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BioMed Research International
Volume 2015, Article ID 515437, 9 pages
http://dx.doi.org/10.1155/2015/515437
Review Article

Monoamine Oxidases as Potential Contributors to Oxidative Stress in Diabetes: Time for a Study in Patients Undergoing Heart Surgery

1Department of Functional Sciences-Pathophysiology, “Victor Babes” University of Medicine and Pharmacy, 2 Eftimie Murgu Square, 300041 Timisoara, Romania
2Department of Microscopical Morphology-Histology, “Victor Babes” University of Medicine and Pharmacy, 2 Eftimie Murgu Square, 300041 Timisoara, Romania
3Department of Microscopical Morphology-Morphopathology, “Victor Babes” University of Medicine and Pharmacy, 2 Eftimie Murgu Square, 300041 Timisoara, Romania
4Department of Cardiology-Cardiovascular Surgery, “Victor Babes” University of Medicine and Pharmacy, 2 Eftimie Murgu Square, 300041 Timisoara, Romania
5Department of Cardiology-2nd Cardiology Clinic, “Victor Babes” University of Medicine and Pharmacy, 2 Eftimie Murgu Square, 300041 Timisoara, Romania

Received 2 July 2014; Revised 1 September 2014; Accepted 17 September 2014

Academic Editor: M.-Saadeh Suleiman

Copyright © 2015 Oana M. Duicu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. A. S. Go, D. Mozaffarian, V. L. Roger et al., “Heart disease and stroke statistics—2014 update: a report from the American Heart Association,” Circulation, vol. 129, no. 3, pp. e28–e292, 2014. View at Publisher · View at Google Scholar · View at Scopus
  2. L. Guariguata, D. R. Whiting, and I. Hambleton, “Global estimates of diabetes prevalence for 2013 and projections for 2035,” Diabetes Research and Clinical Practice, vol. 103, no. 2, pp. 137–149, 2014. View at Google Scholar
  3. Authors/Task Force Members, L. Ryden, P. J. Grant et al., “ESC Guidelines on diabetes, pre-diabetes, and cardiovascular diseases developed in collaboration with the EASD: the Task Force on diabetes, pre-diabetes, and cardiovascular diseases of the European Society of Cardiology (ESC) and developed in collaboration with the European Association for the Study of Diabetes (EASD),” European Heart Journal, vol. 34, no. 39, pp. 3035–3087, 2013. View at Google Scholar
  4. I. Martin-Timon, C. Sevillano-Collantes, A. Segura-Galindo et al., “Type 2 diabetes and cardiovascular disease: have all risk factors the same strength?” World Journal of Diabetes, vol. 5, no. 4, pp. 444–470, 2014. View at Google Scholar
  5. W. B. Kannel and D. L. McGee, “Diabetes and cardiovascular disease. The Framingham study,” The Journal of the American Medical Association, vol. 241, no. 19, pp. 2035–2038, 1979. View at Publisher · View at Google Scholar · View at Scopus
  6. S. Boudina and E. D. Abel, “Diabetic cardiomyopathy revisited,” Circulation, vol. 115, no. 25, pp. 3213–3223, 2007. View at Publisher · View at Google Scholar · View at Scopus
  7. D. B. Zorov, C. R. Filburn, L.-O. Klotz, J. L. Zweier, and S. J. Sollott, “Reactive oxygen species (ROS)-induced ROS release: a new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes,” The Journal of Experimental Medicine, vol. 192, no. 7, pp. 1001–1014, 2000. View at Publisher · View at Google Scholar · View at Scopus
  8. D. B. Zorov, M. Juhaszova, and S. J. Sollott, “Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release,” Physiological Reviews, vol. 94, no. 3, pp. 909–950, 2014. View at Google Scholar
