of Gerontology Series A · doi:10.1093/gerona/glab356 · Cited by 20 · see citing works
Du, Z.-Y., Zhu, H.-L., Chang, W., Zhang, Y., Ling, Q., Wang, K., Zhang, J., Zhang, Q.-B., Kan, X.-L., Wang, Q., et al. (2024) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2024.133997 · Cited by 19 · see citing works
Zhang, W., Hou, W., Chen, M., Chen, E., Xue, D., Ye, C., Li, W., & Pan, Z. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576104 · Cited by 19 · see citing works
Molecular Basis for the Therapeutic Effects of Exercise on Mitochondrial Defects
Memme, J. M., & Hood, D. A. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2020.615038 · Cited by 19 · see citing works
Self-citationThe acute and chronic influence of exercise on mitochondrial dynamics in skeletal muscle
Ritenis, E. J., Padilha, C. S., Cooke, M. B., Stathis, C. G., Philp, A., & CAMERA, D. M. (2024) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00311.2024 · Cited by 17 · see citing works
Mahatme, S., Vaishali, K., Kumar, N., Rao, V., Kovela, R. K., & Sinha, M. K. (2022) · Medicine and Pharmacy Reports · doi:10.15386/mpr-2201 · Cited by 17 · see citing works
Mechanism of Mitochondrial Homeostasis Controlling Ovarian Physiology
Tian, Y., Liu, X., Pei, X., Gao, H., Pan, P., & Yang, Y. (2022) · Endocrinology · doi:10.1210/endocr/bqac189 · Cited by 16 · see citing works
Combined physical exercise reverses the reduced expression of Bmal1 in the liver of aged mice
Pinto, A. P., Muñoz, V. R., Tavares, M. E. A., dos Santos, J. R., Rebelo, M. A., Alberici, L. C., Simabuco, F. M., Teixeira, G. R., Pauli, J. R., de Moura, L. P., et al. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.121175 · Cited by 16 · see citing works
Ottensmeyer, J., Esch, A., Baeta, H., Sieger, S., Gupta, Y., Rathmann, M. F., Jeschke, A., Jacko, D., Schaaf, K., Schiffer, T., et al. (2024) · Current Biology · doi:10.1016/j.cub.2024.07.088 · Cited by 15 · see citing works
Exercise-Boosted Mitochondrial Remodeling in Parkinson’s Disease
Magaña, J. C., Deus, C. M., Giné‐Garriga, M., Montané, J., & Pereira, S. P. (2022) · Biomedicines · doi:10.3390/biomedicines10123228 · Cited by 15 · see citing works
de Jong, J. C. B. C., Verschuren, L., Caspers, M. P. M., van der Hoek, M. D., van der Leij, F. R., Kleemann, R., van den Hoek, A. M., Nieuwenhuizen, A. G., & Keijer, J. (2023) · Biology of Sex Differences · doi:10.1186/s13293-023-00531-w · Cited by 12 · see citing works
Mitophagy: At the heart of mitochondrial quality control in cardiac aging and frailty
Picca, A., Calvani, R., Coelho‐Júnior, H. J., & Marzetti, E. (2021) · Experimental Gerontology · doi:10.1016/j.exger.2021.111508 · Cited by 11 · see citing works
Reynaud, O., Wang, J. P., Ayoub, M., Leduc‐Gaudet, J., Mayaki, D., Dulac, M., Hussain, S. N. A., Bergeron, R., & Gouspillou, G. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00388.2022 · Cited by 9 · see citing works
Selective autophagy: a therapeutic target for healthy aging?
