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Oxidative Medicine and Cellular Longevity
Volume 2015, Article ID 424751, 14 pages
http://dx.doi.org/10.1155/2015/424751
Research Article

Oxidative Stress in Dilated Cardiomyopathy Caused by MYBPC3 Mutation

1Department of Cell and Molecular Physiology, Health Sciences Division, Loyola University Chicago, Maywood, IL 60153, USA
2Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA
3Department of Cardiothoracic Surgery, University of Pittsburgh Medical Center, McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, PA 15219, USA
4Department of Cardiology, Thoraxcenter, Erasmus Medical Center, ’s-Gravendijkwal 230, 3015 CE Rotterdam, Netherlands
5Bosch Institute, Discipline of Anatomy and Histology, University of Sydney, Sydney, NSW 2006, Australia
6Laboratory for Physiology, Institute for Cardiovascular Research, VU University Medical Center, van der Boechorststraat 7, 1081 BT Amsterdam, Netherlands

Received 15 January 2015; Revised 1 July 2015; Accepted 9 August 2015

Academic Editor: Felipe Dal Pizzol

Copyright © 2015 Thomas L. Lynch IV 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, and 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. S. Morimoto, “Sarcomeric proteins and inherited cardiomyopathies,” Cardiovascular Research, vol. 77, no. 4, pp. 659–666, 2008. View at Publisher · View at Google Scholar · View at Scopus
  3. B. J. Maron and M. S. Maron, “Hypertrophic cardiomyopathy,” The Lancet, vol. 381, no. 9862, pp. 242–255, 2013. View at Publisher · View at Google Scholar · View at Scopus
  4. S. J. van Dijk, D. Dooijes, C. dos Remedios et al., “Cardiac myosin-binding protein C mutations and hypertrophic cardiomyopathy: haploinsufficiency, deranged phosphorylation, and cardiomyocyte dysfunction,” Circulation, vol. 119, no. 11, pp. 1473–1483, 2009. View at Publisher · View at Google Scholar · View at Scopus
  5. S. Marston, O. Copeland, K. Gehmlich, S. Schlossarek, and L. Carrrier, “How do MYBPC3 mutations cause hypertrophic cardiomyopathy?” Journal of Muscle Research and Cell Motility, vol. 33, no. 1, pp. 75–80, 2012. View at Publisher · View at Google Scholar · View at Scopus
  6. E. M. McNally, J. R. Golbus, and M. J. Puckelwartz, “Genetic mutations and mechanisms in dilated cardiomyopathy,” Journal of Clinical Investigation, vol. 123, no. 1, pp. 19–26, 2013. View at Publisher · View at Google Scholar · View at Scopus
  7. R. Lombardi, A. Bell, V. Senthil et al., “Differential interactions of thin filament proteins in two cardiac troponin T mouse models of hypertrophic and dilated cardiomyopathies,” Cardiovascular Research, vol. 79, no. 1, pp. 109–117, 2008. View at Publisher · View at Google Scholar · View at Scopus
  8. A. J. Marian, V. Senthil, S. N. Chen, and R. Lombardi, “Antifibrotic effects of antioxidant N-acetylcysteine in a mouse model of human hypertrophic cardiomyopathy mutation,” Journal of the American College of Cardiology, vol. 47, no. 4, pp. 827–834, 2006. View at Publisher · View at Google Scholar · View at Scopus
  9. R. Lombardi, G. Rodriguez, S. N. Chen et al., “Resolution of established cardiac hypertrophy and fibrosis and prevention of systolic dysfunction in a transgenic rabbit model of human cardiomyopathy through thiol-sensitive mechanisms,” Circulation, vol. 119, no. 10, pp. 1398–1407, 2009. View at Publisher · View at Google Scholar · View at Scopus
  10. D. Lu, Y. Ma, W. Zhang et al., “Knockdown of cytochrome P450 2E1 inhibits oxidative stress and apoptosis in the cTnTR141W dilated cardiomyopathy transgenic mice,” Hypertension, vol. 60, no. 1, pp. 81–89, 2012. View at Publisher · View at Google Scholar
  11. B. K. McConnell, K. A. Jones, D. Fatkin et al., “Dilated cardiomyopathy in homozygous myosin-binding protein-C mutant mice,” Journal of Clinical Investigation, vol. 104, no. 9, pp. 1235–1244, 1999. View at Publisher · View at Google Scholar · View at Scopus
  12. D. Barefield, M. Kumar, P. P. de Tombe, and S. Sadayappan, “Contractile dysfunction in a mouse model expressing a heterozygous MYBPC3 mutation associated with hypertrophic cardiomyopathy,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 306, no. 6, pp. H807–H815, 2014. View at Publisher · View at Google Scholar · View at Scopus
