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Linked References

1. A. C. Snyder, “Overtraining and glycogen depletion hypothesis,” Medicine and Science in Sports and Exercise, vol. 30, no. 7, pp. 1146–1150, 1998. View at Publisher · View at Google Scholar · View at Scopus
2. W. Y. Liu and A. Y. Lu, “Effect of overtraining on skeletal muscle glycogen, AMPK activity and sarcolemma GLUT4 protein content in rats,” Chinese Journal of Sports Medicine, vol. 25, no. 6, pp. 668–673, 2006.
3. T. M. Liu and Y. L. Zhang, “Experimental study on the glutamine's intervention effect on the opening of permeability transition pore in myocardial mitochondrial membrane,” Zhongguo Ying Yong Sheng Li Xue Za Zhi, vol. 28, no. 1, pp. 34–37, 2012.
4. A. P. Halestrap, “What is the mitochondrial permeability transition pore?” Journal of Molecular and Cellular Cardiology, vol. 46, no. 6, pp. 821–831, 2009. View at Publisher · View at Google Scholar · View at Scopus
5. G. Szabadkai and R. Rizzuto, “Participation of endoplasmic reticulum and mitochondrial calcium handling in apoptosis: more than just neighborhood?” FEBS Letters, vol. 567, no. 1, pp. 111–115, 2004. View at Publisher · View at Google Scholar · View at Scopus
6. X. Yi, X. M. Yin, and Z. Dong, “Inhibition of Bid-induced apoptosis by Bcl-2. tBid insertion, Bax translocation, and Bax/Bak oligomerization suppressed,” Journal of Biological Chemistry, vol. 278, no. 19, pp. 16992–16999, 2003. View at Publisher · View at Google Scholar · View at Scopus
7. S. Z. Ding, W. X. Wang, K. J. Lian, and H. W. Xu, “The effect of exhaustive swimming on calcium transport in rat heart mitochondria,” Shengwu Hua Xue Za Zhi, vol. 11, no. 3, pp. 366–367, 1995.
8. H. R. Kim, G. H. Lee, E. Y. Cho, S. W. Chae, T. Ahn, and H. J. Chae, “Bax inhibitor 1 regulates ER-stress-induced ROS accumulation through the regulation of cytochrome P450 2E1,” Journal of Cell Science, vol. 122, no. 8, pp. 1126–1133, 2009. View at Publisher · View at Google Scholar · View at Scopus
9. K. S. Echtay, D. Roussel, J. St-Plerre et al., “Superoxide activates mitochondrial uncoupling proteins,” Nature, vol. 415, no. 6867, pp. 96–99, 2002. View at Publisher · View at Google Scholar · View at Scopus
10. Z. Derdak, T. A. Garcia, and G. Baffy, “Detection of uncoupling protein-2 (UCP2) as a mitochondrial modulator of apoptosis,” Methods in Molecular Biology, vol. 559, pp. 205–217, 2009. View at Publisher · View at Google Scholar · View at Scopus
11. T. G. Bedford, C. M. Tipton, and N. C. Wilson, “Maximum oxygen consumption of rats and its changes with various experimental procedures,” Journal of Applied Physiology Respiratory Environmental and Exercise Physiology, vol. 47, no. 6, pp. 1278–1283, 1979. View at Scopus
12. M. Alonso, P. S. Collado, and J. González-Gallego, “Melatonin inhibits the expression of the inducible isoform of nitric oxide synthase and nuclear factor kappa B activation in rat skeletal muscle,” Journal of Pineal Research, vol. 41, no. 1, pp. 8–14, 2006. View at Publisher · View at Google Scholar · View at Scopus
13. H. S. Sherratt, N. J. Watmough, M. A. Johnson, and D. M. Turnbull, “Methods for study of normal and abnormal skeletal muscle mitochondria,” Methods of Biochemical Analysis, vol. 33, pp. 243–335, 1988. View at Scopus
14. O. Cunningham, A. M. McElligott, A. M. Carroll et al., “Selective detection of UCP 3 expression in skeletal muscle: effect of thyroid status and temperature acclimation,” Biochimica et Biophysica Acta, vol. 1604, no. 3, pp. 170–179, 2003. View at Publisher · View at Google Scholar · View at Scopus
15. M. J. Lehmann, W. Lormes, A. Opitz-Gress et al., “Training and overtraining: an overview and experimental results in endurance sports,” Journal of Sports Medicine and Physical Fitness, vol. 37, no. 1, pp. 7–17, 1997. View at Scopus
16. R. Hohl, R. L. P. Ferraresso, R. B. De Oliveira, R. Lucco, R. Brenzikofer, and D. V. De Macedo, “Development and characterization of an overtraining animal model,” Medicine and Science in Sports and Exercise, vol. 41, no. 5, pp. 1155–1163, 2009. View at Publisher · View at Google Scholar · View at Scopus
17. X. L. Sun, Y. Liu, T. Dai, J. H. Ding, and G. Hu, “Uncoupling protein 2 knockout exacerbates depression-like behaviors in mice via enhancing inflammatory response,” Neuroscience, vol. 192, pp. 507–514, 2011.
