Table of Contents Author Guidelines Submit a Manuscript
Oxidative Medicine and Cellular Longevity
Volume 2014, Article ID 541230, 27 pages
http://dx.doi.org/10.1155/2014/541230
Review Article

Oxidative Stress and Mitochondrial Dysfunction across Broad-Ranging Pathologies: Toward Mitochondria-Targeted Clinical Strategies

1Cancer Research Centre at Mercogliano (CROM), Istituto Nazionale Tumori Fondazione G. Pascale-IRCCS, 80131 Naples, Italy
2Research Laboratory, Dental School, Sevilla University, 41009 Sevilla, Spain
3Department of Chemical Sciences, Federico II University, 80126 Naples, Italy
4National Research Council, Institute of Biomembranes and Bioenergetics, 70126 Bari, Italy
5CIBERER, University of Valencia-INCLIVA, 46010 Valencia, Spain
6“Vinca” Institute of Nuclear Sciences, University of Belgrade, 11070 Belgrade, Serbia
7Department of Clinical and Dental Sciences, Polytechnical University of Marche, 60100 Ancona, Italy
8Department of Genetics, ASL Napoli 1, 80136 Naples, Italy

Received 13 December 2013; Accepted 24 February 2014; Published 4 May 2014

Academic Editor: Cinzia Signorini

Copyright © 2014 Giovanni Pagano 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. E. Vitols and A. W. Linnane, “Studies on the oxidative metabolism of Saccharomyces cerevisiae. II. Morphology and oxidative phosphorylation capacity of mitochondria and derived particles from baker's yeast,” The Journal of Biophysical and Biochemical Cytology, vol. 9, pp. 701–710, 1961. View at Google Scholar · View at Scopus
  2. D. Bellamy, “The endogenous citric acid-cycle intermediates and amino acids of,” The Biochemical Journal, vol. 82, pp. 218–224, 1962. View at Google Scholar · View at Scopus
  3. C. Richter and G. E. N. Kass, “Oxidative stress in mitochondria: its relationship to cellular Ca2+ homeostasis, cell death, proliferation and differentiation,” Chemico-Biological Interactions, vol. 77, no. 1, pp. 1–23, 1991. View at Publisher · View at Google Scholar · View at Scopus
  4. R. S. Sohal and U. T. Brunk, “Mitochondrial production of pro-oxidants and cellular senescence,” Mutation Research—DNAging Genetic Instability and Aging, vol. 275, no. 3–6, pp. 295–304, 1992. View at Publisher · View at Google Scholar · View at Scopus
  5. G. Piccolo, P. Banfi, G. Azan et al., “Biological markers of oxidative stress in mitochondrial myopathies with progressive external ophthalmoplegia,” The Journal of the Neurological Sciences, vol. 105, no. 1, pp. 57–60, 1991. View at Publisher · View at Google Scholar · View at Scopus
  6. D. A. Di Monte, P. Chan, and M. S. Sandy, “Glutathione in Parkinson's disease: a link between oxidative stress and mitochondrial damage?” Annals of Neurology, vol. 32, supplement, pp. S111–S115, 1992. View at Google Scholar · View at Scopus
  7. P. F. Chinnery, “Mitochondrial disorders overview. Synonyms: mitochondrial encephalomyopathies, mitochondrial myopathies, oxidative phosphorylation disorders, respiratory chain disorders,” in GeneReviews, R. A. Pagon, T. D. Bird, C. R. Dolan et al., Eds., pp. 1993–2013, University of Washington, Seattle, Wash, USA, 2010, http://www.ncbi.nlm.nih.gov/books/NBK1116/. View at Google Scholar
  8. E. A. Schon, S. di Mauro, and M. Hirano, “Human mitochondrial DNA: roles of inherited and somatic mutations,” Nature Reviews Genetics, vol. 13, no. 12, pp. 878–890, 2012. View at Google Scholar
  9. V. Carelli, C. La Morgia, M. L. Valentino et al., “Idebenone treatment in Leber's hereditary optic neuropathy,” Brain, vol. 134, part 9, p. e188, 2011. View at Google Scholar · View at Scopus
  10. M. Kumar, P. Kaur, M. Kumar et al., “Clinical characterization and mitochondrial DNA sequence variations in Leber hereditary optic neuropathy,” Molecular Vision, vol. 18, pp. 2687–2699, 2012. View at Google Scholar
  11. A. A. Sadun, C. F. Chicani, F. N. Ross-Cisneros et al., “Effect of EPI-743 on the clinical course of the mitochondrial disease leber hereditary optic neuropathy,” Archives of Neurology, vol. 69, no. 3, pp. 331–338, 2012. View at Publisher · View at Google Scholar · View at Scopus
  12. D. Martinelli, M. Catteruccia, F. Piemonte et al., “EPI-743 reverses the progression of the pediatric mitochondrial disease—genetically defined Leigh Syndrome,” Molecular Genetics and Metabolism, vol. 107, no. 3, pp. 383–388, 2012. View at Google Scholar
  13. M. Lebiedzinska, A. Karkucinska-Wieckowska, A. Wojtala et al., “Disrupted ATP synthase activity and mitochondrial hyperpolarisation-dependent oxidative stress is associated with p66Shc phosphorylation in fibroblasts of NARP patients,” International Journal of Biochemistry and Cell Biology, vol. 45, no. 1, pp. 141–150, 2013. View at Google Scholar
  14. M. Mattiazzi, C. Vijayvergiya, C. D. Gajewski et al., “The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants,” Human Molecular Genetics, vol. 13, no. 8, pp. 869–879, 2004. View at Publisher · View at Google Scholar · View at Scopus
  15. Y. Ihara, M. Kibata, T. Hayabara et al., “Free radicals in the cerebrospinal fluid are associated with neurological disorders including mitochondrial encephalomyopathy,” Biochemistry and Molecular Biology International, vol. 42, no. 5, pp. 937–947, 1997. View at Google Scholar · View at Scopus
  16. G. Vattemi, Y. Mechref, M. Marini et al., “Increased protein nitration in mitochondrial diseases: evidence for vessel wall involvement,” Molecular and Cellular Proteomics, vol. 10, no. 4, Article ID M110.002964, 2011. View at Publisher · View at Google Scholar · View at Scopus
  17. T. M. M. Tan, C. Caputo, F. Medici et al., “MELAS syndrome, diabetes and thyroid disease: the role of mitochondrial oxidative stress,” Clinical Endocrinology, vol. 70, no. 2, pp. 340–341, 2009. View at Publisher · View at Google Scholar · View at Scopus
  18. D. Cotán, M. D. Cordero, J. Garrido-Maraver et al., “Secondary coenzyme Q(10) deficiency triggers mitochondria degradation by mitophagy in MELAS fibroblasts,” The FASEB Journal, vol. 25, no. 8, pp. 2669–2687, 2011. View at Publisher · View at Google Scholar · View at Scopus
  19. Y. Katayama, K. Maeda, T. Iizuka et al., “Accumulation of oxidative stress around the stroke-like lesions of MELAS patients,” Mitochondrion, vol. 9, no. 5, pp. 306–313, 2009. View at Publisher · View at Google Scholar · View at Scopus
  20. Y. Ma, Y. Chen, C. Lu, C. Liu, and Y. Wei, “Upregulation of matrix metalloproteinase 1 and disruption of mitochondrial network in skin fibroblasts of patients with MERRF syndrome,” Annals of the New York Academy of Sciences, vol. 1042, pp. 55–63, 2005. View at Publisher · View at Google Scholar · View at Scopus
  21. S. Wu, Y. Ma, Y. Wu, Y. Chen, and Y. Wei, “Mitochondrial DNA mutation-elicited oxidative stress, oxidative damage, and altered gene expression in cultured cells of patients with MERRF syndrome,” Molecular Neurobiology, vol. 41, no. 2-3, pp. 256–266, 2010. View at Publisher · View at Google Scholar · View at Scopus
  22. J. E. Salles, V. A. Moisés, D. R. Almeida, A. R. Chacra, and R. S. Moisés, “Myocardial dysfunction in mitochondrial diabetes treated with Coenzyme Q10,” Diabetes Research and Clinical Practice, vol. 72, no. 1, pp. 100–103, 2006. View at Publisher · View at Google Scholar · View at Scopus
  23. N. Z. Lax, G. R. Campbell, A. K. Reeve et al., “Loss of myelin-associated glycoprotein in kearns-sayre syndrome,” Archives of Neurology, vol. 69, no. 4, pp. 490–499, 2012. View at Publisher · View at Google Scholar · View at Scopus
  24. M. Mancuso, D. Orsucci, V. Calsolaro et al., “Tetracycline treatment in patients with progressive external ophthalmoplegia,” Acta Neurologica Scandinavica, vol. 124, no. 6, pp. 417–423, 2011. View at Publisher · View at Google Scholar · View at Scopus
  25. J. Wolf, B. Obermaier-Kusser, M. Jacobs et al., “A new mitochondrial point mutation in the transfer RNALys gene associated with progressive external ophthalmoplegia with impaired respiratory regulation,” The Journal of the Neurological Sciences, vol. 316, no. 1-2, pp. 108–111, 2012. View at Publisher · View at Google Scholar · View at Scopus
  26. E. M. Manea, G. Leverger, F. Bellmann et al., “Pearson syndrome in the neonatal period: two case reports and review of the literature,” Journal of Pediatric Hematology/Oncology, vol. 31, no. 12, pp. 947–951, 2009. View at Publisher · View at Google Scholar · View at Scopus
  27. K. Kefala-Agoropoulou, E. Roilides, A. Lazaridou et al., “Pearson syndrome in an infant heterozygous for C282Y allele of HFE gene,” Hematology, vol. 12, no. 6, pp. 549–553, 2007. View at Publisher · View at Google Scholar · View at Scopus
  28. J. Uusimaa, S. Finnilä, L. Vainionpää et al., “A mutation in mitochondrial DNA-encoded cytochrome c oxidase II gene in a child with Alpers-Huttenlocher-like disease,” Pediatrics, vol. 111, no. 3, pp. e262–e268, 2003. View at Google Scholar · View at Scopus
  29. M. C. de Vries, R. J. Rodenburg, E. Morava et al., “Multiple oxidative phosphorylation deficiencies in severe childhood multi-system disorders due to polymerase gamma (POLG1) mutations,” European Journal of Pediatrics, vol. 166, no. 3, pp. 229–234, 2007. View at Publisher · View at Google Scholar · View at Scopus
  30. W. Lewis, B. J. Day, J. J. Kohler et al., “Decreased mtDNA, oxidative stress, cardiomyopathy, and death from transgenic cardiac targeted human mutant polymerase γ,” Laboratory Investigation, vol. 87, no. 4, pp. 326–335, 2007. View at Publisher · View at Google Scholar · View at Scopus
