Expression of mitochondrial fission and fusion regulatory proteins in skeletal muscle during chronic use and disuse
Abstract
INTRODUCTION: The mitochondrial network within cells is mediated by fission and fusion processes. METHODS: We investigated the expression of the proteins responsible for these events during conditions of altered oxidative capacity. RESULTS: With chronic contractile activity, the mitochondrial reticulum increased in size, along with concomitant increases in the fusion proteins Opa1 and Mfn2 (by 36% and 53%; P < 0.05). When we induced muscle disuse through denervation for 7 days, fragmented mitochondria were observed, along with significant decreases in the expression of Mfn2 and Opa1 (by 84% and 70%). To assess the effects of aging on mitochondrial morphology, young (5 month) and aged (35 month) Fisher 344 Brown Norway rats were used. Aged animals also possessed smaller mitochondria and displayed increased levels of fission proteins. CONCLUSIONS: Chronic muscle use increases the ratio of fusion:fission proteins, leading to reticular mitochondria, whereas muscle disuse and aging result in a decrease in this ratio, culminating in fragmented organelles.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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 [151]
Fragmented and atypically enlarged mitochondria are often observed in aged skeletal muscle, indicating that mitochondrial dynamics are compromised in advanced age.
“Fragmented and atypically enlarged mitochondria were often observed in aged skeletal muscle (81, 82), indicating that mitochondrial dynamics are compromised in advanced age.”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [81]
Studies in rodents have reported increased or unchanged Drp1 content in aged skeletal muscles.
“Indeed, studies in rodents have reported increased [49,50,51] or unchanged [34,47,52,54] Drp1 content in aged skeletal muscles.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [49]
Mfn2 content in aged rodent skeletal muscle is reported as decreased, unchanged, or increased.
“Mfn2 content has been reported as decreased [34,49,55], unchanged [52], or even increased in aged rodent skeletal muscles [47,50,54].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [49]
Electron microscopy and biochemical analyses show small, more fragmented mitochondria in muscles from old compared with young adult hosts.
“electron microscopy and biochemical analyses have shown small, more fragmented mitochondria in muscles from old as compared to young adult hosts (56, 57)”
From Mitochondria initiate and regulate sarcopenia (2017) · cites this paper as [57]
Spinal cord injury or denervation induces large-scale muscle wasting, and denervation is often part of sarcopenia.
“spinal cord injury or denervation induces large-scale muscle wasting (57, 76, 107, 129, 131, 137), and denervation is a condition often seen as part of sarcopenia.”
From Mitochondria initiate and regulate sarcopenia (2017) · cites this paper as [57]
Altered neuronal signaling is due at least in part to high ROS and mitochondrial dysfunction in muscle cells, and neural dysfunction is communicated to muscle cells.
“we would expect that altered neuronal signaling is due at least in part to high ROS production and mitochondrial dysfunction in the muscle cells, and conversely, that neural dysfunction will be communicated to muscle cells (57, 100).”
From Mitochondria initiate and regulate sarcopenia (2017) · cites this paper as [57]
In skeletal muscle, reduced mitochondrial respiration has been linked to aberrant control of mitochondrial dynamics.
“In skeletal muscle, reduced mitochondrial respiration has also been linked to aberrant control of mitochondrial dynamics [64–67].”
From Proinflammatory NFkB signalling promotes mitochondrial dysfunction in skeletal muscle in response to cellular fuel overloading (2019) · cites this paper as [65]
Cites
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works
Dysfunction of Mitochondria in Human Skeletal Muscle in Type 2 Diabetes
Kelley, D. E., He, J., Menshikova, E. V., & Ritov, V. B. (2002) · Diabetes · doi:10.2337/diabetes.51.10.2944 · Cited by 2,321 · see citing works
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755 · see citing works
Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376 · cited 1× · see citing works
“Essential mammalian skeletal muscle fusion proteins involved in these processes include mitofusin 2 (Mfn2), which is necessary for outer membrane fusion, and the inner mitochondrial membrane protein optical atrophy 1 (Opa1).(5,6) Mitochondrial membrane fission is mediated by dynamin related peptide 1 (Drp1), in combin…”
BackgroundHandschin, C., & Spiegelman, B. M. (2006) · Endocrine Reviews · doi:10.1210/er.2006-0037 · Cited by 1,090 · see citing works
Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
Lee, Y.-J., Jeong, S.-Y., Karbowski, M., Smith, C. L., & Youle, R. J. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-04-0294 · Cited by 1,042 · see citing works
Wang, X., Su, B., Siedlak, S. L., Moreira, P. I., Fujioka, H., Wang, Y., Casadesus, G., & Zhu, X. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804871105 · Cited by 835 · see citing works
Mitofusin-2 Determines Mitochondrial Network Architecture and Mitochondrial Metabolism
Bach, D., Pich, S., Soriano, F. X., Vega, N., Baumgartner, B., Oriola, J., Daugaard, J. R., Lloberas, J., Camps, M., Zierath, J. R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212754200 · Cited by 832 · cited 1× · see citing works
“Mitochondrial morphology is altered during muscle development(1) and in various disease conditions, including diabetes(2,3) and obesity.(3,4) These changes in morphology are mediated by a balance of organelle fusion and fission events.”
