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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.
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“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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 the citing paper
“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]
Citations
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Mitochondrial dysfunction and sarcopenia of aging: from signaling pathways to clinical trials
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“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
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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
“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 245
“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 222
Joseph, A., Adhihetty, P. J., & Leeuwenburgh, C. (2016) · The Journal of Physiology · doi:10.1113/jp270659 · Cited by 186
“2008), as well as mitochondria that appear punctate and fragmented (Ljubicic et al. 2009; Iqbal et al. 2013).”
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“…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
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
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 187
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“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
Impact of Aging and Exercise on Mitochondrial Quality Control in Skeletal Muscle
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“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
“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
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
“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
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
“During aging, an increased incidence of mitochondrial fragmentation has been observed, with a concomitant increase in the expression of mitochondrial fission proteins (19).”
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Age-dependent changes in mitochondrial morphology and volume are not predictors of lifespan
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“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 123
“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
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“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 110
“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].”
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Mitochondrial Impairment in Sarcopenia
Bellanti, F., Buglio, A. L., & Vendemiale, G. (2021) · Biology · doi:10.3390/biology10010031 · Cited by 104
“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
“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
“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 102
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 92
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
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 92
“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 87
Mitofusin 2 as a Driver That Controls Energy Metabolism and Insulin Signaling
Antonio 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
Mechanical ventilation triggers abnormal mitochondrial dynamics and morphology in the diaphragm
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Mitochondrial Mechanisms of Neuromuscular Junction Degeneration with Aging
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Aging shifts mitochondrial dynamics toward fission to promote germline stem cell loss.
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“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
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
“…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 71
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“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 65
“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 68
“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 64
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 63
“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
“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
Manifestations of Age on Autophagy, Mitophagy and Lysosomes in Skeletal Muscle
Triolo, M., & Hood, D. A. (2021) · Cells · doi:10.3390/cells10051054 · Cited by 60
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
“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
“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
“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
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
“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
“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
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
“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
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
Kitaoka, Y., Nakazato, K., & Ogasawara, R. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00465.2016 · Cited by 43
“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 43
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 45
Kim, J., Lee, J.-Y., & Kim, C. Y. (2023) · Nutrients · doi:10.3390/nu15112625 · Cited by 45
“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 44
“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 41
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 43
Regulation of Skeletal Muscle DRP-1 and FIS-1 Protein Expression by IL-6 Signaling
Fix, D. K., VanderVeen, B. N., Counts, B. R., & Carson, J. A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8908457 · Cited by 39
“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
“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
Chen, J.-C., Wang, R., & Wei, C. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2160961 · Cited by 42
“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 40
Kitaoka, Y., Takeda, K., Tamura, Y., Fujimaki, S., Takemasa, T., & Hatta, H. (2016) · Physiological Reports · doi:10.14814/phy2.13064 · Cited by 34
“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 37
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
“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 34
“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
Tryon, L. D., Crilly, M. J., & Hood, D. A. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00266.2014 · Cited by 33
Europa, T. A., Nel, M., & Heckmann, J. M. (2019) · Neuromuscular Disorders · doi:10.1016/j.nmd.2019.03.009 · Cited by 32
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 33
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 32
“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 31
“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
Petrie, M. A., Suneja, M., Faidley, E. A., & Shields, R. K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115791 · Cited by 29
“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
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
“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
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
“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
Takahashi, K., Kitaoka, Y., Yamamoto, K., Matsunaga, Y., & Hatta, H. (2020) · Nutrients · doi:10.3390/nu12030770 · Cited by 25
“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 25
Bellanti, F., Buglio, A. L., & Vendemiale, G. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14122588 · Cited by 24
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
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
“Muscle disuse is associated with altered fission processes and with defective mitochondrial addressing to autophagy [7,18–21].”
Metadata
- 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 (medical) › 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
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