  31. R. P. Saneto, B. H. Cohen, W. C. Copeland et al., “Alpers-Huttenlocher Syndrome,” Pediatric Neurology, vol. 48, no. 3, pp. 167–178, 2013. View at Google Scholar
  32. M. Hirano, C. Garone, and C. M. Quinzii, “CoQ10 deficiencies and MNGIE: two treatable mitochondrial disorders,” Biochimica et Biophysica Acta—General Subjects, vol. 1820, no. 5, pp. 625–631, 2012. View at Publisher · View at Google Scholar · View at Scopus
  33. A. W. El-Hattab and F. Scaglia, “Mitochondrial DNA depletion syndromes: review and updates of genetic basis, manifestations, and therapeutic options,” Neurotherapeutics, vol. 10, no. 2, pp. 186–198, 2013. View at Google Scholar
  34. S. DiMauro, E. A. Schon, V. Carelli et al., “The clinical maze of mitochondrial neurology,” Nature Reviews Neurology, vol. 9, pp. 429–444, 2013. View at Google Scholar
  35. A. Barzilai, G. Rotman, and Y. Shiloh, “ATM deficiency and oxidative stress: a new dimension of defective response to DNA damage,” DNA Repair, vol. 1, no. 1, pp. 3–25, 2002. View at Publisher · View at Google Scholar · View at Scopus
  36. M. Ambrose, J. V. Goldstine, and R. A. Gatti, “Intrinsic mitochondrial dysfunction in ATM-deficient lymphoblastoid cells,” Human Molecular Genetics, vol. 16, no. 18, pp. 2154–2164, 2007. View at Publisher · View at Google Scholar · View at Scopus
  37. P. Degan, M. d'Ischia, F. V. Pallardó et al., “Glutathione levels in blood from ataxia telangiectasia patients suggest in vivo adaptive mechanisms to oxidative stress,” Clinical Biochemistry, vol. 40, no. 9-10, pp. 666–670, 2007. View at Publisher · View at Google Scholar · View at Scopus
  38. Y. A. Valentin-Vega, K. H. MacLean, J. Tait-Mulder et al., “Mitochondrial dysfunction in ataxia-telangiectasia,” Blood, vol. 119, no. 6, pp. 1490–1500, 2012. View at Publisher · View at Google Scholar · View at Scopus
  39. Y. Shiloh, E. Tabor, and Y. Becker, “Abnormal response of ataxia-telangiectasia cells to agents that break the deoxyribose moiety of DNA via a targeted free radical mechanism,” Carcinogenesis, vol. 4, no. 10, pp. 1317–1322, 1983. View at Google Scholar · View at Scopus
  40. M. Poot, H. Hoehn, T. M. Nicotera, and H. W. Rudiger, “Cell kinetic evidence suggests elevated oxidative stress in cultured cells of Bloom's syndrome,” Free Radical Research Communications, vol. 7, no. 3–6, pp. 179–187, 1989. View at Google Scholar · View at Scopus
  41. T. M. Nicotera, “Molecular and biochemical aspects of Bloom's syndrome,” Cancer Genetics and Cytogenetics, vol. 53, no. 1, pp. 1–13, 1991. View at Publisher · View at Google Scholar · View at Scopus
  42. A. Zatterale, F. J. Kelly, P. Degan et al., “Oxidative stress biomarkers in four Bloom syndrome (BS) patients and in their parents suggest in vivo redox abnormalities in BS phenotype,” Clinical Biochemistry, vol. 40, no. 15, pp. 1100–1110, 2007. View at Google Scholar · View at Scopus
  43. A. Javeri, J. Guy Lyons, X. X. Huang, and G. M. Halliday, “Downregulation of Cockayne syndrome B protein reduces human 8-oxoguanine DNA glycosylase-1 expression and repair of UV radiation-induced 8-oxo-7,8-dihydro-2′-deoxyguanine,” Cancer Science, vol. 102, no. 9, pp. 1651–1658, 2011. View at Publisher · View at Google Scholar · View at Scopus
  44. B. Pascucci, T. Lemma, E. Iorio et al., “An altered redox balance mediates the hypersensitivity of Cockayne syndrome primary fibroblasts to oxidative stress,” Aging Cell, vol. 11, no. 3, pp. 520–529, 2012. View at Publisher · View at Google Scholar · View at Scopus
  45. M. Scheibye-Knudsen, M. Ramamoorthy, P. Sykora et al., “Cockayne syndrome group B protein prevents the accumulation of damaged mitochondria by promoting mitochondrial autophagy,” The Journal of Experimental Medicine, vol. 209, no. 4, pp. 855–869, 2012. View at Google Scholar
  46. Y. Kamenisch and M. Berneburg, “Mitochondrial CSA and CSB: protein interactions and protection from ageing associated DNA mutations,” Mechanisms of Ageing and Development, vol. 134, no. 5-6, pp. 270–274, 2013. View at Google Scholar
  47. F. V. Pallardó, P. Degan, M. d’Ischia et al., “Higher age-related prooxidant state in young Down syndrome patients indicates accelerated aging,” Biogerontology, vol. 7, no. 4, pp. 211–220, 2006. View at Google Scholar
  48. L. Tiano, L. Padella, P. Carnevali et al., “Coenzyme Q(10) and oxidative imbalance in Down syndrome: biochemical and clinical aspects,” BioFactors, vol. 32, no. 1–4, pp. 161–167, 2008. View at Google Scholar · View at Scopus
  49. L. Tiano and J. Busciglio, “Mitochondrial dysfunction and Down's syndrome: is there a role for coenzyme Q(10)?” BioFactors, vol. 37, no. 5, pp. 386–392, 2011. View at Publisher · View at Google Scholar · View at Scopus
  50. D. Valenti, G. A. Manente, L. Moro, E. Marra, and R. A. Vacca, “Deficit of complex I activity in human skin fibroblasts with chromosome 21 trisomy and overproduction of reactive oxygen species by mitochondria: involvement of the cAMP/PKA signalling pathway,” Biochemical Journal, vol. 435, no. 3, pp. 679–688, 2011. View at Publisher · View at Google Scholar · View at Scopus
  51. D. Valenti, D. de Rasmo, A. Signorile et al., “Epigallocatechin-3-gallate prevents oxidative phosphorylation deficit and promotes mitochondrial biogenesis in human cells from subjects with Down's syndrome,” Biochimica et Biophysica Acta, vol. 1832, no. 4, pp. 542–552, 2013. View at Google Scholar
  52. L. L. Bambrick and G. Fiskum, “Mitochondrial dysfunction in mouse trisomy 16 brain,” Brain Research, vol. 1188, no. 1, pp. 9–16, 2008. View at Publisher · View at Google Scholar · View at Scopus
  53. B. W. Brooksbank and R. Balazs, “Superoxide dismutase, glutathione peroxidase and lipoperoxidation in Down's syndrome fetal brain,” Brain Research, vol. 318, no. 1, pp. 37–44, 1984. View at Google Scholar · View at Scopus
  54. H. Joenje, F. Arwert, and A. W. Eriksson, “Oxygen-dependence of chromosomal aberrations in Fanconi's anaemia,” Nature, vol. 290, no. 5802, pp. 142–143, 1981. View at Google Scholar · View at Scopus
  55. G. Pagano, A. Aiello Talamanca, G. Castello et al., “From clinical description to in vitro and animal studies, and backwards to patients: oxidative stress and mitochondrial dysfunction in Fanconi anemia,” Free Radical Biology and Medicine, vol. 58, pp. 118–125, 2013. View at Google Scholar
  56. W. Du, R. Rani, J. Sipple et al., “The FA pathway counteracts oxidative stress through selective protection of antioxidant defense gene promoters,” Blood, vol. 119, no. 18, pp. 4142–4151, 2012. View at Google Scholar
  57. S. S. Mukhopadhyay, K. S. Leung, M. J. Hicks, P. J. Hastings, H. Youssoufian, and S. E. Plon, “Defective mitochondrial peroxiredoxin-3 results in sensitivity to oxidative stress in Fanconi anemia,” The Journal of Cell Biology, vol. 175, no. 2, pp. 225–235, 2006. View at Publisher · View at Google Scholar · View at Scopus
  58. U. Kumari, W. Y. Jun, B. H. Bay et al., “Evidence of mitochondrial dysfunction and impaired ROS detoxifying machinery in Fanconi anemia cells,” Oncogene, vol. 33, no. 2, pp. 165–172, 2013. View at Publisher · View at Google Scholar
  59. S. Ravera, D. Vaccaro, P. Cuccarolo et al., “Mitochondrial respiratory chain Complex I defects in Fanconi anemia complementation group A,” Biochimie, vol. 95, no. 10, pp. 1828–1837, 2013. View at Google Scholar
  60. G. Pagano, A. Aiello Talamanca, G. Castello et al., “Bone marrow cell transcripts from Fanconi anaemia patients reveal in vivo alterations in mitochondrial, redox and DNA repair pathways,” European Journal of Haematology, vol. 91, no. 2, pp. 141–151, 2013. View at Google Scholar
  61. G. Viteri, Y. W. Chung, and E. R. Stadtman, “Effect of progerin on the accumulation of oxidized proteins in fibroblasts from Hutchinson Gilford progeria patients,” Mechanisms of Ageing and Development, vol. 131, no. 1, pp. 2–8, 2010. View at Publisher · View at Google Scholar · View at Scopus
  62. S. A. Richards, J. Muter, P. Ritchie, G. Lattanzi, and C. J. Hutchison, “The accumulation of un-repairable DNA damage in laminopathy progeria fibroblasts is caused by ROS generation and is prevented by treatment with N-acetyl cysteine,” Human Molecular Genetics, vol. 20, no. 20, pp. 3997–4004, 2011. View at Publisher · View at Google Scholar · View at Scopus
  63. V. Turinetto, P. Porcedda, V. Minieri et al., “A novel defect in mitochondrial p53 accumulation following DNA damage confers apoptosis resistance in Ataxia Telangiectasia and Nijmegen Breakage Syndrome T-cells,” DNA Repair, vol. 9, no. 11, pp. 1200–1208, 2010. View at Publisher · View at Google Scholar · View at Scopus
  64. H. Krenzlin, I. Demuth, B. Salewsky et al., “DNA damage in nijmegen breakage syndrome cells leads to PARP hyperactivation and increased oxidative stress,” PLoS Genetics, vol. 8, no. 3, Article ID e1002557, 2012. View at Publisher · View at Google Scholar · View at Scopus
  65. L. L. Woo, K. Futami, A. Shimamoto, Y. Furuichi, and K. M. Frank, “The Rothmund-Thomson gene product RECQL4 localizes to the nucleolus in response to oxidative stress,” Experimental Cell Research, vol. 312, no. 17, pp. 3443–3457, 2006. View at Publisher · View at Google Scholar · View at Scopus
  66. T. Davis, H. S. Tivey, A. J. Brook et al., “Activation of p38 MAP kinase and stress signalling in fibroblasts from the progeroid Rothmund-Thomson syndrome,” Age, vol. 35, no. 5, pp. 1767–1783, 2013. View at Google Scholar