  9. A. Daiber, “Redox signaling (cross-talk) from and to mitochondria involves mitochondrial pores and reactive oxygen species,” Biochimica et Biophysica Acta: Bioenergetics, vol. 1797, no. 6-7, pp. 897–906, 2010. View at Publisher · View at Google Scholar · View at Scopus
  10. S. Karbach, P. Wenzel, A. Waisman et al., “eNOS uncoupling in cardiovascular diseases—the role of oxidative stress and inflammation,” Current Pharmaceutical Design, vol. 20, no. 22, pp. 3579–3594, 2014. View at Google Scholar
  11. R. P. Brandes, N. Weissmann, and K. Schröder, “Redox-mediated signal transduction by cardiovascular Nox NADPH oxidases,” Journal of Molecular and Cellular Cardiology, vol. 73, pp. 70–79, 2014. View at Publisher · View at Google Scholar · View at Scopus
  12. A. Sturza, M. S. Leisegang, A. Babelova et al., “Monoamine oxidases are mediators of endothelial dysfunction in the mouse aorta,” Hypertension, vol. 62, no. 1, pp. 140–146, 2013. View at Publisher · View at Google Scholar · View at Scopus
  13. M. A. Ismahil, T. Hamid, S. S. Bansal, B. Patel, J. R. Kingery, and S. D. Prabhu, “Remodeling of the mononuclear phagocyte network underlies chronic inflammation and disease progression in heart failure: critical importance of the cardiosplenic axis,” Circulation research, vol. 114, no. 2, pp. 266–282, 2014. View at Publisher · View at Google Scholar · View at Scopus
  14. N. Glezeva and J. A. Baugh, “Role of inflammation in the pathogenesis of heart failure with preserved ejection fraction and its potential as a therapeutic target,” Heart Failure Reviews, vol. 19, no. 5, pp. 681–694, 2014. View at Publisher · View at Google Scholar
  15. M. M. J. van Greevenbroek, C. G. Schalkwijk, and C. D. A. Stehouwer, “Obesity-associated low-grade inflammation in type 2 diabetes mellitus: causes and consequences,” Netherlands Journal of Medicine, vol. 71, no. 4, pp. 174–187, 2013. View at Google Scholar · View at Scopus
  16. K. Fujiu and R. Nagai, “Contributions of cardiomyocyte-cardiac fibroblast-immune cell interactions in heart failure development,” Basic Research in Cardiology, vol. 108, no. 4, article 357, 2013. View at Publisher · View at Google Scholar · View at Scopus
  17. R. Zhou, A. S. Yazdi, P. Menu, and J. Tschopp, “A role for mitochondria in NLRP3 inflammasome activation,” Nature, vol. 469, no. 7329, pp. 221–226, 2011. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Kröller-Schön, S. Steven, S. Kossmann et al., “Molecular mechanisms of the crosstalk between mitochondria and NADPH oxidase through reactive oxygen species—studies in white blood cells and in animal models,” Antioxidants and Redox Signaling, vol. 20, no. 2, pp. 247–266, 2014. View at Publisher · View at Google Scholar · View at Scopus
  19. Z. V. Varga, Z. Giricz, L. Liaudet, G. Haskó, P. Ferdinandy, and P. Pacher, “Interplay of oxidative, nitrosative/nitrative stress, inflammation, cell death and autophagy in diabetic cardiomyopathy,” Biochimica et Biophysica Acta (BBA): Molecular Basis of Disease, 2014. View at Publisher · View at Google Scholar
  20. J. Fuentes-Antrás, A. M. Ioan, J. Tuñón, J. Egido, and Ó. Lorenzo, “Activation of toll-like receptors and inflammasome complexes in the diabetic cardiomyopathy-associated inflammation,” International Journal of Endocrinology, vol. 2014, Article ID 847827, 10 pages, 2014. View at Publisher · View at Google Scholar · View at Scopus
  21. M. G. Rosca, B. Tandler, and C. L. Hoppel, “Mitochondria in cardiac hypertrophy and heart failure,” Journal of Molecular and Cellular Cardiology, vol. 55, no. 1, pp. 31–41, 2013. View at Publisher · View at Google Scholar · View at Scopus