BackgroundhFis1, a Novel Component of the Mammalian Mitochondrial Fission Machinery
James, D. I., Parone, P. A., Mattenberger, Y., & Martinou, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303758200 · Cited by 653 · see citing works
Mitochondrial Inner-Membrane Fusion and Crista Maintenance Requires the Dynamin-Related GTPase Mgm1
Meeusen, S., DeVay, R. M., Block, J., Cassidy-Stone, A., Wayson, S. M., McCaffery, J. M., & Nunnari, J. M. (2006) · Cell · doi:10.1016/j.cell.2006.09.021 · Cited by 474 · 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
Mitofusins 1/2 and ERRα expression are increased in human skeletal muscle after physical exercise
Cartoni, R., Léger, B., Hock, M. B., Praz, M., Crettenand, A., Pich, S., Ziltener, J., Luthi, F., Dériaz, O., Zorzano, A., et al. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.092031 · Cited by 406 · see citing works
Expression of <i>Mfn2</i>, the Charcot-Marie-Tooth Neuropathy Type 2A Gene, in Human Skeletal Muscle
Bach, D., Naon, D., Pich, S., Soriano, F. X., Vega, N., Rieusset, J., Laville, M., Guillet, C., Boirie, Y., Wallberg-Henriksson, H., et al. (2005) · Diabetes · doi:10.2337/diabetes.54.9.2685 · Cited by 369 · cited 1× · see citing works
“Mitochondrial morphology is altered during muscle development(1) and in various disease conditions, including diabetes(2,3) and obesity.(3,4) These changes in morphology are mediated by a balance of organelle fusion and fission events.”
BackgroundMitochondrial Function and Actin Regulate Dynamin-Related Protein 1-Dependent Mitochondrial Fission
Vos, K. J. D., Allan, V., Grierson, A. J., & Sheetz, M. P. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.064 · Cited by 345 · see citing works
Fzo1, a Protein Involved in Mitochondrial Fusion, Inhibits Apoptosis
Sugioka, R., Shimizu, S., & Tsujimoto, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408910200 · Cited by 341 · see citing works
DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
Jagasia, R., Grote, P., Westermann, B., & Conradt, B. (2005) · Nature · doi:10.1038/nature03316 · Cited by 319 · see citing works
Irrcher, I., Adhihetty, P. J., Sheehan, T. E., Joseph, A.-M., & Hood, D. A. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00409.2002 · Cited by 315 · see citing works
Mitochondrial fission proteins regulate programmed cell death in yeastPreprint
Fannjiang, Y., Cheng, W., Lee, S. J., Qi, B., Pevsner, J., McCaffery, J. M., Hill, R. B., Basáñez, G., & Hardwick, J. M. (2004) · Genes & Development · doi:10.1101/gad.1247904 · Cited by 304 · 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
Zechner, C., Lai, L., Zechner, J. F., Geng, T., Yan, Z., Rumsey, J. W., Collia, D., Chen, Z., Wozniak, D. F., Leone, T. C., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.008 · Cited by 274 · cited 1× · see citing works
“Mice deficient in PGC-1a have reduced expression of Mfn2 mRNA.(36) Conversely, up-regulation in PGC-1a, from a single bout of cycling exercise stimulated ERRa binding at the 2413/”
BackgroundPicard, M. A., White, K., & Turnbull, D. M. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01096.2012 · Cited by 260 · see citing works
MtDNA mutations in aging and apoptosis
Chomyn, A., & Attardi, G. M. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00625-9 · Cited by 243 · see citing works
Lipman, R. D., Chrisp, C. E., Hazzard, D. G., & Bronson, R. T. (1996) · The Journals of Gerontology Series A · doi:10.1093/gerona/51a.1.b54 · Cited by 242 · see citing works
Effect of denervation on mitochondrially mediated apoptosis in skeletal muscle.
Adhihetty, P. J., O'Leary, M. F. N., Chabi, B., Wicks, K. L., & Hood, D. A. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00768.2006 · Cited by 240 · see citing works
Mitochondrial framework (reticulum mitochondriale) in rat diaphragm muscle
Bakeeva, L. E., Chentsov, Y. S., & Skulachev, V. P. (1978) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(78)90104-4 · Cited by 227 · see citing works
Garnier, A., Fortin, D., Zoll, J., N’guessan, B. B., Mettauer, B., Lampert, E., Veksler, V., & Ventura‐Clapier, R. (2005) · The FASEB Journal · doi:10.1096/fj.04-2173com · Cited by 193 · see citing works
The role of PGC-1α on mitochondrial function and apoptotic susceptibility in muscle
Adhihetty, P. J., Uguccioni, G., Leick, L., Hidalgo, J., Pilegaard, H., & Hood, D. A. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00070.2009 · Cited by 168 · see citing works
Koltai, E., Hart, N., Taylor, A. W., Goto, S., Ngo, J. K., Davies, K. J. A., & Radak, Z. (2012) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00337.2011 · Cited by 152 · see citing works
Ding, H., Jiang, N., Liu, H., Liu, X., Liu, D., Zhao, F., Wen, L., Liu, S., Ji, L. L., & Zhang, Y. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.08.007 · Cited by 149 · see citing works
Skeletal muscle metabolism and ultrastructure in relation to age in sedentary men
Örlander, J., Kiessling, K., Larsson, L., Karlsson, J., & ANIANSSON, A. (1978) · Acta Physiologica Scandinavica · doi:10.1111/j.1748-1716.1978.tb06277.x · Cited by 121 · see citing works
Mitochondrial Biogenesis and Fragmentation as Regulators of Muscle Protein Degradation
Romanello, V., & Sandri, M. (2010) · Current Hypertension Reports · doi:10.1007/s11906-010-0157-8 · Cited by 117 · see citing works
Mitochondrial adaptations in denervated muscle: relationship to muscle performance
Wicks, K. L., & Hood, D. A. (1991) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1991.260.4.c841 · Cited by 111 · see citing works
Ogata, T., & Yamasaki, Y. (1985) · Cell and Tissue Research · doi:10.1007/bf00217168 · Cited by 98 · see citing works
Chronic stimulation-induced changes in mitochondria and performance in rat skeletal muscle
Takahashi, M., & Hood, D. A. (1993) · Journal of Applied Physiology · doi:10.1152/jappl.1993.74.2.934 · Cited by 86 · see citing works
Effects of endurance training on a mitochondrial reticulum in limb skeletal muscle
Kirkwood, S. P., Packer, L., & Brooks, G. A. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90296-7 · Cited by 77 · see citing works
Mitochondrial 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
Adhihetty, P. J., Ljubicic, V., & Hood, D. A. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00311.2006 · Cited by 67 · see citing works
Ontogenesis of mitochondrial reticulum in rat diaphragm muscle.
