The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
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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In the citing paper
“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
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
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
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
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×
“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
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
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
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×
“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
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
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
“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
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
“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 530
“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
“Notably, genetic manipulations to activate or inhibit autophagy results into muscle atrophy (Mammucari et al., 2007; Masiero et al., 2009; Romanello et al., 2010).”
Background
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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