  22. M. Osterholt, T. D. Nguyen, M. Schwarzer, and T. Doenst, “Alterations in mitochondrial function in cardiac hypertrophy and heart failure,” Heart Failure Reviews, vol. 18, no. 5, pp. 645–656, 2013. View at Publisher · View at Google Scholar · View at Scopus
  23. C. E. Murdoch, M. Zhang, A. C. Cave, and A. M. Shah, “NADPH oxidase-dependent redox signalling in cardiac hypertrophy, remodelling and failure,” Cardiovascular Research, vol. 71, no. 2, pp. 208–215, 2006. View at Publisher · View at Google Scholar · View at Scopus
  24. Y. Octavia, H. P. Brunner-La Rocca, and A. L. Moens, “NADPH oxidase-dependent oxidative stress in the failing heart: from pathogenic roles to therapeutic approach,” Free Radical Biology and Medicine, vol. 52, no. 2, pp. 291–297, 2012. View at Publisher · View at Google Scholar · View at Scopus
  25. R. Ventura-Clapier, A. Garnier, V. Veksler, and F. Joubert, “Bioenergetics of the failing heart,” Biochimica et Biophysica Acta—Molecular Cell Research, vol. 1813, no. 7, pp. 1360–1372, 2011. View at Publisher · View at Google Scholar · View at Scopus
  26. M. Zhang, A. C. Brewer, K. Schröder et al., “NADPH oxidase-4 mediates protection against chronic load-induced stress in mouse hearts by enhancing angiogenesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 42, pp. 18121–18126, 2010. View at Publisher · View at Google Scholar · View at Scopus
  27. J. Kuroda, T. Ago, S. Matsushima, P. Zhai, M. D. Schneider, and J. Sadoshima, “NADPH oxidase 4 (Nox4) is a major source of oxidative stress in the failing heart,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 35, pp. 15565–15570, 2010. View at Publisher · View at Google Scholar · View at Scopus
  28. J. F. Turrens, “Mitochondrial formation of reactive oxygen species,” The Journal of Physiology, vol. 552, part 2, pp. 335–344, 2003. View at Publisher · View at Google Scholar · View at Scopus
  29. M. P. Murphy, “How mitochondria produce reactive oxygen species,” Biochemical Journal, vol. 417, no. 1, pp. 1–13, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. A. Nickel, M. Kohlhaas, and C. Maack, “Mitochondrial reactive oxygen species production and elimination,” Journal of Molecular and Cellular Cardiology, vol. 73, pp. 26–33, 2014. View at Publisher · View at Google Scholar · View at Scopus
  31. N. Kaludercic, J. Mialet-Perez, N. Paolocci, A. Parini, and F. Di Lisa, “Monoamine oxidases as sources of oxidants in the heart,” Journal of Molecular and Cellular Cardiology, vol. 73, pp. 34–42, 2014. View at Publisher · View at Google Scholar · View at Scopus
  32. E. Schulz, P. Wenzel, T. Münzel, and A. Daiber, “Mitochondrial redox signaling: interaction of mitochondrial reactive oxygen species with other sources of oxidative stress,” Antioxidants and Redox Signaling, vol. 20, no. 2, pp. 308–324, 2014. View at Publisher · View at Google Scholar · View at Scopus
  33. E. J. Lesnefsky, S. Moghaddas, B. Tandler, J. Kerner, and C. L. Hoppel, “Mitochondrial dysfunction in cardiac disease: ischemia—reperfusion, aging, and heart failure,” Journal of Molecular and Cellular Cardiology, vol. 33, no. 6, pp. 1065–1089, 2001. View at Publisher · View at Google Scholar · View at Scopus
  34. C. M. Sag, C. X. C. Santos, and A. M. Shah, “Redox regulation of cardiac hypertrophy,” Journal of Molecular and Cellular Cardiology, vol. 73, pp. 103–111, 2014. View at Publisher · View at Google Scholar · View at Scopus