Bakeeva, L. E., Chentsov, Y. S., & Skulachev, V. P. (1981) · PubMed · Cited by 56 · see citing works
Some mitochondrial changes in denervated muscle
Miledi, R., & Slater, C. R. (1968) · Journal of Cell Science · doi:10.1242/jcs.3.1.49 · Cited by 50 · see citing works
Kayar, S. R., Hoppeler, H. H., Essén-Gustavsson, B., & Schwerzmann, K. (1988) · Journal of Experimental Biology · doi:10.1242/jeb.137.1.253 · Cited by 43 · see citing works
Wagatsuma, A., Kotake, N., Mabuchi, K., & Yamada, S. (2011) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-011-0083-5 · Cited by 38 · see citing works
Mitochondrial distribution in relation to changes in muscle metabolism in rat soleus
Kayar, S. R., Claassen, H., Hoppeler, H. H., & Weiber, E. R. (1986) · Respiration Physiology · doi:10.1016/0034-5687(86)90056-3 · Cited by 30 · see citing works
Heath, I. B., & Rethoret, K. (1980) · PubMed · Cited by 14 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Mitochondrial 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
“In overt contrast to the mitochondrial hyperfusion hypothesis, recent findings show that fission signaling may indeed be upregulated in muscles from old rats, as evidenced by the higher expression of Fis1 and Drp1 relative to younger controls (Iqbal et al. 2013).”
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
Exercise Promotes Healthy Aging of Skeletal Muscle
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
“For example, since denervation is one of the stimuli that induce mitochondrial fission in muscle (Iqbal et al., 2013; Romanello et al., 2010), studies examining muscles in advanced age are more likely to sample regions from denervated fibers and are thus more likely to observe mitochondria with…”
BackgroundResultEffects of Exercise and Aging on Skeletal MusclePreprint
Distéfano, G., & Goodpaster, B. H. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a029785 · Cited by 493 · see citing works
“While some have found no age-related trends in mitochondrial fusion and fission (Bori et al. 2012; Konopka et al. 2014), others have described both an increased fission (Iqbal et al. 2013), or increased fusion (Leduc-Gaudet et al. 2015) in older muscles.”
BackgroundMitochondrial quality control and muscle mass maintenance.
Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434 · see citing works
“Notably, genetic manipulations to activate or inhibit autophagy results into muscle atrophy (Mammucari et al., 2007; Masiero et al., 2009; Romanello et al., 2010).”
BackgroundMitochondria 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
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
“Both SS and IMF fractions appear visibly thinner and smaller within aged muscle compared to young counterparts, and many studies have reported decreased mitochondrial content with age (Short et al. 2003, 2005; Chabi et al. 2008; Ljubicic et al. 2009; Iqbal et al. 2013).”
BackgroundSelf-citationRana, A., Oliveira, M. P., Khamoui, A. V., Aparicio, R., Rera, M., Rossiter, H. B., & Walker, D. W. (2017) · Nature Communications · doi:10.1038/s41467-017-00525-4 · Cited by 294 · see citing works
Mitochondrial morphology is altered in atrophied skeletal muscle of aged mice
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
“This notion is based on previous TEM studies limited to longitudinal orientation, reporting an aging-related decrease in IMF mitochondrial size [42-44].”
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
“Indeed, Mfn2 content has been reported as decreased [34,49,55], unchanged [52], or even increased in aged rodent skeletal muscles [47,50,54].”
BackgroundMolecular Mechanisms of Inflammation in Sarcopenia: Diagnosis and Therapeutic Update
Jiménez-Gutiérrez, G. E., Martínez-Gómez, L. E., Martínez-Armenta, C., Pineda, C., Martínez‐Nava, G. A., & López-Reyes, A. G. (2022) · Cells · doi:10.3390/cells11152359 · Cited by 243 · see citing works
“Earlier this year, the mitochondrial uncoupling agent BAM15 (a protonophore of the respiratory chain) was demonstrated to decrease mitochondrial fission by lowering the expression of Fis1; as a result, increased muscle mass and function, mitochondrial biogenesis quality control, and OXPHOS activity were observed, acco…”
BackgroundSignaling Pathways That Control Muscle Mass
Vainshtein, A., & Sandri, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134759 · Cited by 214 · see citing works
Joseph, A., Adhihetty, P. J., & Leeuwenburgh, C. (2016) · The Journal of Physiology · doi:10.1113/jp270659 · Cited by 186 · see citing works
“2008), as well as mitochondria that appear punctate and fragmented (Ljubicic et al. 2009; Iqbal et al. 2013).”