  67. D. L. Croteau, M. L. Rossi, C. Canugovi et al., “RECQL4 localizes to mitochondria and preserves mitochondrial DNA integrity,” Aging Cell, vol. 11, no. 3, pp. 456–466, 2012. View at Publisher · View at Google Scholar · View at Scopus
  68. F. V. Pallardó, A. Lloret, M. Lebel et al., “Mitochondrial dysfunction in some oxidative stress-related genetic diseases: Ataxia-Telangiectasia, Down Syndrome, Fanconi Anaemia and Werner Syndrome,” Biogerontology, vol. 11, no. 4, pp. 401–419, 2010. View at Publisher · View at Google Scholar · View at Scopus
  69. V. A. Bohr, M. Cooper, D. Orren et al., “Werner syndrome protein: biochemical properties and functional interactions,” Experimental Gerontology, vol. 35, no. 6-7, pp. 695–702, 2000. View at Publisher · View at Google Scholar · View at Scopus
  70. C. von Kobbe, A. May, C. Grandori, and V. A. Bohr, “Werner syndrome cells escape hydrogen peroxide-induced cell proliferation arrest,” The FASEB Journal, vol. 18, no. 15, pp. 1970–1972, 2004. View at Publisher · View at Google Scholar · View at Scopus
  71. G. Pagano, A. Zatterale, P. Degan et al., “Multiple involvement of oxidative stress in Werner syndrome phenotype,” Biogerontology, vol. 6, no. 4, pp. 233–243, 2005. View at Publisher · View at Google Scholar · View at Scopus
  72. A. Lloret, R. Calzone, C. Dunster et al., “Different patterns of in vivo pro-oxidant states in a set of cancer- or aging-related genetic diseases,” Free Radical Biology and Medicine, vol. 44, no. 4, pp. 495–503, 2008. View at Publisher · View at Google Scholar · View at Scopus
  73. M. Hayashi, “Roles of oxidative stress in xeroderma pigmentosum,” Advances in Experimental Medicine and Biology, vol. 637, pp. 120–127, 2008. View at Publisher · View at Google Scholar · View at Scopus
  74. A. P. L. Ting, G. K. M. Low, K. Gopalakrishnan, and M. P. Hande, “Telomere attrition and genomic instability in xeroderma pigmentosum type-b deficient fibroblasts under oxidative stress,” Journal of Cellular and Molecular Medicine, vol. 14, no. 1-2, pp. 403–416, 2010. View at Publisher · View at Google Scholar · View at Scopus
  75. H. R. Rezvani, R. Rossignol, N. Ali et al., “XPC silencing in normal human keratinocytes triggers metabolic alterations through NOX-1 activation-mediated reactive oxygen species,” Biochimica et Biophysica Acta—Bioenergetics, vol. 1807, no. 6, pp. 609–619, 2011. View at Publisher · View at Google Scholar · View at Scopus
  76. J. Tanaka, T. Nagai, and S. Okada, “Serum concentration of coenzyme Q in xeroderma pigmentosum,” Clinical Neurology, vol. 38, no. 1, pp. 57–59, 1998. View at Google Scholar · View at Scopus
  77. X. Xia, D. Werner, O. Popanda, and H. W. Thielmann, “Expression of mitochondrial genes and DNA-repair-related nuclear genes is altered in xeroderma pigmentosum fibroblasts,” The Journal of Cancer Research and Clinical Oncology, vol. 120, no. 8, pp. 454–464, 1994. View at Publisher · View at Google Scholar · View at Scopus
  78. M. Deon, A. Sitta, A. G. Barschak et al., “Induction of lipid peroxidation and decrease of antioxidant defenses in symptomatic and asymptomatic patients with X-linked adrenoleukodystrophy,” International Journal of Developmental Neuroscience, vol. 25, no. 7, pp. 441–444, 2007. View at Publisher · View at Google Scholar · View at Scopus
  79. S. Petrillo, F. Piemonte, A. Pastore et al., “Glutathione imbalance in patients with X-linked adrenoleukodystrophy,” Molecular Genetics and Metabolism, vol. 109, no. 4, pp. 366–370, 2013. View at Google Scholar
  80. A. Schlüter, L. Espinosa, S. Fourcade et al., “Functional genomic analysis unravels a metabolic-inflammatory interplay in adrenoleukodystrophy,” Human Molecular Genetics, vol. 21, no. 5, pp. 1062–1077, 2012. View at Publisher · View at Google Scholar · View at Scopus
  81. J. López-Erauskin, J. Galino, M. Ruiz et al., “Impaired mitochondrial oxidative phosphorylation in the peroxisomal disease X-linked adrenoleukodystrophy,” Human Molecular Genetics, vol. 22, no. 16, pp. 3296–3305, 2013. View at Google Scholar
  82. S. Fourcade, J. López-Erauskin, M. Ruiz et al., “Mitochondrial dysfunction and oxidative damage cooperatively fuel axonal degeneration in X-linked adrenoleukodystrophy,” Biochimie, vol. 98, pp. 143–149, 2014. View at Publisher · View at Google Scholar
  83. J. R. Terrill, H. G. Radley-Crabb, T. Iwasaki et al., “Oxidative stress and pathology in muscular dystrophies: focus on protein thiol oxidation and dysferlinopathies,” FEBS Journal, vol. 280, no. 17, pp. 4149–4164, 2013. View at Google Scholar
  84. R. Renjini, N. Gayathri, A. Nalini, and M. M. Srinivas Bharath, “Oxidative damage in muscular dystrophy correlates with the severity of the pathology: role of glutathione metabolism,” Neurochemical Research, vol. 37, no. 4, pp. 885–898, 2012. View at Publisher · View at Google Scholar · View at Scopus
  85. J. M. Percival, M. P. Siegel, G. Knowels et al., “Defects in mitochondrial localization and ATP synthesis in the mdx mouse model of Duchenne muscular dystrophy are not alleviated by PDE5 inhibition,” Human Molecular Genetics, vol. 22, no. 1, pp. 153–167, 2013. View at Google Scholar
  86. J. M. Cooper, L. V. P. Korlipara, P. E. Hart, J. L. Bradley, and A. H. V. Schapira, “Coenzyme Q(10) and vitamin E deficiency in Friedreich's ataxia: predictor of efficacy of vitamin e and coenzyme Q(10) therapy,” The European Journal of Neurology, vol. 15, no. 12, pp. 1371–1379, 2008. View at Publisher · View at Google Scholar · View at Scopus
  87. M. Sparaco, L. M. Gaeta, F. M. Santorelli et al., “Friedreich's ataxia: oxidative stress and cytoskeletal abnormalities,” The Journal of the Neurological Sciences, vol. 287, no. 1-2, pp. 111–118, 2009. View at Publisher · View at Google Scholar · View at Scopus
  88. R. Santos, S. Lefevre, D. Sliwa, A. Seguin, J. Camadro, and E. Lesuisse, “Friedreich ataxia: molecular mechanisms, redox considerations, and therapeutic opportunities,” Antioxidants and Redox Signaling, vol. 13, no. 5, pp. 651–690, 2010. View at Publisher · View at Google Scholar · View at Scopus
  89. H. C. Hyson, K. Kieburtz, I. Shoulson et al., “Safety and tolerability of high-dosage coenzyme Q(10) in Huntington's disease and healthy subjects,” Movement Disorders, vol. 25, no. 12, pp. 1924–1928, 2010. View at Publisher · View at Google Scholar · View at Scopus
  90. A. Valencia, E. Sapp, J. S. Kimm et al., “Elevated NADPH oxidase activity contributes to oxidative stress and cell death in Huntington's disease,” Human Molecular Genetics, vol. 22, no. 6, pp. 1112–1131, 2013. View at Google Scholar
  91. L. Yang, N. Y. Calingasan, E. J. Wille et al., “Combination therapy with Coenzyme Q(10) and creatine produces additive neuroprotective effects in models of Parkinson's and Huntington's diseases,” Journal of Neurochemistry, vol. 109, no. 5, pp. 1427–1439, 2009. View at Publisher · View at Google Scholar · View at Scopus
  92. M. Ribeiro, A. C. Silva, J. Rodrigues et al., “Oxidizing effects of exogenous stressors in Huntington's disease knock-in striatal cells—protective effect of cystamine and creatine,” Toxicological Sciences, vol. 136, no. 2, pp. 487–499, 2013. View at Publisher · View at Google Scholar
  93. N. Tyagi, A. V. Ovechkin, D. Lominadze, K. S. Moshal, and S. C. Tyagi, “Mitochondrial mechanism of microvascular endothelial cells apoptosis in hyperhomocysteinemia,” Journal of Cellular Biochemistry, vol. 98, no. 5, pp. 1150–1162, 2006. View at Publisher · View at Google Scholar · View at Scopus
  94. K. S. Moshal, S. M. Tipparaju, T. P. Vacek et al., “Mitochondrial matrix metalloproteinase activation decreases myocyte contractility in hyperhomocysteinemia,” The American Journal of Physiology—Heart and Circulatory Physiology, vol. 295, no. 2, pp. H890–H897, 2008. View at Publisher · View at Google Scholar · View at Scopus
  95. C. S. Vanzin, G. B. Biancini, A. Sitta et al., “Experimental evidence of oxidative stress in plasma of homocystinuric patients: a possible role for homocysteine,” Molecular Genetics and Metabolism, vol. 104, no. 1-2, pp. 112–117, 2011. View at Publisher · View at Google Scholar · View at Scopus
  96. E. Nur, D. P. Brandjes, J. B. Schnog et al., “Plasma levels of advanced glycation end products are associated with haemolysis-related organ complications in sickle cell patients,” British Journal of Haematology, vol. 151, no. 1, pp. 62–69, 2010. View at Publisher · View at Google Scholar · View at Scopus
  97. J. Amer, H. Ghoti, E. Rachmilewitz, A. Koren, C. Levin, and E. Fibach, “Red blood cells, platelets and polymorphonuclear neutrophils of patients with sickle cell disease exhibit oxidative stress that can be ameliorated by antioxidants,” British Journal of Haematology, vol. 132, no. 1, pp. 108–113, 2006. View at Publisher · View at Google Scholar · View at Scopus
  98. J. A. Grasso, A. L. Sullivan, and L. W. Sullivan, “Ultrastructural studies of the bone marrow in sickle cell anaemia. I. The structure of sickled erythrocytes and reticulocytes and their phagocytic destruction,” British Journal of Haematology, vol. 31, no. 2, pp. 135–148, 1975. View at Google Scholar · View at Scopus
  99. C. Hershko, “Pathogenesis and management of iron toxicity in thalassemia,” Annals of the New York Academy of Sciences, vol. 1202, pp. 1–9, 2010. View at Publisher · View at Google Scholar · View at Scopus