  35. E. D. Abel and T. Doenst, “Mitochondrial adaptations to physiological vs. pathological cardiac hypertrophy,” Cardiovascular Research, vol. 90, no. 2, pp. 234–242, 2011. View at Publisher · View at Google Scholar · View at Scopus
  36. T. Liu and B. O'Rourke, “Regulation of mitochondrial Ca2+ and its effects on energetics and redox balance in normal and failing heart,” Journal of Bioenergetics and Biomembranes, vol. 41, no. 2, pp. 127–132, 2009. View at Publisher · View at Google Scholar · View at Scopus
  37. M. Luo and M. E. Anderson, “Mechanisms of altered Ca2+ handling in heart failure,” Circulation Research, vol. 113, no. 6, pp. 690–708, 2013. View at Publisher · View at Google Scholar · View at Scopus
  38. H. Tsutsui, S. Kinugawa, and S. Matsushima, “Oxidative stress and heart failure,” American Journal of Physiology: Heart and Circulatory Physiology, vol. 301, no. 6, pp. H2181–H2190, 2011. View at Publisher · View at Google Scholar · View at Scopus
  39. T. Doenst, T. D. Nguyen, and E. D. Abel, “Cardiac metabolism in heart failure: implications beyond atp production,” Circulation Research, vol. 113, no. 6, pp. 709–724, 2013. View at Publisher · View at Google Scholar · View at Scopus
  40. A. N. Carley, H. Taegtmeyer, and E. D. Lewandowski, “Mechanisms linking energy substrate metabolism to the function of the heart,” Circulation Research, vol. 114, no. 4, pp. 717–729, 2014. View at Publisher · View at Google Scholar · View at Scopus
  41. H. Ardehali, H. N. Sabbah, M. A. Burke et al., “Targeting myocardial substrate metabolism in heart failure: potential for new therapies,” European Journal of Heart Failure, vol. 14, no. 2, pp. 120–129, 2012. View at Publisher · View at Google Scholar · View at Scopus
  42. S. Neubauer, “The failing heart—an engine out of fuel,” The New England Journal of Medicine, vol. 356, no. 11, pp. 1140–1151, 2007. View at Publisher · View at Google Scholar · View at Scopus
  43. W. C. Stanley, F. A. Recchia, and G. D. Lopaschuk, “Myocardial substrate metabolism in the normal and failing heart,” Physiological Reviews, vol. 85, no. 3, pp. 1093–1129, 2005. View at Publisher · View at Google Scholar · View at Scopus
  44. H. M. Viola and L. C. Hool, “Targeting calcium and the mitochondria in prevention of pathology in the heart,” Current Drug Targets, vol. 12, no. 5, pp. 748–760, 2011. View at Publisher · View at Google Scholar · View at Scopus
  45. A. Herrero and G. Barja, “Localization of the site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria,” Journal of Bioenergetics and Biomembranes, vol. 32, no. 6, pp. 609–615, 2000. View at Publisher · View at Google Scholar · View at Scopus
  46. D. Han, E. Williams, and E. Cadenas, “Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space,” Biochemical Journal, vol. 353, no. 2, pp. 411–416, 2001. View at Publisher · View at Google Scholar · View at Scopus
  47. F. L. Muller, Y. Liu, and H. Van Remmen, “Complex III releases superoxide to both sides of the inner mitochondrial membrane,” Journal of Biological Chemistry, vol. 279, no. 47, pp. 49064–49073, 2004. View at Publisher · View at Google Scholar · View at Scopus
  48. J. St-Pierre, J. A. Buckingham, S. J. Roebuck, and M. D. Brand, “Topology of superoxide production from different sites in the mitochondrial electron transport chain,” The Journal of Biological Chemistry, vol. 277, no. 47, pp. 44784–44790, 2002. View at Publisher · View at Google Scholar · View at Scopus