BackgroundSelf-citationNielsen, J., Gejl, K. D., Hey‐Mogensen, M., Holmberg, H., Suetta, C., Krustrup, P., Elemans, C. P. H., & Ørtenblad, N. (2017) · The Journal of Physiology · doi:10.1113/jp273040 · Cited by 191 · see citing works
“…athletes having a higher respiration rate per mitochondria (Pesta et al. 2011; Jacobs and Lundby, 2013; Boushel et al. 2014b) and the fact that aerobic training is known to increase mitochondrial fusion (Iqbal et al. 2013), which increases mitochondrial intrinsic ATP production (Mitra et al. 2009).”
BackgroundRomanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · 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-citationMitochondrial quality control as a key determinant of cell survival
Sedlackova, L., & Korolchuk, V. I. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.12.012 · Cited by 186 · see citing works
VanderVeen, B. N., Fix, D. K., & Carson, J. A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/3292087 · Cited by 182 · see citing works
“Mitochondrial dynamics’ processes have been extensively studied and characterized both in vivo and in vitro and have been previously reviewed [13, 90, 94, 95].”
BackgroundUnravelling 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
Impact of Aging and Exercise on Mitochondrial Quality Control in Skeletal Muscle
Kim, Y., Triolo, M., & Hood, D. A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/3165396 · Cited by 158 · see citing works
“For example, in a study comparing young (5 months) and old (35 months) Fisher 344 Brown Norway (BN) rats, aging skeletal muscles were observed to have elevated protein levels of Fis1 and Drp1, as well as downregulated Mfn2 levels, compared to their young counterparts [8].”
BackgroundInfluentialMitochondria 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
“However, mitochondria can range from small individual organelles to rather extensive and connected reticular systems (57).”
BackgroundResultInfluentialAcute exercise remodels mitochondrial membrane interactions in mouse skeletal muscle
Picard, M. A., Gentil, B. J., McManus, M. J., White, K., Louis, K. S., Gartside, S. E., Wallace, D. C., & Turnbull, D. M. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00819.2013 · Cited by 145 · see citing works
Carter, H. N., Kim, Y., Erlich, A. T., Zarrin‐khat, D., & Hood, D. A. (2018) · The Journal of Physiology · doi:10.1113/jp275998 · Cited by 136 · see citing works
“These results are similar to our previous findings (Iqbal et al. 2013).”
ResultSelf-citationNisr, R. B., Shah, D. S., Ganley, I. G., & Hundal, H. S. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03148-8 · Cited by 142 · see citing works
Oxidative stress-induced mitochondrial fragmentation and movement in skeletal muscle myoblasts
Iqbal, S., & Hood, D. A. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00017.2014 · Cited by 129 · see citing works
“During aging, an increased incidence of mitochondrial fragmentation has been observed, with a concomitant increase in the expression of mitochondrial fission proteins (19).”
BackgroundJu, J.-S., Jeon, S.-I., Park, J.-Y., Lee, J.-Y., Lee, S.-C., Cho, K.-J., & Jeong, J.-M. (2016) · The Journal of Physiological Sciences · doi:10.1007/s12576-016-0440-9 · Cited by 125 · see citing works
Age-dependent changes in mitochondrial morphology and volume are not predictors of lifespan
Regmi, S. G., Rolland, S. G. M., & Conradt, B. (2014) · Aging · doi:10.18632/aging.100639 · Cited by 124 · see citing works
“While an increase in the expression of the gene Drp1 (Dynamin-related protein 1), which encodes a dynamin-related GTPase that promotes mitochondrial fission, was observed in the in vitro study using rat muscle cells [27], another study, also using tissues derived from rat, reported that the expression of both fission-…”
InfluentialAxelrod, C. L., Fealy, C. E., Mulya, A., & Kirwan, J. P. (2018) · Acta Physiologica · doi:10.1111/apha.13216 · Cited by 120 · see citing works
“In a pre‐clinical model, after 7 days of exercise Sprague‐ Dawley rats displayed a profusion shift similar to the results described herein.(40) Furthermore, prolonged sedentarism or aging induced profission phenotypes, suggesting a relationship between skeletal muscle oxidative capacity and mitochondrial dynamics.”
ResultParkin is required for exercise-induced mitophagy in muscle: Impact of aging
Chen, C. C. W., Erlich, A. T., Crilly, M. J., & Hood, D. A. (2018) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00391.2017 · Cited by 108 · see citing works
Self-citationTheurey, P., & Pizzo, P. (2018) · Genes · doi:10.3390/genes9010022 · Cited by 103 · see citing works
“In particular, the number and density of mitochondria [10–12], as well as mitogenesis [13,14], have been showed to be reduced, whereas for mitochondrial dynamics and content contradictory inconclusive results have been reported [15,16] (see also [8] for a recent review).”