  100. E. Ferro, G. Visalli, R. Civa et al., “Oxidative damage and genotoxicity biomarkers in transfused and untransfused thalassemic subjects,” Free Radical Biology and Medicine, vol. 53, no. 10, pp. 1829–1837, 2012. View at Google Scholar
  101. V. Tsagris and G. Liapi-Adamidou, “Serum carnitine levels in patients with homozygous beta thalassemia: a possible new role for carnitine?” European Journal of Pediatrics, vol. 164, no. 3, pp. 131–134, 2005. View at Publisher · View at Google Scholar · View at Scopus
  102. I. Rebrin and R. S. Sohal, “Pro-oxidant shift in glutathione redox state during aging,” Advanced Drug Delivery Reviews, vol. 60, no. 13-14, pp. 1545–1552, 2008. View at Publisher · View at Google Scholar · View at Scopus
  103. P. Møller, M. Løhr, J. K. Folkmann, L. Mikkelsen, and S. Loft, “Aging and oxidatively damaged nuclear DNA in animal organs,” Free Radical Biology and Medicine, vol. 48, no. 10, pp. 1275–1285, 2010. View at Publisher · View at Google Scholar · View at Scopus
  104. S. B. Cau, F. S. Carneiro, and R. C. Tostes, “Differential modulation of nitric oxide synthases in aging: therapeutic opportunities,” Frontiers in Physiology, vol. 3, article 218, 2012. View at Google Scholar
  105. C. Musicco, V. Capelli, V. Pesce et al., “Accumulation of overoxidized Peroxiredoxin III in aged rat liver mitochondria,” Biochimica et Biophysica Acta—Bioenergetics, vol. 1787, no. 7, pp. 890–896, 2009. View at Publisher · View at Google Scholar · View at Scopus
  106. C. H. Wang, S. B. Wu, Y. T. Wu et al., “Oxidative stress response elicited by mitochondrial dysfunction: implication in the pathophysiology of aging,” Experimental Biology and Medicine, vol. 238, no. 5, pp. 450–460, 2013. View at Google Scholar
  107. M. C. Gomez-Cabrera, F. Sanchis-Gomar, R. Garcia-Valles et al., “Mitochondria as sources and targets of damage in cellular aging,” Clinical Chemistry and Laboratory Medicine, vol. 50, no. 8, pp. 1287–1295, 2012. View at Google Scholar
  108. E. Takimoto and D. A. Kass, “Role of oxidative stress in cardiac hypertrophy and remodeling,” Hypertension, vol. 49, no. 2, pp. 241–248, 2007. View at Publisher · View at Google Scholar · View at Scopus
  109. V. M. Victor, M. Rocha, E. Solá, C. Bañuls, K. Garcia-Malpartida, and A. Hernández-Mijares, “Oxidative stress, endothelial dysfunction and atherosclerosis,” Current Pharmaceutical Design, vol. 15, no. 26, pp. 2988–3002, 2009. View at Publisher · View at Google Scholar · View at Scopus
  110. F. Di Lisa, N. Kaludercic, A. Carpi, R. Menabò, and M. Giorgio, “Mitochondria and vascular pathology,” Pharmacological Reports, vol. 61, no. 1, pp. 123–130, 2009. View at Google Scholar · View at Scopus
  111. I. Perrotta, E. Perrotta, S. Sesti et al., “MnSOD expression in human atherosclerotic plaques: an immunohistochemical and ultrastructural study,” Cardiovascular Pathology, vol. 22, no. 6, pp. 428–437, 2013. View at Google Scholar
  112. I. A. Sobenin, M. A. Sazonova, A. Y. Postnov et al., “Changes of mitochondria in atherosclerosis: possible determinant in the pathogenesis of the disease,” Atherosclerosis, vol. 227, no. 2, pp. 283–288, 2013. View at Google Scholar
  113. B. Guzik, A. Sagan, D. Ludew et al., “Mechanisms of oxidative stress in human aortic aneurysms—association with clinical risk factors for atherosclerosis and disease severity,” International Journal of Cardiology, vol. 168, no. 3, pp. 2389–2396, 2013. View at Google Scholar
  114. B. Hansel, P. Giral, E. Nobecourt et al., “Metabolic syndrome is associated with elevated oxidative stress and dysfunctional dense high-density lipoprotein particles displaying impaired antioxidative activity,” The Journal of Clinical Endocrinology and Metabolism, vol. 89, no. 10, pp. 4963–4971, 2004. View at Publisher · View at Google Scholar · View at Scopus
  115. V. O. Palmieri, I. Grattagliano, P. Portincasa, and G. Palasciano, “Systemic oxidative alterations are associated with visceral adiposity and liver steatosis in patients with metabolic syndrome,” The Journal of Nutrition, vol. 136, no. 12, pp. 3022–3026, 2006. View at Google Scholar · View at Scopus
  116. S. Koene, R. J. Rodenburg, M. S. van der Knaap et al., “Natural disease course and genotype-phenotype correlations in Complex I deficiency caused by nuclear gene defects: what we learned from 130 cases,” Journal of Inherited Metabolic Diseases, vol. 35, no. 5, pp. 737–747, 2012. View at Google Scholar
  117. C. Huang, S. Su, M. Hsieh et al., “Depleted leukocyte mitochondrial DNA copy number in metabolic syndrome,” Journal of Atherosclerosis and Thrombosis, vol. 18, no. 10, pp. 867–873, 2011. View at Publisher · View at Google Scholar · View at Scopus
  118. T. Mitchell and V. Darley-Usmar, “Metabolic syndrome and mitochondrial dysfunction: insights from preclinical studies with a mitochondrially targeted antioxidant,” Free Radical Biology and Medicine, vol. 52, no. 5, pp. 838–840, 2012. View at Publisher · View at Google Scholar · View at Scopus
  119. A. Auinger, D. Rubin, M. Sabandal et al., “A common haplotype of carnitine palmitoyltransferase 1b is associated with the metabolic syndrome,” British Journal of Nutrition, vol. 109, no. 5, pp. 810–815, 2013. View at Google Scholar
  120. O. Altindag, O. Erel, N. Aksoy, S. Selek, H. Celik, and M. Karaoglanoglu, “Increased oxidative stress and its relation with collagen metabolism in knee osteoarthritis,” Rheumatology International, vol. 27, no. 4, pp. 339–344, 2007. View at Publisher · View at Google Scholar · View at Scopus
  121. M. Fernandez-Moreno, A. Soto-Hermida, S. Pertega et al., “Mitochondrial DNA (mtDNA) haplogroups and serum levels of anti-oxidant enzymes in patients with osteoarthritis,” BMC Musculoskeletal Disorders, vol. 12, article 264, 2011. View at Publisher · View at Google Scholar · View at Scopus
  122. Z. Li, J. Shen, Y. Chen et al., “Mitochondrial genome sequencing of chondrocytes in osteoarthritis by human mitochondria RT2 Profiler PCR array,” Molecular Medicine Reports, vol. 6, no. 1, pp. 39–44, 2012. View at Google Scholar
  123. M. Fernández-Moreno, A. Soto-Hermida, N. Oreiro et al., “Mitochondrial haplogroups define two phenotypes of osteoarthritis,” Frontiers in Physiology, vol. 3, article 129, 2012. View at Google Scholar
  124. C. Gavrilidis, S. Miwa, T. von Zglinicki et al., “Mitochondrial dysfunction in osteoarthritis is associated with down-regulation of superoxide dismutase 2,” Arthritis and Rheumatism, vol. 65, no. 5, pp. 378–387, 2013. View at Google Scholar
  125. O. Tabak, R. Gelisgen, H. Erman et al., “Oxidative lipid, protein, and DNA damage as oxidative stress markers in vascular complications of diabetes mellitus,” Clinical and Investigative Medicine, vol. 34, no. 3, pp. E163–E171, 2011. View at Google Scholar · View at Scopus
  126. A. P. Remor, F. J. de Matos, K. Ghisoni et al., “Differential effects of insulin on peripheral diabetes-related changes in mitochondrial bioenergetics: involvement of advanced glycosylated end products,” Biochimica et Biophysica Acta—Molecular Basis of Disease, vol. 1812, no. 11, pp. 1460–1471, 2011. View at Publisher · View at Google Scholar · View at Scopus
  127. S. Bansal, M. Siddarth, D. Chawla, B. D. Banerjee, S. V. Madhu, and A. K. Tripathi, “Advanced glycation end products enhance reactive oxygen and nitrogen species generation in neutrophils in vitro,” Molecular and Cellular Biochemistry, vol. 361, no. 1-2, pp. 289–296, 2012. View at Google Scholar · View at Scopus
  128. R. Noriega-Cisneros, C. Cortés-Rojo, S. Manzo-Avalos et al., “Mitochondrial response to oxidative and nitrosative stress in early stages of diabetes,” Mitochondrion, vol. 13, no. 6, pp. 835–840, 2013. View at Google Scholar
  129. M. A. Amer, M. H. Ghattas, D. M. Abo-Elmatty et al., “Influence of glutathione S-transferase polymorphisms on type-2 diabetes mellitus risk,” Genetics and Molecular Research, vol. 10, no. 4, pp. 3722–3730, 2011. View at Google Scholar
  130. S. Khan, G. V. Raghuram, A. Bhargava et al., “Role and clinical significance of lymphocyte mitochondrial dysfunction in type 2 diabetes mellitus,” Translational Research, vol. 158, no. 6, pp. 344–359, 2011. View at Publisher · View at Google Scholar · View at Scopus
  131. C. Avila, R. J. Huang, M. V. Stevens et al., “Platelet mitochondrial dysfunction is evident in type 2 diabetes in association with modifications of mitochondrial anti-oxidant stress proteins,” Experimental and Clinical Endocrinology and Diabetes, vol. 120, no. 4, pp. 248–251, 2012. View at Publisher · View at Google Scholar · View at Scopus
  132. V. Calabrese, C. Cornelius, V. Leso et al., “Oxidative stress, glutathione status, sirtuin and cellular stress response in type 2 diabetes,” Biochimica et Biophysica Acta—Molecular Basis of Disease, vol. 1822, no. 5, pp. 729–736, 2012. View at Publisher · View at Google Scholar · View at Scopus
  133. S. P. Gray, E. Di Marco, J. Okabe et al., “NADPH oxidase 1 plays a key role in diabetes mellitus-accelerated atherosclerosis,” Circulation, vol. 127, no. 18, pp. 1888–1902, 2013. View at Google Scholar
  134. E. Area-Gomez, M. Del Carmen Lara Castillo, M. D. Tambini et al., “Upregulated function of mitochondria-associated ER membranes in Alzheimer disease,” The EMBO Journal, vol. 31, no. 21, pp. 4106–4123, 2012. View at Google Scholar
  135. H. Atamna and W. H. Frey II, “Mechanisms of mitochondrial dysfunction and energy deficiency in Alzheimer's disease,” Mitochondrion, vol. 7, no. 5, pp. 297–310, 2007. View at Publisher · View at Google Scholar · View at Scopus