  49. Y.-R. Chen and J. L. Zweier, “Cardiac mitochondria and reactive oxygen species generation,” Circulation Research, vol. 114, no. 3, pp. 524–537, 2014. View at Publisher · View at Google Scholar · View at Scopus
  50. A. Y. Andreyev, Y. E. Kushnareva, and A. A. Starkov, “Mitochondrial metabolism of reactive oxygen species,” Biochemistry, vol. 70, no. 2, pp. 200–214, 2005. View at Publisher · View at Google Scholar · View at Scopus
  51. T. Ide, H. Tsutsui, S. Kinugawa et al., “Mitochondrial electron transport complex I is a potential source of oxygen free radicals in the failing myocardium,” Circulation Research, vol. 85, no. 4, pp. 357–363, 1999. View at Publisher · View at Google Scholar · View at Scopus
  52. T. Ide, H. Tsutsui, S. Kinugawa et al., “Direct evidence for increased hydroxyl radicals originating from superoxide in the failing myocardium,” Circulation Research, vol. 86, no. 2, pp. 152–157, 2000. View at Publisher · View at Google Scholar · View at Scopus
  53. J. Marín-García, M. J. Goldenthal, and G. W. Moe, “Abnormal cardiac and skeletal muscle mitochondrial function in pacing-induced cardiac failure,” Cardiovascular Research, vol. 52, no. 1, pp. 103–110, 2001. View at Publisher · View at Google Scholar · View at Scopus
  54. J. Marín-García, M. J. Goldenthal, S. Damle, Y. Pi, and G. W. Moe, “Regional distribution of mitochondrial dysfunction and apoptotic remodeling in pacing-induced heart failure,” Journal of Cardiac Failure, vol. 15, no. 8, pp. 700–708, 2009. View at Publisher · View at Google Scholar · View at Scopus
  55. T. Doenst, G. Pytel, A. Schrepper et al., “Decreased rates of substrate oxidation ex vivo predict the onset of heart failure and contractile dysfunction in rats with pressure overload,” Cardiovascular Research, vol. 86, no. 3, pp. 461–470, 2010. View at Publisher · View at Google Scholar · View at Scopus
  56. M. Schwarzer, M. Osterholt, A. Lunkenbein et al., “Mitochondrial ROS production and respiratory complex activity in rats with pressure overload-induced heart failure,” The Journal of Physiology, vol. 592, pp. 3767–3782, 2014. View at Google Scholar
  57. E. R. Griffiths, I. Friehs, E. Scherr, D. Poutias, F. X. McGowan, and P. J. del Nido, “Electron transport chain dysfunction in neonatal pressure-overload hypertrophy precedes cardiomyocyte apoptosis independent of oxidative stress,” Journal of Thoracic and Cardiovascular Surgery, vol. 139, no. 6, pp. 1609–1617, 2010. View at Publisher · View at Google Scholar · View at Scopus
  58. G. C. Sparagna, A. J. Chicco, R. C. Murphy et al., “Loss of cardiac tetralinoleoyl cardiolipin in human and experimental heart failure,” Journal of Lipid Research, vol. 48, no. 7, pp. 1559–1570, 2007. View at Publisher · View at Google Scholar · View at Scopus
  59. T. Ide, H. Tsutsui, S. Hayashidani et al., “Mitochondrial DNA damage and dysfunction associated with oxidative stress in failing hearts after myocardial infarction,” Circulation Research, vol. 88, no. 5, pp. 529–535, 2001. View at Publisher · View at Google Scholar · View at Scopus
  60. M. G. Rosca, E. J. Vazquez, J. Kerner et al., “Cardiac mitochondria in heart failure: decrease in respirasomes and oxidative phosphorylation,” Cardiovascular Research, vol. 80, no. 1, pp. 30–39, 2008. View at Publisher · View at Google Scholar · View at Scopus
  61. M. G. Rosca and C. L. Hoppel, “New aspects of impaired mitochondrial function in heart failure,” Journal of Bioenergetics and Biomembranes, vol. 41, no. 2, pp. 107–112, 2009. View at Publisher · View at Google Scholar · View at Scopus