BackgroundMitochondrial Dysfunction: A Key Player in Brain Aging and Diseases
Bartman, S., Coppotelli, G., & Ross, J. M. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46030130 · Cited by 101 · see citing works
“On the other hand, data on protein levels involved in mitochondrial dynamics during aging in skeletal muscle are quite discordant, with studies reporting a decrease [79–81], no change [82,83], and even an increase [84].”
BackgroundLei, 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
“However, a comparison between young versus old mice revealed a higher mitochondrial fusion index (Mfn2-to-Drp1 ratio) in aged skeletal muscle [85].”
BackgroundInfluentialThe 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
“Aged skeletal muscle mitochondria have been reported to be fragmented in rats [39] or atypically enlarged in aged muscles of houseflies [40], mice [41–43], rats [44], and muscle cells of humans [41].”
BackgroundEffects of Nrf2 deficiency on mitochondrial oxidative stress in aged skeletal muscle
Kitaoka, Y., Tamura, Y., Takahashi, K., Takeda, K., Takemasa, T., & Hatta, H. (2019) · Physiological Reports · doi:10.14814/phy2.13998 · Cited by 94 · see citing works
“Morphologically, aging induces mitochondrial fragmentation or unusual enlargement in skeletal muscle (Iqbal et al. 2013; Leduc-Gaudet et al. 2015).”
BackgroundMitochondrial Properties in Skeletal Muscle Fiber
Dong, H., & Tsai, S. (2023) · Cells · doi:10.3390/cells12172183 · Cited by 95 · see citing works
Callahan, D. M., Bedrin, N. G., Subramanian, M., Berking, J., Ades, P. A., Toth, M. J., & Miller, M. S. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01362.2013 · Cited by 89 · 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
Zampieri, S., Mammucari, C., Romanello, V., Barberi, L., Pietrangelo, L., Fusella, A., Mosole, S., Gherardi, G., Höfer, C., Löfler, S., et al. (2016) · Physiological Reports · doi:10.14814/phy2.13005 · Cited by 88 · see citing works
“Exercise training also impacts on mitochondria dynamics inducing fusion and fission phenomena to sustain cellular energy requirements (Bori et al. 2012; Iqbal et al. 2013; Konopka and Sreekumaran Nair 2013).”
BackgroundDenervation-induced skeletal muscle fibrosis is mediated by CTGF/CCN2 independently of TGF-β
Rebolledo, D. L., González, D., Faundez-Contreras, J., Contreras, O., Vio, C. P., Murphy-Ullrich, J. E., Lipson, K. E., & Brandan, E. (2019) · Matrix Biology · doi:10.1016/j.matbio.2019.01.002 · Cited by 86 · see citing works
Mitofusin 2 as a Driver That Controls Energy Metabolism and Insulin Signaling
Zorzano, A., Hernández‐Álvarez, M. I., Sebastián, D., & Muñoz, J. P. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6208 · Cited by 83 · see citing works
Mechanical ventilation triggers abnormal mitochondrial dynamics and morphology in the diaphragm
Picard, M. A., Azuelos, I., Jung, B., Giordano, C., Matecki, S., Hussain, S. N. A., White, K., Li, T., Liang, F., Benedetti, A., et al. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00873.2014 · 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
Aging shifts mitochondrial dynamics toward fission to promote germline stem cell loss.
Amartuvshin, O., Lin, C., Hsu, S., Kao, S., Chen, A., Tang, W., Chou, H., Chang, D., Hsu, Y., Hsiao, B., et al. (2020) · Aging Cell · doi:10.1111/acel.13191 · Cited by 75 · see citing works
Faitg, J., Leduc-Gaudet, J.-P., Reynaud, O., Ferland, G., Gaudreau, P., & Gouspillou, G. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00420 · Cited by 72 · see citing works
“While some studies have provided data suggesting that aging is associated with a fragmentation of IMF mitochondria (Poggi et al., 1987;Huang et al., 2010;Lanza et al., 2012;Iqbal et al., 2013), others have provided data indicating that aging is associated with an increased size of IMF mitochondria (Sebastian et al.”
BackgroundLippi, L., de Sire, A., Mezian, K., Curci, C., Perrero, L., Turco, A., Andaloro, S., Ammendolia, A., Fusco, N., & Invernizzi, M. (2022) · Aging Clinical and Experimental Research · doi:10.1007/s40520-021-02073-w · Cited by 65 · see citing works
Mitofusin 1 and optic atrophy 1 shift metabolism to mitochondrial respiration during aging.
Son, J. M., Sarsour, E. H., Kakkerla Balaraju, A., Fussell, J., Kalen, A. L., Wagner, B. A., Buettner, G. R., & Goswami, P. C. (2017) · Aging Cell · doi:10.1111/acel.12649 · Cited by 71 · see citing works
“…studies and results presented here clearly showed a higher frequency of mitochondrial fusion during aging, other studies report a higher abundance of mitochondrial fragmentation (fission) in aged neurons of C. elegans (Jiang et al., 2015) and in vitro aged rat muscle cells (Iqbal et al., 2013).”