  136. M. Dumont, K. Kipiani, F. Yu et al., “Coenzyme Q(10) decreases amyloid pathology and improves behavior in a transgenic mouse model of alzheimer's disease,” The Journal of Alzheimer's Disease, vol. 27, no. 1, pp. 211–223, 2011. View at Publisher · View at Google Scholar · View at Scopus
  137. K. Murakami, N. Murata, Y. Noda et al., “Stimulation of the amyloidogenic pathway by cytoplasmic superoxide radicals in an Alzheimer's disease mouse model,” Bioscience, Biotechnology, and Biochemistry, vol. 76, no. 6, pp. 1098–1103, 2012. View at Google Scholar
  138. S. S. Hardas, R. Sultana, A. M. Clark et al., “Oxidative modification of lipoic acid by HNE in Alzheimer disease brain,” Redox Biology, vol. 1, no. 1, pp. 80–85, 2013. View at Google Scholar
  139. G. Aliev, H. H. Palacios, E. Gasimov et al., “Oxidative stress induced mitochondrial failure and vascular hypoperfusion as a key initiator for the development of alzheimer disease,” Pharmaceuticals, vol. 3, no. 1, pp. 158–187, 2010. View at Publisher · View at Google Scholar · View at Scopus
  140. A. Zarrouk, A. Vejux, T. Nury et al., “Induction of mitochondrial changes associated with oxidative stress on very long chain fatty acids (C22:0, C24:0, or C26:0)-treated human neuronal cells (SK-NB-E),” Oxidative Medicine and Cellular Longevity, vol. 2012, Article ID 623257, 15 pages, 2012. View at Publisher · View at Google Scholar
  141. J. Kou, G. G. Kovacs, R. Höftberger et al., “Peroxisomal alterations in Alzheimer's disease,” Acta Neuropathologica, vol. 122, no. 3, pp. 271–283, 2011. View at Google Scholar
  142. M. Cozzolino and M. T. Carrì, “Mitochondrial dysfunction in ALS,” Progress in Neurobiology, vol. 97, no. 2, pp. 54–66, 2012. View at Google Scholar
  143. E. Cova, P. Bongioanni, C. Cereda et al., “Time course of oxidant markers and antioxidant defenses in subgroups of amyotrophic lateral sclerosis patients,” Neurochemistry International, vol. 56, no. 5, pp. 687–693, 2010. View at Publisher · View at Google Scholar · View at Scopus
  144. C. M. Karch, M. Prudencio, D. D. Winkler, P. J. Hart, and D. R. Borchelt, “Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 19, pp. 7774–7779, 2009. View at Publisher · View at Google Scholar · View at Scopus
  145. G. E. Rodríguez, D. M. González, G. M. Monachelli et al., “Morphological abnormalities in mitochondria of the skin of patients with sporadic amyotrophic lateral sclerosis,” Arquivos de Neuro-Psiquiatria, vol. 70, no. 1, pp. 40–44, 2012. View at Google Scholar
  146. P. Ghiasi, S. Hosseinkhani, A. Noori, S. Nafissi, and K. Khajeh, “Mitochondrial complex I deficiency and ATP/ADP ratio in lymphocytes of amyotrophic lateral sclerosis patients,” Neurological Research, vol. 34, no. 3, pp. 297–303, 2012. View at Publisher · View at Google Scholar · View at Scopus
  147. Y. Chuang, “Mitochondrial dysfunction and oxidative stress in seizure-induced neuronal cell death,” Acta Neurologica Taiwanica, vol. 19, no. 1, pp. 3–15, 2010. View at Google Scholar · View at Scopus
  148. D. Malinska, B. Kulawiak, A. P. Kudin et al., “Complex III-dependent superoxide production of brain mitochondria contributes to seizure-related ROS formation,” Biochimica et Biophysica Acta—Bioenergetics, vol. 1797, no. 6-7, pp. 1163–1170, 2010. View at Publisher · View at Google Scholar · View at Scopus
  149. J. A. Mayr, F. A. Zimmermann, C. Fauth et al., “Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation,” American Journal of Human Genetics, vol. 89, no. 6, pp. 792–797, 2011. View at Publisher · View at Google Scholar · View at Scopus
  150. J. L. García-Giménez, M. Seco-Cervera, C. Aguado et al., “Lafora disease fibroblasts exemplify the molecular interdependence between thioredoxin 1 and the proteasome in mammalian cells,” Free Radical Biology and Medicine C, vol. 65, pp. 347–359, 2013. View at Google Scholar
  151. N. E. Booth, S. Myhill, and J. McLaren-Howard, “Mitochondrial dysfunction and the pathophysiology of Myalgic Encephalomyelitis/Chronic Fatigue Syndrome (ME/CFS),” International Journal of Clinical and Experimental Medicine, vol. 5, no. 3, pp. 208–220, 2012. View at Google Scholar
  152. M. Maes, I. Mihaylova, M. Kubera, M. Uytterhoeven, N. Vrydags, and E. Bosmans, “Increased 8-hydroxy-deoxyguanosine, a marker of oxidative damage to DNA, in major depression and myalgic encephalomyelitis/chronic fatigue syndrome,” Neuroendocrinology Letters, vol. 30, no. 6, pp. 715–722, 2009. View at Google Scholar · View at Scopus
  153. M. Maes, I. Mihaylova, M. Kubera, M. Uytterhoeven, N. Vrydags, and E. Bosmans, “Coenzyme Q(10) deficiency in myalgic encephalomyelitis/chronic fatigue syndrome (ME/CFS) is related to fatigue, autonomic and neurocognitive symptoms and is another risk factor explaining the early mortality in ME/CFS due to cardiovascular disorder,” Neuroendocrinology Letters, vol. 30, no. 4, pp. 470–476, 2009. View at Google Scholar · View at Scopus
  154. M. Maes, M. Kubera, M. Uytterhoeven, N. Vrydags, and E. Bosmans, “Increased plasma peroxides as a marker of oxidative stress in myalgic encephalomyelitis/chronic fatigue syndrome (ME/CFS),” Medical Science Monitor, vol. 17, no. 4, pp. SC11–SC15, 2011. View at Google Scholar · View at Scopus
  155. Y. Jammes, J. G. Steinberg, and S. Delliaux, “Chronic fatigue syndrome: acute infection and history of physical activity affect resting levels and response to exercise of plasma oxidant/antioxidant status and heat shock proteins,” Journal of Internal Medicine, vol. 272, no. 1, pp. 74–84, 2012. View at Publisher · View at Google Scholar · View at Scopus
  156. B. Smits, L. van den Heuvel, H. Knoop et al., “Mitochondrial enzymes discriminate between mitochondrial disorders and chronic fatigue syndrome,” Mitochondrion, vol. 11, no. 5, pp. 735–738, 2011. View at Publisher · View at Google Scholar · View at Scopus
  157. E. Miller, A. Walczak, J. Saluk, M. B. Ponczek, and I. Majsterek, “Oxidative modification of patient's plasma proteins and its role in pathogenesis of multiple sclerosis,” Clinical Biochemistry, vol. 45, no. 1-2, pp. 26–30, 2012. View at Publisher · View at Google Scholar · View at Scopus
  158. M. T. Fischer, R. Sharma, J. L. Lim et al., “NADPH oxidase expression in active multiple sclerosis lesions in relation to oxidative tissue damage and mitochondrial injury,” Brain, vol. 135, part 3, pp. 886–899, 2012. View at Publisher · View at Google Scholar · View at Scopus
  159. G. R. Campbell and D. J. Mahad, “Clonal expansion of mitochondrial DNA deletions and the progression of multiple sclerosis,” CNS and Neurological Disorders—Drug Targets, vol. 11, no. 5, pp. 589–597, 2012. View at Google Scholar
  160. E. Miller, A. Walczak, I. Majsterek et al., “Melatonin reduces oxidative stress in the erythrocytes of multiple sclerosis patients with secondary progressive clinical course,” Journal of Neuroimmunology, vol. 257, no. 1-2, pp. 97–101, 2013. View at Google Scholar
  161. R. C. S. Seet, C. J. Lee, E. C. H. Lim et al., “Oxidative damage in Parkinson disease: measurement using accurate biomarkers,” Free Radical Biology and Medicine, vol. 48, no. 4, pp. 560–566, 2010. View at Publisher · View at Google Scholar · View at Scopus
  162. L. K. Mischley, J. Allen, and R. Bradley, “Coenzyme Q(10) deficiency in patients with Parkinson's disease,” The Journal of the Neurological Sciences, vol. 318, no. 1-2, pp. 72–75, 2012. View at Publisher · View at Google Scholar · View at Scopus
  163. M. Naoi, W. Maruyama, M. Shamoto-Nagai, H. Yi, Y. Akao, and M. Tanaka, “Oxidative stress in mitochondria: decision to survival and death of neurons in neurodegenerative disorders,” Molecular Neurobiology, vol. 31, no. 1–3, pp. 81–93, 2005. View at Google Scholar · View at Scopus
  164. S. R. Danielson, J. M. Held, M. Oo, R. Riley, B. W. Gibson, and J. K. Andersen, “Quantitative mapping of reversible mitochondrial complex I cysteine oxidation in a Parkinson disease mouse model,” The Journal of Biological Chemistry, vol. 286, no. 9, pp. 7601–7608, 2011. View at Publisher · View at Google Scholar · View at Scopus
  165. I. Cacciatore, L. Baldassarre, E. Fornasari et al., “Recent advances in the treatment of neurodegenerative diseases based on GSH delivery systems,” Oxidative Medicine and Cellular Longevity, vol. 2012, Article ID 240146, 12 pages, 2012. View at Publisher · View at Google Scholar
  166. S. Rose, S. Melnyk, T. A. Trusty et al., “Intracellular and extracellular redox status and free radical generation in primary immune cells from children with autism,” Autism Research and Treatment, vol. 2012, Article ID 986519, 10 pages, 2012. View at Publisher · View at Google Scholar
  167. A. Pecorelli, S. Leoncini, C. de Felice et al., “Non-protein-bound iron and 4-hydroxynonenal protein adducts in classic autism,” Brain and Development, vol. 35, no. 2, pp. 146–154, 2013. View at Publisher · View at Google Scholar · View at Scopus
  168. A. Frustaci, M. Neri, A. Cesario et al., “Oxidative stress-related biomarkers in autism: systematic review and meta-analyses,” Free Radical Biology and Medicine, vol. 52, no. 10, pp. 2128–2141, 2012. View at Google Scholar
  169. S. Rose, S. Melnyk, O. Pavliv et al., “Evidence of oxidative damage and inflammation associated with low glutathione redox status in the autism brain,” Translational Psychiatry, vol. 2, article e134, 2012. View at Google Scholar