  62. V. G. Sharov, A. V. Todor, N. Silverman, S. Goldstein, and H. N. Sabbah, “Abnormal mitochondrial respiration in failed human myocardium,” Journal of Molecular and Cellular Cardiology, vol. 32, no. 12, pp. 2361–2367, 2000. View at Publisher · View at Google Scholar · View at Scopus
  63. H. Lemieux, S. Semsroth, H. Antretter, D. Höfer, and E. Gnaiger, “Mitochondrial respiratory control and early defects of oxidative phosphorylation in the failing human heart,” International Journal of Biochemistry and Cell Biology, vol. 43, no. 12, pp. 1729–1738, 2011. View at Publisher · View at Google Scholar · View at Scopus
  64. R. J. Scheubel, M. Tostlebe, A. Simm et al., “Dysfunction of mitochondrial respiratory chain complex I in human failing myocardium is not due to disturbed mitochondrial gene expression,” Journal of the American College of Cardiology, vol. 40, no. 12, pp. 2174–2181, 2002. View at Publisher · View at Google Scholar · View at Scopus
  65. M. Bayeva, M. Gheorghiade, and H. Ardehali, “Mitochondria as a therapeutic target in heart failure,” Journal of the American College of Cardiology, vol. 61, no. 6, pp. 599–610, 2013. View at Publisher · View at Google Scholar · View at Scopus
  66. N. Stride, S. Larsen, M. Hey-Mogensen et al., “Decreased mitochondrial oxidative phosphorylation capacity in the human heart with left ventricular systolic dysfunction,” European Journal of Heart Failure, vol. 15, no. 2, pp. 150–157, 2013. View at Publisher · View at Google Scholar · View at Scopus
  67. O. Duicu, C. Juşcă, L. Falniţă et al., “Substrate-specific impairment of mitochondrial respiration in permeabilized fibers from patients with coronary heart disease versus valvular disease,” Molecular and Cellular Biochemistry, vol. 379, no. 1-2, pp. 229–234, 2013. View at Publisher · View at Google Scholar · View at Scopus
  68. A. M. Cordero-Reyes, A. A. Gupte, K. A. Youker et al., “Freshly isolated mitochondria from failing human hearts exhibit preserved respiratory function,” Journal of Molecular and Cellular Cardiology, vol. 68, pp. 98–105, 2014. View at Publisher · View at Google Scholar · View at Scopus
  69. S. Boudina and E. D. Abel, “Diabetic cardiomyopathy, causes and effects,” Reviews in Endocrine and Metabolic Disorders, vol. 11, no. 1, pp. 31–39, 2010. View at Publisher · View at Google Scholar · View at Scopus
  70. R. Harmancey and H. Taegtmeyer, “The complexities of diabetic cardiomyopathy: lessons from patients and animal models,” Current Diabetes Reports, vol. 8, no. 3, pp. 243–248, 2008. View at Publisher · View at Google Scholar · View at Scopus
  71. H. Bugger and E. D. Abel, “Mitochondria in the diabetic heart,” Cardiovascular Research, vol. 88, no. 2, pp. 229–240, 2010. View at Publisher · View at Google Scholar · View at Scopus
  72. R. Blake and I. A. Trounce, “Mitochondrial dysfunction and complications associated with diabetes,” Biochimica et Biophysica Acta, vol. 1840, no. 4, pp. 1404–1412, 2014. View at Publisher · View at Google Scholar
  73. S. D. Martin and S. L. McGee, “The role of mitochondria in the aetiology of insulin resistance and type 2 diabetes,” Biochimica et Biophysica Acta, vol. 1840, no. 4, pp. 1303–1312, 2014. View at Google Scholar