BackgroundResultVanderVeen, B. N., Fix, D. K., Montalvo, R. N., Counts, B. R., Smuder, A. J., Murphy, E. A., Koh, H., & Carson, J. A. (2018) · Experimental Physiology · doi:10.1113/ep087429 · Cited by 68 · see citing works
Bell, M. B., Bush, Z., McGinnis, G. R., & Rowe, G. C. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00719.2018 · Cited by 62 · see citing works
“In both rodents and humans, endurance exercise has been shown to increase the expression of genes involved in fusion and fission (8, 20, 28, 33).”
BackgroundFan, J., Fan, J., & Khanzada, Z. (2025) · Muscles · doi:10.3390/muscles4030026 · Cited by 64 · see citing works
“Both conditions impair mitochondrial distribution and energy output, exacerbating muscle aging and the development of muscle-related diseases [110,111].”
Harper, C., Gopalan, V., & Goh, J. (2021) · Journal of Translational Medicine · doi:10.1186/s12967-021-02737-1 · Cited by 62 · see citing works
“Some studies indicate that aging confers dysregulation in the direction of disproportionately elevated fission [54], consistent with the fragmented mitochondrial structures often observed in aged rodent skeletal muscle [55].”
ResultMitochondrial health and muscle plasticity after spinal cord injury
Gorgey, A. S., Witt, O., O’Brien, L. C., Cardozo, C. P., Chen, Q., Lesnefsky, E. J., & Graham, Z. (2018) · European Journal of Applied Physiology · doi:10.1007/s00421-018-4039-0 · Cited by 63 · 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 maximal depth of SS mitochondria and the average area of individual IMF mitochondria also decline with age [102].”
BackgroundMitochondrial Bioenergetics and Turnover during Chronic Muscle Disuse
Memme, J. M., Slavin, M. B., Moradi, N., & Hood, D. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105179 · Cited by 59 · see citing works
“Furthermore, inter-myofibrillar (IMF) mitochondria, following hindlimb suspension, appear swollen and irregular along with a >60% reduction in the subsarcolemmal (SS) mitochondrial layer lying proximal to the myonuclei [33,100].”
BackgroundHe, W., Wang, P., Chen, Q., & Li, C. (2020) · Skeletal Muscle · doi:10.1186/s13395-020-00245-2 · Cited by 57 · 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
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
“In contrast, a recent study demonstrated 82 that an endurance exercise-type chronic muscle contractile activity increased mitochondrial 83 fusion protein levels (Iqbal et al. 2013).”
BackgroundResultInfluentialTriolo, M., Slavin, M., Moradi, N., & Hood, D. A. (2022) · The Journal of Physiology · doi:10.1113/jp282173 · Cited by 52 · see citing works
“2018b) and organellar fragmentation (Ljubicic et al. 2009; Iqbal et al. 2013; O’Leary et al. 2013; Carter et al. 2018a).”
BackgroundInfluentialCaffin, F., Prola, A., Piquereau, J., Novotova, M., David, D. J., Garnier, A., Fortin, D., Alavi, M. V., Veksler, V., Ventura‐Clapier, R., et al. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.263079 · Cited by 55 · see citing works
“Respiratory parameters of total mitochondrial population were studied in situ as previously described (Kuznetsov et al. 2008).”
MethodFrom mitochondria to sarcopenia: role of 17β-estradiol and testosterone
Tian, X., Lou, S., & Shi, R. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1156583 · Cited by 54 · see citing works
Regulation of muscle and mitochondrial health by the mitochondrial fission protein Drp1 in aged mice
Dulac, M., Leduc‐Gaudet, J., Cefis, M., Ayoub, M., Reynaud, O., Shams, A., Moamer, A., Nery Ferreira, M. F., Hussain, S. N., & Gouspillou, G. (2021) · The Journal of Physiology · doi:10.1113/jp281752 · Cited by 51 · see citing works
“These changes in the expression of mitochondrial fusion and fission proteins were associated with mitochondrial fragmentation in aged animals (Iqbal et al. 2013).”
BackgroundResultInfluentialThe role of mitochondrial fusion and fission in skeletal muscle function and dysfunction
Hood, D. A. (2015) · Frontiers in Bioscience · doi:10.2741/4303 · Cited by 50 · see citing works
“fission to fusion proteins in rat skeletal muscle (49).”
BackgroundInfluentialSligar, 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
Marzetti, E., Guerra, F., Calvani, R., Marini, F., Biancolillo, A., Gervasoni, J., Primiano, A., Coelho-Júnior, H. J., Landi, F., Bernabei, R., et al. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.564417 · Cited by 45 · see citing works
“In particular, derangements of skeletal myocyte quality control mechanisms are thought to play a relevant role in the development and progression of age-related muscle wasting (Iqbal et al., 2013).”
BackgroundHan, C., Lu, P., & Yan, S.-Z. (2021) · Experimental Gerontology · doi:10.1016/j.exger.2021.111648 · Cited by 44 · see citing works
Exercise and the Regulation of Mitochondrial Turnover
Hood, D. A., Tryon, L. D., Vainshtein, A., Memme, J. M., Chen, C., Pauly, M., Crilly, M. J., & Carter, H. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2015.07.007 · Cited by 44 · see citing works
Kitaoka, Y., Nakazato, K., & Ogasawara, R. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00465.2016 · Cited by 43 · see citing works
“A previous study demonstrated that chronic muscle contractile activity led to increased levels of mitochondrial fusion proteins (21).”