  170. A. Anitha, K. Nakamura, I. Thanseem et al., “Downregulation of the expression of mitochondrial electron transport complex genes in autism brains,” Brain Pathology, vol. 23, no. 3, pp. 294–302, 2013. View at Google Scholar
  171. E. Napoli, S. Wong, and C. Giulivi, “Evidence of reactive oxygen species-mediated damage to mitochondrial DNA in children with typical autism,” Molecular Autism, vol. 4, no. 1, p. 2, 2013. View at Google Scholar
  172. C. Ross-Inta, A. Omanska-Klusek, S. Wong et al., “Evidence of mitochondrial dysfunction in fragile X-associated tremor/ataxia syndrome,” Biochemical Journal, vol. 429, no. 3, pp. 545–552, 2010. View at Publisher · View at Google Scholar · View at Scopus
  173. U. Banerjee, A. Dasgupta, J. K. Rout, and O. P. Singh, “Effects of lithium therapy on Na+-K+-ATPase activity and lipid peroxidation in bipolar disorder,” Progress in Neuro-Psychopharmacology and Biological Psychiatry, vol. 37, no. 1, pp. 56–61, 2012. View at Publisher · View at Google Scholar · View at Scopus
  174. M. Raffa, S. Barhoumi, F. Atig et al., “Reduced antioxidant defense systems in schizophrenia and bipolar I disorder,” Progress in Neuro-Psychopharmacology and Biological Psychiatry, vol. 39, no. 2, pp. 371–375, 2012. View at Google Scholar
  175. A. C. Andreazza, J. F. Wang, F. Salmasi et al., “Specific subcellular changes in oxidative stress in prefrontal cortex from patients with bipolar disorder,” Journal of Neurochemistry, vol. 127, no. 4, pp. 552–561, 2013. View at Google Scholar
  176. B. S. Rawdin, S. H. Mellon, F. S. Dhabhar et al., “Dysregulated relationship of inflammation and oxidative stress in major depression,” Brain, Behavior, and Immunity, vol. 31, no. 1, pp. 143–152, 2013. View at Google Scholar
  177. A. Szuster-Ciesielska, M. Słotwińska, A. Stachura et al., “Accelerated apoptosis of blood leukocytes and oxidative stress in blood of patients with major depression,” Progress in Neuro-Psychopharmacology and Biological Psychiatry, vol. 32, no. 3, pp. 686–694, 2008. View at Publisher · View at Google Scholar · View at Scopus
  178. S. A. Gibson, Ž. Korade, and R. C. Shelton, “Oxidative stress and glutathione response in tissue cultures from persons with major depression,” Journal of Psychiatric Research, vol. 46, no. 10, pp. 1326–1632, 2012. View at Google Scholar
  179. D. Ben-Shachar and R. Karry, “Neuroanatomical pattern of mithochondrial complex I pathology varies between schizoprenia, bipolar disorder and major depression,” PLoS ONE, vol. 3, no. 11, Article ID e3676, 2008. View at Publisher · View at Google Scholar · View at Scopus
  180. S. Chakraborty, O. P. Singh, A. Dasgupta, N. Mandal, and H. N. Das, “Correlation between lipid peroxidation-induced TBARS level and disease severity in obsessive-compulsive disorder,” Progress in Neuro-Psychopharmacology and Biological Psychiatry, vol. 33, no. 2, pp. 363–366, 2009. View at Publisher · View at Google Scholar · View at Scopus
  181. A. Behl, G. Swami, S. S. Sircar, M. S. Bhatia, and B. D. Banerjee, “Relationship of possible stress-related biochemical markers to oxidative/antioxidative status in obsessive-compulsive disorder,” Neuropsychobiology, vol. 61, no. 4, pp. 210–214, 2010. View at Publisher · View at Google Scholar · View at Scopus
  182. N. Orhan, C. I. Kucukali, U. Cakir, N. Seker, and M. Aydin, “Genetic variants in nuclear-encoded mitochondrial proteins are associated with oxidative stress in obsessive compulsive disorders,” Journal of Psychiatric Research, vol. 46, no. 2, pp. 212–218, 2012. View at Publisher · View at Google Scholar · View at Scopus
  183. G. Anderson, M. Maes, and M. Berk, “Schizophrenia is primed for an increased expression of depression through activation of immuno-inflammatory, oxidative and nitrosative stress, and tryptophan catabolite pathways,” Progress in Neuro-Psychopharmacology and Biological Psychiatry, vol. 42, pp. 101–114, 2013. View at Google Scholar
  184. M. Pedrini, R. Massuda, G. R. Fries et al., “Similarities in serum oxidative stress markers and inflammatory cytokines in patients with overt schizophrenia at early and late stages of chronicity,” Journal of Psychiatric Research, vol. 46, no. 6, pp. 819–824, 2012. View at Publisher · View at Google Scholar · View at Scopus
  185. A. Kulak, P. Steullet, J. H. Cabungcal et al., “Redox dysregulation in the pathophysiology of schizophrenia and bipolar disorder: insights from animal models,” Antioxidants and Redox Signaling, vol. 18, no. 12, pp. 1428–1443, 2012. View at Google Scholar
  186. X. Y. Zhang, D. C. Chen, M. H. Xiu et al., “Plasma total antioxidant status and cognitive impairments in schizophrenia,” Schizophrenia Research, vol. 139, no. 1–3, pp. 66–72, 2012. View at Publisher · View at Google Scholar · View at Scopus
  187. C. Gubert, L. Stertz, B. Pfaffenseller et al., “Mitochondrial activity and oxidative stress markers in peripheral blood mononuclear cells of patients with bipolar disorder, schizophrenia, and healthy subjects,” Journal of Psychiatric Research, vol. 47, no. 10, pp. 1396–1402, 2013. View at Google Scholar
  188. A. Costa, A. Scholer-Dahirel, and F. Mechta-Grigoriou, “The role of reactive oxygen species and metabolism on cancer cells and their microenvironment,” Seminars in Cancer Biology, 2014. View at Publisher · View at Google Scholar
  189. D. Hanahan and R. A. Weinberg, “Hallmarks of cancer: the next generation,” Cell, vol. 144, no. 5, pp. 646–674, 2011. View at Publisher · View at Google Scholar · View at Scopus
  190. A. Masoudi-Nejad and Y. Asgari, “Metabolic Cancer Biology: structural-based analysis of cancer as a metabolic disease, new sights and opportunities for disease treatment,” Seminars in Cancer Biology, 2014. View at Publisher · View at Google Scholar
  191. Y. Soini, K. Haapasaari, M. H. Vaarala, T. Turpeenniemi-Hujanen, V. Kärjä, and P. Karihtala, “8-hydroxydeguanosine and nitrotyrosine are prognostic factors in urinary bladder carcinoma,” International Journal of Clinical and Experimental Pathology, vol. 4, no. 3, pp. 267–275, 2011. View at Google Scholar · View at Scopus
  192. N. Badjatia, A. Satyam, P. Singh, A. Seth, and A. Sharma, “Altered antioxidant status and lipid peroxidation in Indian patients with urothelial bladder carcinoma,” Urologic Oncology: Seminars and Original Investigations, vol. 28, no. 4, pp. 360–367, 2010. View at Publisher · View at Google Scholar · View at Scopus
  193. A. I. Guney, D. S. Ergec, H. H. Tavukcu et al., “Detection of mitochondrial DNA mutations in nonmuscle invasive bladder cancer,” Genetic Testing and Molecular Biomarkers, vol. 16, no. 7, pp. 672–678, 2012. View at Google Scholar
  194. H. T. Niu, C. M. Yang, G. Jiang et al., “Cancer stroma proteome expression profile of superficial bladder transitional cell carcinoma and biomarker discovery,” The Journal of Cancer Research and Clinical Oncology, vol. 137, no. 8, pp. 1273–1282, 2011. View at Publisher · View at Google Scholar · View at Scopus
  195. M. Kedzierska, B. Olas, B. Wachowicz, A. Jeziorski, and J. Piekarski, “Relationship between thiol, tyrosine nitration and carbonyl formation as biomarkers of oxidative stress and changes of hemostatic function of plasma from breast cancer patients before surgery,” Clinical Biochemistry, vol. 45, no. 3, pp. 231–236, 2012. View at Publisher · View at Google Scholar · View at Scopus
  196. D. Pande, R. Negi, K. Karki et al., “Oxidative damage markers as possible discriminatory biomarkers in breast carcinoma,” Translational Research, vol. 160, no. 6, pp. 411–418, 2012. View at Google Scholar
  197. U. E. Martinez-Outschoorn, R. Balliet, Z. Lin et al., “BRCA1 mutations drive oxidative stress and glycolysis in the tumor microenvironment: implications for breast cancer prevention with antioxidant therapies,” Cell Cycle, vol. 11, no. 23, pp. 4402–4413, 2012. View at Google Scholar
  198. A. F. Salem, A. Howell, M. Sartini et al., “Downregulation of stromal BRCA1 drives breast cancer tumor growth via upregulation of HIF-1α, autophagy and ketone body production,” Cell Cycle, vol. 11, no. 22, pp. 4167–4173, 2012. View at Google Scholar
  199. F. Sotgia, D. Whitaker-Menezes, U. E. Martinez-Outschoorn et al., “Mitochondria, “fuel” breast cancer metabolism: fifteen markers of mitochondrial biogenesis label epithelial cancer cells, but are excluded from adjacent stromal cell,” Cell Cycle, vol. 11, no. 23, pp. 4390–4401, 2012. View at Google Scholar
  200. E. D. Coene, M. S. Hollinshead, A. A. T. Waeytens et al., “Phosphorylated BRCA1 is predominantly located in the nucleus and mitochondria,” Molecular Biology of the Cell, vol. 16, no. 2, pp. 997–1010, 2005. View at Publisher · View at Google Scholar · View at Scopus
  201. R. V. Cooney, Q. Dai, Y. Gao et al., “Low plasma coenzyme Q(10) levels and breast cancer risk in Chinese women,” Cancer Epidemiology Biomarkers and Prevention, vol. 20, no. 6, pp. 1124–1130, 2011. View at Publisher · View at Google Scholar · View at Scopus
  202. M. Looi, A. Z. H. Ahmad Zailani Hatta, A. Z. H. M. Dali, S. A. M. Ali, W. Z. W. Ngah, and Y. A. M. Yusof, “Oxidative damage and antioxidant status in patients with cervical intraepithelial neoplasia and carcinoma of the cervix,” European Journal of Cancer Prevention, vol. 17, no. 6, pp. 555–560, 2008. View at Publisher · View at Google Scholar · View at Scopus
  203. L. Li, C. Chen, Z. Cao et al., “Expression of peroxiredoxin III cervical lesions,” ZZhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi, vol. 23, no. 6, pp. 443–445, 2009. View at Google Scholar · View at Scopus