  74. O. Lorenzo, E. Ramírez, B. Picatoste, J. Egido, and J. Tuñón, “Alteration of energy substrates and ROS production in diabetic cardiomyopathy,” Mediators of Inflammation, vol. 2013, Article ID 461967, 11 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  75. C. E. Flarsheim, I. L. Grupp, and M. A. Matlib, “Mitochondrial dysfunction accompanies diastolic dysfunction in diabetic rat heart,” The American Journal of Physiology—Heart and Circulatory Physiology, vol. 271, no. 1, pp. H192–H202, 1996. View at Google Scholar · View at Scopus
  76. O. M. Lashin, P. A. Szweda, L. I. Szweda, and A. M. P. Romani, “Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart,” Free Radical Biology and Medicine, vol. 40, no. 5, pp. 886–896, 2006. View at Publisher · View at Google Scholar · View at Scopus
  77. H. Bugger and E. D. Abel, “Rodent models of diabetic cardiomyopathy,” Disease Models and Mechanisms, vol. 2, no. 9-10, pp. 454–466, 2009. View at Publisher · View at Google Scholar · View at Scopus
  78. G. N. Pierce and N. S. Dhalla, “Heart mitochondrial function in chronic experimental diabetes in rats,” Canadian Journal of Cardiology, vol. 1, no. 1, pp. 48–54, 1985. View at Google Scholar · View at Scopus
  79. Y. Tanaka, N. Konno, and K. J. Kako, “Mitochondrial dysfunction observed in situ in cardiomyocytes of rats in experimental diabetes,” Cardiovascular Research, vol. 26, no. 4, pp. 409–414, 1992. View at Publisher · View at Google Scholar · View at Scopus
  80. T. H. Kuo, K. H. Moore, F. Giacomelli, and J. Wiener, “Defective oxidative metabolism of heart mitochondria from genetially diabetic mice,” Diabetes, vol. 32, no. 9, pp. 781–787, 1983. View at Publisher · View at Google Scholar · View at Scopus
  81. S. Boudina, S. Sena, B. T. O'Neill, P. Tathireddy, M. E. Young, and E. D. Abel, “Reduced mitochondrial oxidative capacity and increased mitochondrial uncoupling impair myocardial energetics in obesity,” Circulation, vol. 112, no. 17, pp. 2686–2695, 2005. View at Publisher · View at Google Scholar · View at Scopus
  82. S. Boudina and E. D. Abel, “Mitochondrial uncoupling: a key contributor to reduced cardiac efficiency in diabetes,” Physiology, vol. 21, no. 4, pp. 250–258, 2006. View at Publisher · View at Google Scholar · View at Scopus
  83. E. R. Dabkowski, C. L. Williamson, V. C. Bukowski et al., “Diabetic cardiomyopathy-associated dysfunction in spatially distinct mitochondrial subpopulations,” The American Journal of Physiology—Heart and Circulatory Physiology, vol. 296, no. 2, pp. H359–H369, 2009. View at Publisher · View at Google Scholar · View at Scopus
  84. E. J. Anderson, A. P. Kypson, E. Rodriguez, C. A. Anderson, E. J. Lehr, and P. D. Neufer, “Substrate-specific derangements in mitochondrial metabolism and redox balance in the atrium of the type 2 diabetic human heart,” Journal of the American College of Cardiology, vol. 54, no. 20, pp. 1891–1898, 2009. View at Publisher · View at Google Scholar · View at Scopus
  85. E. J. Anderson, E. Rodriguez, C. A. Anderson, K. Thayne, W. R. Chitwood, and A. P. Kypson, “Increased propensity for cell death in diabetic human heart is mediated by mitochondrial-dependent pathways,” American Journal of Physiology: Heart and Circulatory Physiology, vol. 300, no. 1, pp. H118–H124, 2011. View at Publisher · View at Google Scholar · View at Scopus
  86. T. L. Croston, D. Thapa, A. A. Holden et al., “Functional deficiencies of subsarcolemmal mitochondria in the type 2 diabetic human heart,” American Journal of Physiology. Heart and Circulatory Physiology, vol. 307, no. 1, pp. H54–H65, 2014. View at Publisher · View at Google Scholar