18. A. M. Niess, H. H. Dickhuth, H. Northoff, and E. Fehrenbach, “Free radicals and oxidative stress in exercise-immunological aspects,” Exercise Immunology Review, no. 5, pp. 22–56, 1999. View at Scopus
19. M. C. Gómez-Cabrera, F. V. Pallardó, J. Sastre, J. Viña, and L. Garcia-Del-Moral, “Allopurinol and markers of muscle damage among participants in the tour de France,” Journal of the American Medical Association, vol. 289, no. 19, pp. 2503–2504, 2003. View at Publisher · View at Google Scholar · View at Scopus
20. C. C. Zoppi and D. V. MacEdo, “Overreaching-induced oxidative stress, enhanced HSP72 expression, antioxidant and oxidative enzymes downregulation,” Scandinavian Journal of Medicine and Science in Sports, vol. 18, no. 1, pp. 67–76, 2008. View at Publisher · View at Google Scholar · View at Scopus
21. W. L. Knez, D. G. Jenkins, and J. S. Coombes, “Oxidative stress in half and full Ironman triathletes,” Medicine and Science in Sports and Exercise, vol. 39, no. 2, pp. 283–288, 2007. View at Publisher · View at Google Scholar · View at Scopus
22. M. Tanskanen, M. Atalay, and A. Uusitalo, “Altered oxidative stress in overtrained athletes,” Journal of Sports Sciences, vol. 28, no. 3, pp. 309–317, 2010. View at Publisher · View at Google Scholar · View at Scopus
23. K. Margonis, I. G. Fatouros, A. Z. Jamurtas et al., “Oxidative stress biomarkers responses to physical overtraining: implications for diagnosis,” Free Radical Biology and Medicine, vol. 43, no. 6, pp. 901–910, 2007. View at Publisher · View at Google Scholar · View at Scopus
24. Y. Echigoya, S. Morita, T. Itou, and T. Sakai, “Effects of extracellular lactate on production of reactive oxygen species by equine polymorphonuclear leukocytes in vitro,” American Journal of Veterinary Research, vol. 73, no. 8, pp. 1290–1298, 2012.
25. J. Nie, C. Jiang, Y. Zhang, Q. Shi, and S. Liu, “Study on molecular mechanism of exercise—induced fatigue in mitochondrial membrane. IV. Relationships between proton potential energy across membrane, proton leak and ROS generation during acute exercise,” Chinese Journal of Sports Medicine, vol. 20, no. 2, pp. 134–138, 2001.
26. A. J. Lambert and M. D. Brand, “Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane,” Biochemical Journal, vol. 382, no. 2, pp. 511–517, 2004. View at Publisher · View at Google Scholar · View at Scopus
27. R. J. Mailloux and M. E. Harper, “Uncoupling proteins and the control of mitochondrial reactive oxygen species production,” Free Radical Biology and Medicine, vol. 51, no. 6, pp. 1106–1115, 2011.