Manastireanu, D. M., Salazar, N., Bejarano, E., & Nieto-Torres, J. L. (2024) · Aging Advances · doi:10.4103/agingadv.agingadv-d-24-00002 · Cited by 7 · see citing works
Loss of ovarian function prevents exercise-induced activation of hepatic mitophagic flux
Franczak, E., Kugler, B. A., Salathe, S. F., Allen, J., Sardiu, M. E., McCoin, C. S., Hevener, A. L., Morris, E. M., & Thyfault, J. P. (2025) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00107.2025 · Cited by 9 · see citing works
Parkin Inhibits RANKL-Induced Osteoclastogenesis and Ovariectomy-Induced Bone Loss
Hou, W., Chen, M., Ye, C., Chen, E., Li, W., & Zhang, W. (2022) · Biomolecules · doi:10.3390/biom12111602 · Cited by 9 · see citing works
Sex‐specific mitochondrial dynamics and mitophagy response to muscle damage
Luk, H., Jiwan, N. C., Appell, C. R., Levitt, D. E., & Vingren, J. L. (2022) · Physiological Reports · doi:10.14814/phy2.15230 · Cited by 9 · see citing works
Xu, J., Wei, H., Sun, Z., Li, W., Long, J., Liu, J., Feng, Z., & Cao, K. (2025) · Antioxidants · doi:10.3390/antiox14040398 · Cited by 8 · see citing works
Oliveira, A. N., Tamura, Y., Memme, J. M., & Hood, D. A. (2023) · Mitochondrial Communications · doi:10.1016/j.mitoco.2023.10.001 · Cited by 8 · see citing works
Self-citationEsteca, M. V., Divino, I. A., da Silva, A. L. V., Severino, M. B., Braga, R. R., Ropelle, E. R., Simabuco, F. M., & Baptista, I. L. (2024) · Acta Physiologica · doi:10.1111/apha.14111 · Cited by 7 · see citing works
Laskin, G. R., Rentería, L. I., Muller‐Delp, J. M., Kim, J., Chase, P. B., Hwang, H. S., & Gordon, B. S. (2024) · The Journal of Physiology · doi:10.1113/jp286334 · Cited by 7 · see citing works
Mitophagy Regulation in Skeletal Muscle: Effect of Endurance Exercise and Age
Erlich, A. T., & Hood, D. A. (2019) · Journal of Science in Sport and Exercise · doi:10.1007/s42978-019-00041-5 · Cited by 7 · see citing works
Self-citationMitochondrial quality control in health and disease: mechanisms and therapeutic targets
Creus, A., Mohapatra, S., Ortega, L., & Sebastián, D. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02813-2 · Cited by 7 · see citing works
Sensing local energetics to acutely regulate mitophagy in skeletal muscle
Nichenko, A. S., Specht, K. S., Craige, S. M., & Drake, J. C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.987317 · Cited by 7 · see citing works
Mitophagy in skeletal muscle: Impact of ageing, exercise and disuse
Kuznyetsova, A., & Hood, D. A. (2025) · Experimental Physiology · doi:10.1113/ep093041 · Cited by 5 · see citing works
Self-citationAcheson, J., Joanisse, S., Sale, C., & Hodson, N. W. (2024) · Bioscience Reports · doi:10.1042/bsr20240137 · Cited by 4 · see citing works
Mitochondrial proteostasis mediated by CRL5 Ozz and Alix maintains skeletal muscle functionPreprint
Campos, Y., Rodriguez-Enriquez, R., Palacios, G. F., van de Vlekkert, D., Qiu, X., Weesner, J., Gomero, E. M., Demmers, J., Bertorini, T. E., Opferman, J. T., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.11.548601 · Cited by 3 · see citing works
Interplay between mTORC1 signaling and iron homeostasis in muscle atrophy
Jee, E., Ouf, W., Kim, J., & Kim, Y. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.10.257 · Cited by 2 · see citing works
Current Progress in the Role of Ferroptosis in Skeletal Muscle Atrophy
Chen, Y., Guo, Y., Zhao, Z., Yang, S., Guo, B., & Xu, J. (2026) · Mediators of Inflammation · doi:10.1155/mi/3578349 · Cited by 2 · see citing works
The Impact of Traditional Chinese Medicine on Mitophagy in Disease Models
Yu, L., Shi, T., Li, Y.-Q., Mu, J.-K., Yang, Y.-Q., Li, W., Yu, J., & Yang, X. (2021) · Current Pharmaceutical Design · doi:10.2174/1381612827666211006150410 · Cited by 2 · see citing works
Pires, R. A., Correia, T. M. L., de Almeida, A. A., Coqueiro, R. D. S., Machado, M., Teles, M. F., Peixoto, Á. S., Queiroz, R. F., & Pereira, R. (2022) · Life · doi:10.3390/life12122113 · Cited by 2 · see citing works
Campos, Y., Palacios, G., Gomero, E. M., van de Vlekkert, D., Venkataraman, K., John, J., Weesner, J. A., Wakefield, R., Qiu, X., Rodriguez-Enriquez, R., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-09363-3 · Cited by 4 · see citing works