BackgroundResultTargeting 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 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
Kim, J., Lee, J.-Y., & Kim, C. Y. (2023) · Nutrients · doi:10.3390/nu15112625 · Cited by 41 · see citing works
“A significantly reduced number of SCs, particularly in type II muscle fibers of the elderly (70–86 years of age) compared to that of younger adults (18–40 years of age) has been reported [80].”
BackgroundExercise, mitochondrial dysfunction and inflammasomes in skeletal muscle
Slavin, M. B., Khemraj, P., & Hood, D. A. (2023) · Biomedical Journal · doi:10.1016/j.bj.2023.100636 · Cited by 41 · see citing works
“This process is regulated by the mitofusin proteins, MFN1 and MFN2, along with OPA1, which are required for the fusion of the outer-and inner mitochondrial membrane, respectively [11].”
BackgroundInfluentialGill, J. F., Delezie, J., Santos, G., McGuirk, S., Schnyder, S., Frank, S., Rausch, M., St‐Pierre, J., & Handschin, C. (2019) · Aging Cell · doi:10.1111/acel.12993 · Cited by 39 · see citing works
Motanova, E. S., Pirazzini, M., Negro, S., Rossetto, O., & Narici, M. V. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102586 · Cited by 40 · see citing works
Regulation of Skeletal Muscle DRP-1 and FIS-1 Protein Expression by IL-6 Signaling
Fix, D. K., Vanderveen, B. N., Counts, B., & Carson, J. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8908457 · Cited by 36 · see citing works
“Mitochondrial remodeling (dynamics) is a process that consists of constant fi ssion and fusion of mitochondria in response to metabolic stressors [19, 21, 23].”
Handy, R. M., & Holloway, G. P. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1151389 · Cited by 38 · see citing works
“Further, experiments modelling muscle disuse in rodents through denervation or hind limb suspension have demonstrated a significant reduction in the mitochondrial fusion: fission ratio and fragmentation of the mitochondrial reticulum (Iqbal et al., 2013).”
BackgroundRuegsegger, G. N., Pataky, M. W., Simha, S., Robinson, M. M., Klaus, K. A., & Nair, K. S. (2023) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00405.2023 · Cited by 38 · see citing works
Chen, J.-C., Wang, R., & Wei, C. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2160961 · Cited by 37 · see citing works
“In mice, mitochondrial morphology also changes with the aging process and can be quantified by the thickness of the mitochondrial layer, distribution, and size (Iqbal et al. 2013).”
BackgroundThirupathi, A., Pieri, B. L. D. S., Queiroz, J. A. M. P., Rodrigues, M. S., Silveira, G. D. B., de Souza, D. R., Luciano, T. F., Silveira, P. C. L., & de Souza, C. T. (2019) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-019-00663-x · Cited by 38 · see citing works
Kitaoka, Y., Takeda, K., Tamura, Y., Fujimaki, S., Takemasa, T., & Hatta, H. (2016) · Physiological Reports · doi:10.14814/phy2.13064 · Cited by 34 · see citing works
“fusion proteins in skeletal muscle (Iqbal et al. 2013; Kitaoka et al. 2016), we found that denervation increased mitochondrial fission proteins, but decreased fusion proteins.”
BackgroundExercise 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
Low-frequency stimulation regulates metabolic gene expression in paralyzed muscle
Petrie, M. A., Suneja, M., & Shields, R. K. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00628.2014 · Cited by 33 · see citing works
“ACAD9)(49, 58), tricarboxylic acid cycle (BRP44, BRP44L, OGDH, SDHB)(6, 49), oxidative 93 phosphorylation (NDUFB1, NDUFA2, CYC1, COQ10A )(27, 49), and mitochondrial 94 remodeling (MFF, OPA1, MFN1, and MFN2) (7, 35, 46, 49).”
InfluentialThe unfolded protein response in relation to mitochondrial biogenesis in skeletal muscle cells
Moosavi, Z. S. M., & Hood, D. A. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00320.2016 · Cited by 33 · see citing works
“Thus, we employed siRNA techniques, as we have done previously (17, 39), to partially reduce CHOP levels.”
MethodRecent advances in mitochondrial turnover during chronic muscle disuse
Tryon, L. D., Vainshtein, A., Memme, J. M., Crilly, M. J., & Hood, D. A. (2014) · Integrative Medicine Research · doi:10.1016/j.imr.2014.09.001 · Cited by 33 · see citing works
Tryon, L. D., Crilly, M. J., & Hood, D. A. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00266.2014 · Cited by 32 · see citing works
Europa, T. A., Nel, M., & Heckmann, J. M. (2019) · Neuromuscular Disorders · doi:10.1016/j.nmd.2019.03.009 · Cited by 32 · see citing works
Regulation of lysosomes in skeletal muscle during exercise, disuse and aging
Moradi, N., Sanfrancesco, V. C., Champsi, S., & Hood, D. A. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.09.028 · Cited by 32 · see citing works
The loss of LRPPRC function induces the mitochondrial unfolded protein response
Köhler, F., Müller-Rischart, A. K., Conradt, B., & Rolland, S. G. M. (2015) · Aging · doi:10.18632/aging.100812 · Cited by 30 · see citing works
“elegans and in rat that mitochondrial fragmentation increases with age and that this fragmentation is accompanied with a loss of mitochondrial volume [26,27].”