  13. B. K. McConnell, D. Fatkin, C. Semsarian et al., “Comparison of two murine models of familial hypertrophic cardiomyopathy,” Circulation Research, vol. 88, no. 4, pp. 383–389, 2001. View at Publisher · View at Google Scholar · View at Scopus
  14. B. M. Palmer, D. Georgakopoulos, P. M. Janssen et al., “Role of cardiac myosin binding protein C in sustaining left ventricular systolic stiffening,” Circulation Research, vol. 94, no. 9, pp. 1249–1255, 2004. View at Publisher · View at Google Scholar · View at Scopus
  15. J. B. Owen and D. A. Butterfield, “Measurement of oxidized/reduced glutathione ratio.,” Methods in Molecular Biology, vol. 648, pp. 269–277, 2010. View at Publisher · View at Google Scholar · View at Scopus
  16. O. Zitka, S. Skalickova, J. Gumulec et al., “Redox status expressed as GSH:GSSG ratio as a marker for oxidative stress in paediatric tumour patients,” Oncology Letters, vol. 4, no. 6, pp. 1247–1253, 2012. View at Publisher · View at Google Scholar · View at Scopus
  17. I. Dalle-Donne, R. Rossi, D. Giustarini, A. Milzani, and R. Colombo, “Protein carbonyl groups as biomarkers of oxidative stress,” Clinica Chimica Acta, vol. 329, no. 1-2, pp. 23–38, 2003. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Luo and N. B. Wehr, “Protein carbonylation: avoiding pitfalls in the 2,4-dinitrophenylhydrazine assay,” Redox Report, vol. 14, no. 4, pp. 159–166, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. H. Esterbauer, R. J. Schaur, and H. Zollner, “Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes,” Free Radical Biology and Medicine, vol. 11, no. 1, pp. 81–128, 1991. View at Publisher · View at Google Scholar · View at Scopus
  20. Y. Riahi, G. Cohen, O. Shamni, and S. Sasson, “Signaling and cytotoxic functions of 4-hydroxyalkenals,” American Journal of Physiology—Endocrinology and Metabolism, vol. 299, no. 6, pp. E879–E886, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. Y. Nishijima, A. Sridhar, I. Bonilla et al., “Tetrahydrobiopterin depletion and NOS2 uncoupling contribute to heart failure-induced alterations in atrial electrophysiology,” Cardiovascular Research, vol. 91, no. 1, pp. 71–79, 2011. View at Publisher · View at Google Scholar · View at Scopus
  22. S. I. Dikalov, I. A. Kirilyuk, M. Voinov, and I. A. Grigor'Ev, “EPR detection of cellular and mitochondrial superoxide using cyclic hydroxylamines,” Free Radical Research, vol. 45, no. 4, pp. 417–430, 2011. View at Publisher · View at Google Scholar · View at Scopus
  23. S. V. Plotnikov, A. C. Millard, P. J. Campagnola, and W. A. Mohler, “Characterization of the myosin-based source for second-harmonic generation from muscle sarcomeres,” Biophysical Journal, vol. 90, no. 2, pp. 693–703, 2006. View at Publisher · View at Google Scholar · View at Scopus
  24. M. Sivaguru, S. Durgam, R. Ambekar et al., “Quantitative analysis of collagen fiber organization in injured tendons using Fourier transform-second harmonic generation imaging,” Optics Express, vol. 18, no. 24, pp. 24983–24993, 2010. View at Publisher · View at Google Scholar · View at Scopus
  25. M. Sivaguru, J. P. Eichorst, S. Durgam, G. A. Fried, A. A. Stewart, and M. C. Stewart, “Imaging horse tendons using multimodal 2-photon microscopy,” Methods, vol. 66, no. 2, pp. 256–267, 2014. View at Publisher · View at Google Scholar · View at Scopus
  26. J. Schindelin, I. Arganda-Carreras, E. Frise et al., “Fiji: an open-source platform for biological-image analysis,” Nature Methods, vol. 9, no. 7, pp. 676–682, 2012. View at Publisher · View at Google Scholar · View at Scopus
  27. P. P. Dimitrow, A. Undas, P. Wołkow, W. Tracz, and J. S. Dubiel, “Enhanced oxidative stress in hypertrophic cardiomyopathy,” Pharmacological Reports, vol. 61, no. 3, pp. 491–495, 2009. View at Publisher · View at Google Scholar · View at Scopus
  28. D. Romero-Alvira, E. Roche, and L. Placer, “Cardiomyopathies and oxidative stress,” Medical Hypotheses, vol. 47, no. 2, pp. 137–144, 1996. View at Publisher · View at Google Scholar · View at Scopus
  29. B. Halliwell, “Oxidative stress, nutrition and health. experimental strategies for optimization of nutritional antioxidant intake in humans,” Free Radical Research, vol. 25, no. 1, pp. 57–74, 1996. View at Publisher · View at Google Scholar · View at Scopus
