The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Type II skeletal myofibers possess unique properties that potentiate mitochondrial H2O2 generation
Abstract
Mitochondrial dysfunction is implicated in a number of skeletal muscle pathologies, most notably aging-induced atrophy and loss of type II myofibers. Although oxygen-derived free radicals are thought to be a primary cause of mitochondrial dysfunction, the underlying factors governing mitochondrial superoxide production in different skeletal myofiber types is unknown. Using a novel in situ approach to measure H 2 O 2 production (indicator of superoxide formation) in permeabilized rat skeletal muscle fiber bundles, we found that mitochondrial free radical leak (H 2 O 2 produced/O 2 consumed) is two- to threefold higher ( P < 0.05) in white (WG, primarily type IIB fibers) than in red (RG, type IIA) gastrocnemius or soleus (type I) myofibers during basal respiration supported by complex I (pyruvate + malate) or complex II (succinate) substrates. In the presence of respiratory inhibitors, maximal rates of superoxide produced at both complex I and complex III are markedly higher in RG and WG than in soleus muscle despite ∼50% less mitochondrial content in WG myofibers. Duplicate experiments conducted with ±exogenous superoxide dismutase revealed striking differences in the topology and/or dismutation of superoxide in WG vs. soleus and RG muscle. When normalized for mitochondrial content, overall H 2 O 2 scavenging capacity is lower in RG and WG fibers, whereas glutathione peroxidase activity, which is largely responsible for H 2 O 2 removal in mitochondria, is similar in all three muscle types. These findings suggest that type II myofibers, particularly type IIB, possess unique properties that potentiate mitochondrial superoxide production and/or release, providing a potential mechanism for the heterogeneous development of mitochondrial dysfunction in skeletal muscle.
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Citations
Cites
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
Premature ageing in mice expressing defective mitochondrial DNA polymerase
Trifunovic, A., Wredenberg, A., Falkenberg, M., Spelbrink, J. N., Rovio, A. T., Bruder, C. E., Bohlooly-Y, M., Gidlöf, S., Oldfors, A., Wibom, R., et al. (2004) · Nature · doi:10.1038/nature02517 · Cited by 2,734
Oxidative Stress and Stress-Activated Signaling Pathways: A Unifying Hypothesis of Type 2 Diabetes
Evans, J. L., Goldfine, I. D., Maddux, B. A., & Grodsky, G. M. (2002) · Endocrine Reviews · doi:10.1210/er.2001-0039 · Cited by 2,232
Topology of superoxide production from different sites in the mitochondrial electron transport chain
St-Pierre, J., Buckingham, J. A., Roebuck, S. J., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207217200 · Cited by 1,545
Generation of reactive oxygen species by the mitochondrial electron transport chain
Liu, Y., Fiskum, G., & Schubert, D. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2002.00744.x · Cited by 1,260
Complex iii releases superoxide to both sides of the inner mitochondrial membrane
Muller, F. L., Liu, Y., & Van Remmen, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407715200 · Cited by 1,036
Han, D., Antunes, F., Canali, R., Rettori, D., & Cadenas, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210269200 · Cited by 711
Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age
Hansford, R. G., Hogue, B. A., & Mildaziene, V. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022420007908 · Cited by 447 · cited 1×
“These findings largely confirm those of previous studies on isolated mitochondria from rat brain, heart, and skeletal muscle (14, 16, 17, 26, 43, 48, 50), demonstrating that complex I is the major site of O2 generation during succinate-supported respiration due to reverse electron flow from complex II to complex I.”
ResultMitochondrial abnormalities are more frequent in muscles undergoing sarcopenia
Bua, E. A., McKiernan, S. H., Wanagat, J., McKenzie, D., & Aiken, J. M. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01102.2001 · Cited by 223
Reduced oxidative power but unchanged antioxidative capacity in skeletal muscle from aged humans
Tonkonogi, M., Fernström, M., Walsh, B., Ji, L. L., Rooyackers, O., Hammarqvist, F., Wernerman, J., & Sahlin, K. (2003) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1044-9 · Cited by 159
Respiration-dependent Removal of Exogenous H2O2 in Brain Mitochondria
Zoccarato, F., Cavallini, L., & Alexandre, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308143200 · Cited by 130
Cited by
Fiber Types in Mammalian Skeletal Muscles
Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022
Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production
Powers, S. K., & Jackson, M. J. (2008) · Physiological Reviews · doi:10.1152/physrev.00031.2007 · Cited by 2,459
Anderson, E. J., Lustig, M. E., Boyle, K. E., Woodlief, T. L., Kane, D. A., Lin, C.-T., Price, J. W., Kang, L., Rabinovitch, P. S., Szeto, H. H., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37048 · Cited by 1,253
Self-citationExercise-induced oxidative stress: Friend or foe?
Powers, S. K., Deminice, R., Ozdemir, M., Yoshihara, T., Bomkamp, M. P., & Hyatt, H. (2020) · Journal of Sport and Health Science · doi:10.1016/j.jshs.2020.04.001 · Cited by 655
Mitochondrial respiration is decreased in skeletal muscle of patients with type 2 diabetes
Mogensen, M., Sahlin, K., Fernström, M., Glintborg, D., Vind, B. F., Beck-Nielsen, H., & Højlund, K. (2007) · Diabetes · doi:10.2337/db06-0981 · Cited by 573
Metadata
- Authors
- Anderson, E. J., & Neufer, P. D.
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2006-03
- Volume
- 290
- Issue
- 3
- Pages
- C844-C851
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W2040559102
- Cited by
- 329
- References
- 11
- FWCI
- 3.23
- Type
- journal article
- Language
- en
- Open access
- closed
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