  204. S. Srivastava, S. M. Natu, A. Gupta et al., “Lipid peroxidation and antioxidants in different stages of cervical cancer: prognostic significance,” Indian Journal of Cancer, vol. 46, no. 4, pp. 297–302, 2009. View at Publisher · View at Google Scholar · View at Scopus
  205. A. Sharma, M. Rajappa, A. Satyam, and M. Sharma, “Oxidant/anti-oxidant dynamics in patients with advanced cervical cancer: correlation with treatment response,” Molecular and Cellular Biochemistry, vol. 341, no. 1-2, pp. 65–72, 2010. View at Publisher · View at Google Scholar · View at Scopus
  206. F. de Marco, E. Bucaj, C. Foppoli et al., “Oxidative stress in HPV-driven viral carcinogenesis: redox proteomics analysis of HPV-16 dysplastic and neoplastic tissues,” PLoS ONE, vol. 7, no. 3, Article ID e34366, 2012. View at Publisher · View at Google Scholar · View at Scopus
  207. L. Gao, X. Pan, L. Li et al., “Null genotypes of gstm1 and gstt1 contribute to risk of cervical neoplasia: an evidence-based meta-analysis,” PLoS ONE, vol. 6, no. 5, Article ID e20157, 2011. View at Publisher · View at Google Scholar · View at Scopus
  208. M. Safaeian, A. Hildesheim, P. Gonzalez et al., “Single nucleotide polymorphisms in the PRDX3 and RPS19 and risk of HPV persistence and cervical precancer/cancer,” PLoS ONE, vol. 7, no. 4, Article ID e33619, 2012. View at Publisher · View at Google Scholar · View at Scopus
  209. J. K. Strzelczyk, T. Wielkoszyński, Ł. Krakowczyk et al., “The activity of antioxidant enzymes in colorectal adenocarcinoma and corresponding normal mucosa,” Acta Biochimica Polonica, vol. 59, no. 4, pp. 549–556, 2012. View at Google Scholar
  210. M. Scarpa, R. Cardin, M. Bortolami et al., “Mucosal immune environment in colonic carcinogenesis: CD80 expression is associated to oxidative DNA damage and TLR4-NFκB signalling,” European Journal of Cancer, vol. 49, no. 1, pp. 254–263, 2013. View at Google Scholar
  211. B. Thyagarajan, R. Wang, H. Barcelo et al., “Mitochondrial copy number is associated with colorectal cancer risk,” Cancer Epidemiology, Biomarkers and Prevention, vol. 21, no. 9, pp. 1574–1581, 2012. View at Google Scholar
  212. S. Pejić, A. Todorović, V. Stojiljković et al., “Antioxidant enzymes and lipid peroxidation in endometrium of patients with polyps, myoma, hyperplasia and adenocarcinoma,” Reproductive Biology and Endocrinology, vol. 7, article 149, 2009. View at Google Scholar
  213. A. Cormio, F. Guerra, G. Cormio et al., “The PGC-1α-dependent pathway of mitochondrial biogenesis is upregulated in type I endometrial cancer,” Biochemical and Biophysical Research Communications, vol. 390, no. 4, pp. 1182–1185, 2009. View at Publisher · View at Google Scholar · View at Scopus
  214. F. Guerra, I. Kurelac, A. Cormio et al., “Placing mitochondrial DNA mutations within the progression model of type I endometrial carcinoma,” Human Molecular Genetics, vol. 20, no. 12, pp. 2394–2405, 2011. View at Publisher · View at Google Scholar · View at Scopus
  215. J. Ni, M. Mei, and L. Sun, “Oxidative DNA damage and repair in chronic atrophic gastritis and gastric cancer,” Hepato-Gastroenterology, vol. 59, no. 115, pp. 671–675, 2012. View at Publisher · View at Google Scholar · View at Scopus
  216. T. Uehara, D. Ma, Y. Yao et al., “H. pylori infection is associated with DNA damage of Lgr5-positive epithelial stem cells in the stomach of patients with gastric cancer,” Digestive Diseases and Sciences, vol. 58, no. 1, pp. 140–149, 2013. View at Google Scholar
  217. A. M. Machado, C. Desler, S. Bøggild et al., “Helicobacter pylori infection affects mitochondrial function and DNA repair, thus, mediating genetic instability in gastric cells,” Mechanisms of Ageing and Development, vol. 134, no. 10, pp. 460–466, 2013. View at Google Scholar
  218. Y. Suzuki, K. Imai, K. Takai et al., “Hepatocellular carcinoma patients with increased oxidative stress levels are prone to recurrence after curative treatment: a prospective case series study using the d-ROM test,” The Journal of Cancer Research and Clinical Oncology, vol. 139, no. 5, pp. 845–852, 2013. View at Google Scholar
  219. S. Tanaka, K. Miyanishi, M. Kobune et al., “Increased hepatic oxidative DNA damage in patients with nonalcoholic steatohepatitis who develop hepatocellular carcinoma,” Journal of Gastroenterology, vol. 48, no. 11, pp. 1249–1258, 2013. View at Google Scholar
  220. T. Tamai, H. Uto, Y. Takami et al., “Serum manganese superoxide dismutase and thioredoxin are potential prognostic markers for hepatitis C virus-related hepatocellular carcinoma,” World Journal of Gastroenterology, vol. 17, no. 44, pp. 4890–4898, 2011. View at Publisher · View at Google Scholar · View at Scopus
  221. Y. Jin, Q. Yu, D. Zhou et al., “The mitochondrial DNA 9-bp deletion polymorphism is a risk factor for hepatocellular carcinoma in the Chinese population,” Genetic Testing and Molecular Biomarkers, vol. 16, no. 5, pp. 330–334, 2012. View at Google Scholar
  222. W. Duan, R. Hua, W. Yi et al., “The association between OGG1 Ser326Cys polymorphism and lung cancer susceptibility: a meta-analysis of 27 studies,” PLoS ONE, vol. 7, no. 4, Article ID e35970, 2012. View at Publisher · View at Google Scholar · View at Scopus
  223. U. Cobanoglu, H. Demir, A. Cebi et al., “Lipid peroxidation, DNA damage and coenzyme Q(10) in lung cancer patients—markers for risk assessment?” Asian Pacific Journal of Cancer Prevention, vol. 12, no. 6, pp. 1399–1403, 2011. View at Google Scholar · View at Scopus
  224. J. Janik, M. Swoboda, B. Janowska et al., “8-Oxoguanine incision activity is impaired in lung tissues of NSCLC patients with the polymorphism of OGG1 and XRCC1 genes,” Mutation Research—Fundamental and Molecular Mechanisms of Mutagenesis, vol. 709-710, pp. 21–31, 2011. View at Publisher · View at Google Scholar · View at Scopus
  225. J. R. Tsai, H. M. Wang, P. L. Liu et al., “High expression of heme oxygenase-1 is associated with tumor invasiveness and poor clinical outcome in non-small cell lung cancer patients,” Cell Oncology, vol. 35, no. 6, pp. 461–471, 2012. View at Google Scholar
  226. K. Ito, T. Yano, Y. Morodomi et al., “Serum antioxidant capacity and oxidative injury to pulmonary DNA in never-smokers with primary lung cancer,” Anticancer Research, vol. 32, no. 3, pp. 1063–1067, 2012. View at Google Scholar · View at Scopus
  227. X. Ye, Q. Li, G. Wang et al., “Mitochondrial and energy metabolism-related properties as novel indicators of lung cancer stem cells,” International Journal of Cancer, vol. 129, no. 4, pp. 820–831, 2011. View at Publisher · View at Google Scholar · View at Scopus
  228. Y. C. Chae, M. C. Caino, S. Lisanti et al., “Control of tumor bioenergetics and survival stress signaling by mitochondrial HSP90s,” Cancer Cell, vol. 22, no. 3, pp. 331–344, 2012. View at Google Scholar
  229. D. Murtas, F. Piras, L. Minerba et al., “Nuclear 8-hydroxy-2′-deoxyguanosine as survival biomarker in patients with cutaneous melanoma,” Oncology Reports, vol. 23, no. 2, pp. 329–335, 2010. View at Publisher · View at Google Scholar · View at Scopus
  230. M. Ibarrola-Villava, M. Peña-Chilet, L. P. Fernandez et al., “Genetic polymorphisms in DNA repair and oxidative stress pathways associated with malignant melanoma susceptibility,” European Journal of Cancer, vol. 47, no. 17, pp. 2618–2625, 2011. View at Publisher · View at Google Scholar · View at Scopus
  231. X. Lin, W. Zheng, J. Liu et al., “Oxidative stress in malignant melanoma enhances Tumor Necrosis Factor-α secretion of tumor-associated macrophages that promote cancer cell invasion,” Antioxidants and Redox Signaling, vol. 19, no. 12, pp. 1337–1355, 2013. View at Google Scholar
  232. M. Barbi de Moura, G. Vincent, S. L. Fayewicz et al., “Mitochondrial respiration—an important therapeutic target in melanoma,” PLoS ONE, vol. 7, no. 8, Article ID e40690, 2012. View at Google Scholar
  233. R. K. Singh, A. K. Tripathi, P. Tripathi, S. Singh, R. Singh, and R. Ahmad, “Studies on biomarkers for oxidative stress in patients with chronic myeloid leukemia,” Hematology/Oncology and Stem Cell Therapy, vol. 2, no. 1, pp. 285–288, 2009. View at Google Scholar · View at Scopus
  234. K. Sailaja, D. Surekha, D. Nageswara Rao, D. Raghunadha Rao, and S. Vishnupriya, “Association of the GSTP1 gene (Ile105Val) Polymorphism with chronic myeloid leukemia,” Asian Pacific Journal of Cancer Prevention, vol. 11, no. 2, pp. 461–464, 2010. View at Google Scholar · View at Scopus
  235. R. Ahmad, A. K. Tripathi, P. Tripathi, R. Singh, S. Singh, and R. K. Singh, “Studies on lipid peroxidation and non-enzymatic antioxidant status as indices of oxidative stress in patients with chronic myeloid leukaemia,” Singapore Medical Journal, vol. 51, no. 2, pp. 110–115, 2010. View at Google Scholar · View at Scopus
  236. F. Zhou, W. Zhang, Y. Wei et al., “Involvement of oxidative stress in the relapse of acute myeloid leukemia,” The Journal of Biological Chemistry, vol. 285, no. 20, pp. 15010–15015, 2010. View at Publisher · View at Google Scholar · View at Scopus
  237. K. K. Palande, R. Beekman, L. E. van der Meeren, H. Berna Beverloo, P. J. M. Valk, and I. P. Touw, “The antioxidant protein peroxiredoxin 4 is epigenetically down regulated in acute promyelocytic leukemia,” PLoS ONE, vol. 6, no. 1, Article ID e16340, 2011. View at Publisher · View at Google Scholar · View at Scopus