BackgroundRole of gp130 in basal and exercise-trained skeletal muscle mitochondrial quality control
Fix, D. K., Hardee, J. P., Gao, S., VanderVeen, B. N., Velázquez, K. T., & Carson, J. A. (2018) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01063.2017 · Cited by 30 · see citing works
“COX enzyme activity was determined by measuring the rate of oxidation of fully reduced cytochrome c at 550 nm as previously described (26).”
BackgroundMethodTargeting skeletal muscle mitochondria to prevent type 2 diabetes in youth
Gordon, J. W., Dolinsky, V. W., Mughal, W., Gordon, G. R., & McGavock, J. (2015) · Biochemistry and Cell Biology · doi:10.1139/bcb-2015-0012 · Cited by 30 · see citing works
Petrie, M. A., Suneja, M., Faidley, E. A., & Shields, R. K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115791 · Cited by 29 · see citing works
“Accordingly, genes associated with glycolysis (PDK4, PDHA1, PDHB, and PDHX) [28–33], fatty acid oxidation (ACADVL, ACADL, ACAD8, ACAD9) [33–36], tricarboxylic acid cycle (TCA) (BRP44, BRP44L, OGDH, SDHB) [33, 37], oxidative phosphorylation (NDUFB1, NDUFA2, CYC1, COQ10A) [33, 38], and mitochondria dynamics including fi…”
BackgroundInfluentialHoshino, D., Kitaoka, Y., & Hatta, H. (2016) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.5.13 · Cited by 31 · see citing works
Joseph, A.-M., Nguyen, L. M. ‐., Welter, A., Dominguez, J. M., Behnke, B. J., & Adhihetty, P. J. (2014) · Biogerontology · doi:10.1007/s10522-014-9526-z · Cited by 28 · see citing works
“Additionally, expression levels of these mitofusins were increased in human skeletal muscle after exercise (Cartoni et al. 2005), as well as in rodents following chronic contractile activity (Iqbal et al. 2013).”
InfluentialExercise 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-citationGehrig, S. M., Mihaylova, V., Frese, S., Mueller, S. M., Ligon‐Auer, M., Spengler, C. M., Petersen, J. A., Lundby, C., & Jung, H. H. (2016) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-016-0488-x · Cited by 27 · see citing works
“decrease in levels of functional mitochondria [17].”
Uemichi, K., Shirai, T., Hanakita, H., & Takemasa, T. (2021) · Physiological Reports · doi:10.14814/phy2.14789 · Cited by 27 · see citing works
Takahashi, K., Kitaoka, Y., Yamamoto, K., Matsunaga, Y., & Hatta, H. (2020) · Nutrients · doi:10.3390/nu12030770 · Cited by 25 · see citing works
“In addition, mitochondria change not only their content and respiratory capacity, but also their morphology in relation to the expression of dynamics regulatory proteins [51,52].”
BackgroundMemme, J. M., Sanfrancesco, V. C., & Hood, D. A. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00080.2023 · Cited by 24 · see citing works
Bellanti, F., Buglio, A. L., & Vendemiale, G. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14122588 · Cited by 24 · see citing works
Mitochondrial plasticity in cancer-related muscle wasting: potential approaches for its management
Vitorino, R., Moreira-Gonçalves, D., & Ferreira, R. (2015) · Current opinion in clinical nutrition and metabolic care · doi:10.1097/mco.0000000000000161 · Cited by 21 · see citing works
Deval, C., Calonne, J., Coudy‐Gandilhon, C., Vazeille, E., Béchet, D., Polge, C., Taillandier, D., Attaix, D., & Combaret, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103691 · Cited by 22 · see citing works
“Muscle disuse is associated with altered fission processes and with defective mitochondrial addressing to autophagy [7,18–21].”
- Authors
- Iqbal, S., Ostojic, O., Singh, K., Joseph, A., & Hood, D. A.
- Affiliations
- York University (CA)
- School of Kinesiology and Health Science, and the Muscle Health Research Centre York University Toronto Ontario M3J 1P3 Canada
- Corresponding author
- Hood, David A.
- ORCID
- Hood, David A.
- Venue
- Muscle & Nerve
- Publisher
- Wiley
- Published
- 2013-11-22
- Volume
- 48
- Issue
- 6
- Pages
- 963-970
- ISSN
- 0148-639X (ISSN-L)
- 1097-4598
- OpenAlex
- W1512819323
- Cited by
- 169
- References
- 43
- Citations by year
- 2026: 6 · 2025: 12 · 2024: 7 · 2023: 13 · 2022: 13 · 2021: 18 · 2020: 17 · 2019: 15 · 2018: 18 · 2017: 10 · 2016: 13 · 2015: 15 · 2014: 9 · 2013: 3
- FWCI
- 5.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Muscle & Nerve (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- mitochondrial fission, mitochondrial fusion, skeletal muscle, OPA1, mitofusin 2, mitochondrial reticulum, muscle disuse, denervation, aging, exercise training, mitochondrial morphology, oxidative capacity
- MeSH terms
- Aging, Animals, Electron Transport Complex IV, Disease Models, Animal, Gene Expression Regulation, Male, Membrane Proteins, Mitochondria, Muscle, Muscle Denervation, Muscular Diseases, Rats, Inbred F344, Rats, Sprague-Dawley, Muscle, Skeletal, GTP Phosphohydrolases, Mitochondrial Proteins, Microscopy, Electron, Transmission, Rats, Mitochondrial Dynamics
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