  87. D. Montaigne, X. Marechal, A. Coisne et al., “Myocardial contractile dysfunction is associated with impaired mitochondrial function and dynamics in type 2 diabetic but not in obese patients,” Circulation, 2014. View at Publisher · View at Google Scholar
  88. M. P. Stern, “Diabetes and cardiovascular disease: the “common soil” hypothesis,” Diabetes, vol. 44, no. 4, pp. 369–374, 1995. View at Google Scholar · View at Scopus
  89. M. B. H. Youdim and J. P. M. Finberg, “New directions in monoamine oxidase A and B: selective inhibitors and substrates,” Biochemical Pharmacology, vol. 41, no. 2, pp. 155–162, 1991. View at Publisher · View at Google Scholar · View at Scopus
  90. M. Bortolato, K. Chen, and J. C. Shih, “Monoamine oxidase inactivation: from pathophysiology to therapeutics,” Advanced Drug Delivery Reviews, vol. 60, no. 13-14, pp. 1527–1533, 2008. View at Publisher · View at Google Scholar · View at Scopus
  91. P. Bianchi, O. Kunduzova, E. Masini et al., “Oxidative stress by monoamine oxidase mediates receptor-independent cardiomyocyte apoptosis by serotonin and postischemic myocardial injury,” Circulation, vol. 112, no. 21, pp. 3297–3305, 2005. View at Publisher · View at Google Scholar · View at Scopus
  92. N. Kaludercic, E. Takimoto, T. Nagayama et al., “Monoamine oxidase A-mediated enhanced catabolism of norepinephrine contributes to adverse remodeling and pump failure in hearts with pressure overload,” Circulation Research, vol. 106, no. 1, pp. 193–202, 2010. View at Publisher · View at Google Scholar · View at Scopus
  93. N. Kaludercic, A. Carpi, T. Nagayama et al., “Monoamine oxidase B prompts mitochondrial and cardiac dysfunction in pressure overloaded hearts,” Antioxidants and Redox Signaling, vol. 20, no. 2, pp. 267–280, 2014. View at Publisher · View at Google Scholar · View at Scopus
  94. M. E. Manni, M. Zazzeri, C. Musilli, E. Bigagli, M. Lodovici, and L. Raimondi, “Exposure of cardiomyocytes to angiotensin II induces over-activation of monoamine oxidase type A: implications in heart failure,” European Journal of Pharmacology, vol. 718, no. 1–3, pp. 271–276, 2013. View at Publisher · View at Google Scholar · View at Scopus
  95. O. Duicu, A. Sturza, L. Noveanu et al., “Mitochondria and endothelial dysfunction: a glimpse of monoamine oxidases,” Experimental & Clinical Cardiology, supplement A, pp. 52A–56A, 2013. View at Google Scholar
  96. A. Sturza, O. Duicu, and L. Noveanu, “Monoamine oxidase inhibition corrects endothelial dysfunction in experimental diabetes,” Cardiovascular Research, vol. 2014, no. 103, p. P172, 2014. View at Google Scholar
  97. E. J. Anderson, J. T. Efird, S. W. Davies et al., “Monoamine oxidase is a major determinant of redox balance in human atrial myocardium and is associated with postoperative atrial fibrillation,” Journal of the American Heart Association, vol. 3, no. 1, Article ID e000713, 2014. View at Publisher · View at Google Scholar · View at Scopus
  98. E. Braunwald, “Shattuck lecture cardiovascular medicine at the turn of the millennium: triumphs, concerns, and opportunities,” The New England Journal of Medicine, vol. 337, no. 19, pp. 1360–1369, 1997. View at Publisher · View at Google Scholar · View at Scopus
  99. R. P. Juni, H. J. Duckers, P. M. Vanhoutte, R. Virmani, and A. L. Moens, “Oxidative stress and pathological changes after coronary artery interventions,” Journal of the American College of Cardiology, vol. 61, no. 14, pp. 1471–1481, 2013. View at Publisher · View at Google Scholar · View at Scopus