  30. B. Halliwell and S. Chirico, “Lipid peroxidation: its mechanism, measurement, and significance,” The American Journal of Clinical Nutrition, vol. 57, pp. 715S–725S, 1993. View at Google Scholar
  31. M. Elas, J. Bielanska, K. Pustelny et al., “Detection of mitochondrial dysfunction by EPR technique in mouse model of dilated cardiomyopathy,” Free Radical Biology and Medicine, vol. 45, no. 3, pp. 321–328, 2008. View at Publisher · View at Google Scholar · View at Scopus
  32. B. K. McConnell, K. A. Jones, D. Fatkin et al., “Dilated cardiomyopathy in homozygous myosin-binding protein-C mutant mice,” Journal of Clinical Investigation, vol. 104, article 1771, 1999. View at Publisher · View at Google Scholar · View at Scopus
  33. S. V. Plotnikov, A. M. Kenny, S. J. Walsh et al., “Measurement of muscle disease by quantitative second-harmonic generation imaging,” Journal of Biomedical Optics, vol. 13, no. 4, Article ID 044018, 2008. View at Publisher · View at Google Scholar · View at Scopus
  34. D. Roude, G. Recher, J.-J. Bellanger, M.-T. Lavault, E. Schaub, and F. Tiaho, “Modeling of supramolecular centrosymmetry effect on sarcomeric SHG intensity pattern of skeletal muscles,” Biophysical Journal, vol. 101, no. 2, pp. 494–503, 2011. View at Publisher · View at Google Scholar · View at Scopus
  35. G. Recher, D. Rouède, E. Schaub, and F. Tiaho, “Skeletal muscle sarcomeric SHG patterns photo-conversion by femtosecond infrared laser,” Biomedical Optics Express, vol. 2, no. 2, pp. 374–384, 2011. View at Publisher · View at Google Scholar · View at Scopus
  36. R. S. Whelan, V. Kaplinskiy, and R. N. Kitsis, “Cell death in the pathogenesis of heart disease: mechanisms and significance,” Annual Review of Physiology, vol. 72, pp. 19–44, 2009. View at Publisher · View at Google Scholar · View at Scopus
  37. A. González, S. Ravassa, J. Beaumont, B. López, and J. Díez, “New targets to treat the structural remodeling of the myocardium,” Journal of the American College of Cardiology, vol. 58, no. 18, pp. 1833–1843, 2011. View at Publisher · View at Google Scholar · View at Scopus
  38. D. Jarreta, J. Orús, A. Barrientos et al., “Mitochondrial function in heart muscle from patients with idiopathic dilated cardiomyopathy,” Cardiovascular Research, vol. 45, no. 4, pp. 860–865, 2000. View at Publisher · View at Google Scholar · View at Scopus
  39. M. R. Duchen, “Roles of mitochondria in health and disease,” Diabetes, vol. 53, supplement 1, pp. S96–S102, 2004. View at Publisher · View at Google Scholar · View at Scopus
  40. 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
  41. D. Yücel, S. Aydoğdu, S. Çehreli et al., “Increased oxidative stress in dilated cardiomyopathic heart failure,” Clinical Chemistry, vol. 44, no. 1, pp. 148–154, 1998. View at Google Scholar · View at Scopus
  42. D. J. Betteridge, “What is oxidative stress?” Metabolism, vol. 49, no. 2, pp. 3–8, 2000. View at Google Scholar · View at Scopus
  43. J. Nordberg and E. S. J. Arnér, “Reactive oxygen species, antioxidants, and the mammalian thioredoxin system,” Free Radical Biology and Medicine, vol. 31, no. 11, pp. 1287–1312, 2001. View at Publisher · View at Google Scholar · View at Scopus
  44. Å. B. Gustafsson and R. A. Gottlieb, “Heart mitochondria: gates of life and death,” Cardiovascular Research, vol. 77, no. 2, pp. 334–343, 2008. View at Publisher · View at Google Scholar · View at Scopus
  45. G. Poli and M. Parola, “Oxidative damage and fibrogenesis,” Free Radical Biology and Medicine, vol. 22, no. 1-2, pp. 287–305, 1997. View at Publisher · View at Google Scholar · View at Scopus
  46. 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
  47. 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
  48. C. Chen and B. H. Paw, “Cellular and mitochondrial iron homeostasis in vertebrates,” Biochimica et Biophysica Acta, vol. 1823, no. 9, pp. 1459–1467, 2012. View at Publisher · View at Google Scholar · View at Scopus
  49. F. Foury and D. Talibi, “Mitochondrial control of iron homeostasis. A genome wide analysis of gene expression in a yeast frataxin-deficient strain,” Journal of Biological Chemistry, vol. 276, no. 11, pp. 7762–7768, 2001. View at Publisher · View at Google Scholar · View at Scopus