28. M. D. Brand, C. Affourtit, T. C. Esteves et al., “Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins,” Free Radical Biology and Medicine, vol. 37, no. 6, pp. 755–767, 2004. View at Publisher · View at Google Scholar · View at Scopus
29. R. N. Cortright, D. Zheng, J. P. Jones et al., “Regulation of skeletal muscle UCP-2 and UCP-3 gene expression by exercise and denervation,” American Journal of Physiology, vol. 276, no. 1, pp. E217–E221, 1999. View at Scopus
30. G. R. Degasperi, T. Romanatto, R. G. P. Denis et al., “UCP2 protects hypothalamic cells from TNF-α-induced damage,” FEBS Letters, vol. 582, no. 20, pp. 3103–3110, 2008. View at Publisher · View at Google Scholar · View at Scopus
31. C. B. Chan, D. De Leo, J. W. Joseph et al., “Increased uncoupling protein-2 levels in β-cells are associated with impaired glucose-stimulated insulin secretion: mechanism of action,” Diabetes, vol. 50, no. 6, pp. 1302–1310, 2001. View at Scopus
32. J. A. Stuart, J. A. Harper, K. M. Brindle, M. B. Jekabsons, and M. D. Brand, “Physiological levels of mammalian uncoupling protein 2 do not uncouple yeast mitochondria,” Journal of Biological Chemistry, vol. 276, no. 21, pp. 18633–18639, 2001. View at Publisher · View at Google Scholar · View at Scopus
33. K. D. Chavin, S. Yang, H. Z. Lin et al., “Obesity induces expression of uncoupling protein-2 in hepatocytes and promotes liver ATP depletion,” Journal of Biological Chemistry, vol. 274, no. 9, pp. 5692–5700, 1999. View at Publisher · View at Google Scholar · View at Scopus
34. F. Bouillaud, “UCP2, not a physiologically relevant uncoupler but a glucose sparing switch impacting ROS production and glucose sensing,” Biochimica et Biophysica Acta, vol. 1787, no. 5, pp. 377–383, 2009. View at Publisher · View at Google Scholar · View at Scopus
35. H. Westerblad and D. G. Allen, “Emerging roles of ROS/RNS in muscle function and fatigue, Antioxidants,” Redox Signaling, vol. 15, no. 9, pp. 2487–2499, 2011.
36. A. M. Bellinger, S. Reiken, M. Dura et al., “Remodeling of ryanodine receptor complex causes“leaky” channels: a molecular mechanism for decreased exercise capacity,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 6, pp. 2198–2202, 2008. View at Publisher · View at Google Scholar · View at Scopus
37. N. Li, J. Wang, F. Gao, Y. Tian, R. Song, and S. J. Zhu, “The role of uncoupling protein 2 in the apoptosis induced by free fatty acid in rat cardiomyocytes,” Journal of Cardiovascular Pharmacology, vol. 55, no. 2, pp. 161–167, 2010. View at Publisher · View at Google Scholar · View at Scopus
38. S. Deng, Y. Yang, Y. Han et al., “UCP2 inhibits ROS-mediated apoptosis in A549 under hypoxic conditions,” PLoS ONE, vol. 7, no. 1, Article ID e30714, 2012.
39. Z. N. Oltvai, C. L. Milliman, and S. J. Korsmeyer, “Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death,” Cell, vol. 74, no. 4, pp. 609–619, 1993. View at Publisher · View at Google Scholar · View at Scopus
40. H. Kamata, S. I. Honda, S. Maeda, L. Chang, H. Hirata, and M. Karin, “Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases,” Cell, vol. 120, no. 5, pp. 649–661, 2005. View at Publisher · View at Google Scholar · View at Scopus
41. R. M. Kluck, E. Bossy-Wetzel, D. R. Green, and D. D. Newmeyer, “The release of cytochrome c from mitochondria: a primary site for Bcl- 2 regulation of apoptosis,” Science, vol. 275, no. 5303, pp. 1132–1136, 1997. View at Publisher · View at Google Scholar · View at Scopus
42. M. Narita, S. Shimizu, T. Ito et al., “Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 25, pp. 14681–14686, 1998. View at Publisher · View at Google Scholar · View at Scopus
43. S. C. Cosulich, P. J. Savory, and P. R. Clarke, “Bcl-2 regulates amplification of caspase activation by cytochrome c,” Current Biology, vol. 9, no. 3, pp. 147–150, 1999. View at Publisher · View at Google Scholar · View at Scopus
44. G. Villani, M. Greco, S. Papa, and G. Attardi, “Low reserve of cytochrome c oxidase capacity in vivo in the respiratory chain of a variety of human cell types,” Journal of Biological Chemistry, vol. 273, no. 48, pp. 31829–31836, 1999. View at Publisher · View at Google Scholar · View at Scopus
45. B. Kadenbach, S. Arnold, I. Lee, and M. Hüttemann, “The possible role of cytochrome c oxidase in stress-induced apoptosis and degenerative diseases,” Biochimica et Biophysica Acta, vol. 1655, no. 1–3, pp. 400–408, 2004. View at Publisher · View at Google Scholar · View at Scopus