Sanfrancesco, V. C., Mea, D. D., & Hood, D. A. (2026) · Muscles · doi:10.3390/muscles5020039 · Cited by 1 · see citing works
Self-citationLinking mitochondrial dysfunction to sarcopenia
Alway, S. E. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822146-4.00004-1 · Cited by 1 · see citing works
Parkin R274W mutation affects muscle and mitochondrial physiology
Sevegnani, M., Lama, A., Girardi, F., Hess, M. W., Rueda, M. P. C., Pichler, I., Biressi, S., & Piccoli, G. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167302 · Cited by 1 · see citing works
Parkin the progression of sarcopenia
Henríquez‐Olguín, C., & Knudsen, J. R. (2019) · The Journal of Physiology · doi:10.1113/jp277770 · Cited by 1 · see citing works
Roles of autophagy & mitophagy in the regulation of skeletal muscle function
Leduc‐Gaudet, J. (2021) · eScholarship@McGill (McGill) · doi:10.82308/1594
Prospective Advances in Exercise-Induced Autophagy on Health
Liang, J., Kirberger, M., & Chen, N. (2021) · Springer eBooks · doi:10.1007/978-981-16-4525-9_11
Exercise and Mitochondrial Function: Importance and Inference- A Mini Review
Vaishali, K., Kumar, N., Rao, V., Kovela, R. K., & Sinha, M. K. (2021) · Current Molecular Medicine · doi:10.2174/1566524021666211129110542
Kangxia, L. I., Yingqi, W. A. N. G., Caitao, C. H. E. N., Yanxia, S. O. N. G., Wu, W., & Li, J. (2024) · Rehabilitation Medicine · doi:10.3724/sp.j.1329.2024.04014
Self-citationReynaud, O., Ayoub, M., Leduc‐Gaudet, J., Cefis, M., Lussier, M. P., Hussain, S. N. A., & Gouspillou, G. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.13.659533
Impact of different exercise modalities on mitophagy in human skeletal muscle
Muñoz-Medina, C., Carriel-Nesvara, A., Botella, J., & Castro-Sepulveda, M. (2025) · International review of cytology · doi:10.1016/bs.ircmb.2025.10.005
de Jong, J. C. B. C., Verschuren, L., Caspers, M. P. M., van der Hoek, M. D., van der Leij, F. R., Kleemann, R., van den Hoek, A. M., Nieuwenhuizen, A. G., & Keijer, J. (2023) · Figshare · doi:10.6084/m9.figshare.23658071
de Jong, J. C. B. C., Verschuren, L., Caspers, M. P. M., van der Hoek, M. D., van der Leij, F. R., Kleemann, R., van den Hoek, A. M., Nieuwenhuizen, A. G., & Keijer, J. (2023) · Figshare · doi:10.6084/m9.figshare.23658080
de Jong, J. C. B. C., Verschuren, L., Caspers, M. P. M., van der Hoek, M. D., van der Leij, F. R., Kleemann, R., van den Hoek, A. M., Nieuwenhuizen, A. G., & Keijer, J. (2023) · Figshare · doi:10.6084/m9.figshare.23658077
de Jong, J. C. B. C., Verschuren, L., Caspers, M. P. M., van der Hoek, M. D., van der Leij, F. R., Kleemann, R., van den Hoek, A. M., Nieuwenhuizen, A. G., & Keijer, J. (2023) · Figshare · doi:10.6084/m9.figshare.23658074
Reynaud, O., Ayoub, M., Leduc‐Gaudet, J., Cefis, M., Lussier, M. P., Hussain, S. N. A., & Gouspillou, G. (2026) · Scientific Reports · doi:10.1038/s41598-025-34223-9
- Authors
- Chen, C. C. W., Erlich, A. T., Crilly, M. J., & Hood, D. A.
- Affiliations
- York University (CA)
- Corresponding author
- Hood, David A.
- ORCID
- Hood, David A.
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 2018-09-01
- Volume
- 315
- Issue
- 3
- Pages
- E404-E415
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- OpenAlex
- W2807114871
- Semantic Scholar
- 4601835e866b1f7b1dd68edc05405eb6f445e786
- Cited by
- 108
- References
- 67
- Citations by year
- 2026: 11 · 2025: 9 · 2024: 13 · 2023: 14 · 2022: 19 · 2021: 19 · 2020: 11 · 2019: 7 · 2018: 5
- FWCI
- 8.19
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada (Conseil de Recherches en Sciences Naturelles et en Génie du Canada)
- Canada Research Chairs (Chaires de recherche du Canada)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- Parkin, mitophagy, physical activity, muscle aging, mitochondrial homeostasis, mitochondrial biogenesis, PGC-1α, mitofusin 2, mitochondrial ubiquitination, E3 ubiquitin ligase, skeletal muscle, autophagy
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Aging, Animals, Electron Transport Complex IV, Mice, Inbred C57BL, Mitochondria, Muscle, Physical Conditioning, Animal, Repressor Proteins, Mice, Knockout, Muscle, Skeletal, GTP Phosphohydrolases, Ubiquitin-Protein Ligases, Mice, Ubiquitination, Mitophagy
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