  238. A. Akinlolu, T. Akingbola, and B. Salau, “Lipid peroxidation in Nigerians affected with haematological malignancies,” African Journal of Medicine and Medical Sciences, vol. 41, supplement, pp. 145–148, 2012. View at Google Scholar
  239. J. Boultwood, C. Fidler, K. I. Mills et al., “Amplification of mitochondrial DNA in acute myeloid leukaemia,” British Journal of Haematology, vol. 95, no. 2, pp. 426–431, 1996. View at Google Scholar · View at Scopus
  240. P. Koistinen, S. Ruuska, M. Säily et al., “An association between manganese superoxide dismutase polymorphism and outcome of chemotherapy in acute myeloid leukemia,” Haematologica, vol. 91, no. 6, pp. 829–832, 2006. View at Google Scholar · View at Scopus
  241. V. Schildgen, M. Wulfert, and N. Gattermann, “Impaired mitochondrial gene transcription in myelodysplastic syndromes and acute myeloid leukemia with myelodysplasia-related changes,” Experimental Hematology, vol. 39, no. 6, pp. 666.e1–675.e1, 2011. View at Publisher · View at Google Scholar · View at Scopus
  242. S. Gokul, V. S. Patil, R. Jailkhani, K. Hallikeri, and K. K. Kattappagari, “Oxidant-antioxidant status in blood and tumor tissue of oral squamous cell carcinoma patients,” Oral Diseases, vol. 16, no. 1, pp. 29–33, 2010. View at Publisher · View at Google Scholar · View at Scopus
  243. S. D. Korde, A. Basak, M. Chaudhary, M. Goyal, and A. Vagga, “Enhanced nitrosative and oxidative stress with decreased total antioxidant capacity in patients with oral precancer and oral squamous cell carcinoma,” Oncology, vol. 80, no. 5-6, pp. 382–389, 2011. View at Publisher · View at Google Scholar · View at Scopus
  244. V. Marakala, M. Malathi, and A. R. Shivashankara, “Lipid peroxidation and antioxidant vitamin status in oral cavity and oropharyngeal cancer patients,” Asian Pacific Organization for Cancer Prevention, vol. 13, no. 11, pp. 5763–5765, 2012. View at Google Scholar
  245. B. Vlková, P. Stanko, G. Minárik et al., “Salivary markers of oxidative stress in patients with oral premalignant lesions,” Archives of Oral Biology, vol. 57, no. 12, pp. 1651–1656, 2012. View at Google Scholar
  246. S. Liu, R. Jiang, F. Chen, W. Wang, and J. Lin, “Somatic mutations in the D-loop of mitochondrial DNA in oral squamous cell carcinoma,” European Archives of Oto-Rhino-Laryngology, vol. 269, no. 6, pp. 1665–1670, 2012. View at Publisher · View at Google Scholar · View at Scopus
  247. G. Gasparre, A. M. Porcelli, E. Bonora et al., “Disruptive mitochondrial DNA mutations in complex I subunits are markers of oncocytic phenotype in thyroid tumors,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 21, pp. 9001–9006, 2007. View at Publisher · View at Google Scholar · View at Scopus
  248. E. Bonora, A. M. Porcelli, G. Gasparre et al., “Defective oxidative phosphorylation in thyroid oncocytic carcinoma is associated with pathogenic mitochondrial DNA mutations affecting complexes I and III,” Cancer Research, vol. 66, no. 12, pp. 6087–6096, 2006. View at Publisher · View at Google Scholar · View at Scopus
  249. S. Sciascia, D. Roccatello, M. T. Bertero et al., “8-isoprostane, prostaglandin E2, C-reactive protein and serum amyloid A as markers of inflammation and oxidative stress in antiphospholipid syndrome: a pilot study,” Inflammation Research, vol. 61, no. 8, pp. 809–816, 2012. View at Google Scholar
  250. C. Perez-Sanchez, P. Ruiz-Limon, M. A. Aguirre et al., “Mitochondrial dysfunction in antiphospholipid syndrome: implications in the pathogenesis of the disease and effects of coenzyme Q(10) treatment,” Blood, vol. 119, no. 24, pp. 5859–5870, 2012. View at Google Scholar
  251. M. Naziroğlu, I. Kökçam, H. Simşek et al., “Lipid peroxidation and antioxidants in plasma and red blood cells from patients with pemphigus vulgaris,” Journal of Basic and Cinical Physiology and Pharmacology, vol. 14, no. 1, pp. 31–42, 2003. View at Google Scholar
  252. O. Abida, R. Ben Mansour, B. Gargouri et al., “Catalase and lipid peroxidation values in serum of Tunisian patients with pemphigus vulgaris and foliaceus,” Biological Trace Element Research, vol. 150, no. 1–3, pp. 74–80, 2012. View at Google Scholar
  253. S. Marchenko, A. I. Chernyavsky, J. Arredondo, V. Gindi, and S. A. Grando, “Antimitochondrial autoantibodies in pemphigus vulgaris: a missing link in disease pathophysiology,” The Journal of Biological Chemistry, vol. 285, no. 6, pp. 3695–3704, 2010. View at Publisher · View at Google Scholar · View at Scopus
  254. M. Kalantari-Dehaghi, Y. Chen, W. Deng et al., “Mechanisms of mitochondrial damage in keratinocytes by pemphigus vulgaris antibodies,” The Journal of Biological Chemistry, vol. 288, no. 23, pp. 16916–16925, 2013. View at Google Scholar
  255. W. J. Cash, D. R. McCance, I. S. Young et al., “Primary biliary cirrhosis is associated with oxidative stress and endothelial dysfunction but not increased cardiovascular risk,” Hepatology Research, vol. 40, no. 11, pp. 1098–1106, 2010. View at Publisher · View at Google Scholar · View at Scopus
  256. P. Sorrentino, L. Terracciano, S. D'Angelo et al., “Oxidative stress and steatosis are cofactors of liver injury in primary biliary cirrhosis,” Journal of Gastroenterology, vol. 45, no. 10, pp. 1053–1062, 2010. View at Publisher · View at Google Scholar · View at Scopus
  257. T. L. Salunga, Z. Cui, S. Shimoda et al., “Oxidative stress-induced apoptosis of bile duct cells in primary biliary cirrhosis,” Journal of Autoimmunity, vol. 29, no. 2-3, pp. 78–86, 2007. View at Publisher · View at Google Scholar · View at Scopus
  258. P. S. C. Leung, L. Rossaro, P. A. Davis et al., “Antimitochondrial antibodies in acute liver failure: implications for primary biliary cirrhosis,” Hepatology, vol. 46, no. 5, pp. 1436–1442, 2007. View at Publisher · View at Google Scholar · View at Scopus
  259. K. H. Basavaraj, P. Vasu Devaraju, and K. S. Rao, “Studies on serum 8-hydroxy guanosine (8-OHdG) as reliable biomarker for psoriasis,” Journal of the European Academy of Dermatology and Venereology, vol. 27, no. 5, pp. 655–657, 2013. View at Publisher · View at Google Scholar · View at Scopus
  260. S. Kaur, K. Zilmer, V. Leping et al., “Serum methylglyoxal level and its association with oxidative stress and disease severity in patients with psoriasis,” Archives of Dermatological Research, vol. 305, no. 6, pp. 489–494, 2013. View at Google Scholar
  261. V. V. Barygina, M. Becatti, G. Soldi et al., “Altered redox status in the blood of psoriatic patients: involvement of NADPH oxidase and role of anti-TNF-α therapy,” Redox Reports, vol. 18, no. 3, pp. 100–106, 2013. View at Google Scholar
  262. S. A. Gabr and A. H. Al-Ghadir, “Role of cellular oxidative stress and cytochrome c in the pathogenesis of psoriasis,” Archives of Dermatological Research, vol. 304, no. 6, pp. 451–457, 2012. View at Publisher · View at Google Scholar · View at Scopus
  263. K. Stark, H. Törmä, and E. H. Oliw, “Co-localization of COX-2, CYP4F8, and mPGES-1 in epidermis with prominent expression of CYP4F8 mRNA in psoriatic lesions,” Prostaglandins and Other Lipid Mediators, vol. 79, no. 1-2, pp. 114–125, 2006. View at Publisher · View at Google Scholar · View at Scopus
  264. D. Shah, A. Wanchu, and A. Bhatnagar, “Interaction between oxidative stress and chemokines: possible pathogenic role in systemic lupus erythematosus and rheumatoid arthritis,” Immunobiology, vol. 216, no. 9, pp. 1010–1017, 2011. View at Publisher · View at Google Scholar · View at Scopus
  265. A. M. Connor, N. Mahomed, R. Gandhi, E. C. Keystone, and S. A. Berger, “TNFα modulates protein degradation pathways in rheumatoid arthritis synovial fibroblasts,” Arthritis Research and Therapy, vol. 14, no. 2, article R62, 2012. View at Publisher · View at Google Scholar · View at Scopus
  266. L. K. Stamp, I. Khalilova, J. M. Tarr et al., “Myeloperoxidase and oxidative stress in rheumatoid arthritis,” Rheumatology, vol. 51, no. 10, pp. 1796–1803, 2012. View at Google Scholar
  267. S. Kundu, P. Ghosh, S. Datta et al., “Oxidative stress as a potential biomarker for determining disease activity in patients with rheumatoid arthritis,” Free Radical Research, vol. 46, no. 12, pp. 1482–1489, 2012. View at Google Scholar
  268. S. Ahmad, S. Habib, and A. Moinuddin, “Preferential recognition of epitopes on AGE-IgG by the autoantibodies in rheumatoid arthritis patients,” Human Immunology, vol. 74, no. 1, pp. 23–27, 2013. View at Google Scholar
  269. L. C. Harty, M. Biniecka, J. O'Sullivan et al., “Mitochondrial mutagenesis correlates with the local inflammatory environment in arthritis,” Annals of the Rheumatic Diseases, vol. 71, no. 4, pp. 582–588, 2012. View at Publisher · View at Google Scholar · View at Scopus
  270. K. B. Norheim, G. Jonsson, E. Harboe, M. Hanasand, L. Gøransson, and R. Omdal, “Oxidative stress, as measured by protein oxidation, is increased in primary Sjøgren's syndrome,” Free Radical Research, vol. 46, no. 2, pp. 141–146, 2012. View at Publisher · View at Google Scholar · View at Scopus
  271. H. F. Cay, I. Sezer, S. Dogan et al., “Polymorphism in the TNF-α gene promoter at position −1031 is associated with increased circulating levels of TNF-α, myeloperoxidase and nitrotyrosine in primary Sjögren's Syndrome,” Clinical and Experimental Rheumatology, vol. 30, no. 6, pp. 843–849, 2012. View at Google Scholar
  272. K. Ryo, H. Yamada, Y. Nakagawa et al., “Possible involvement of oxidative stress in salivary gland of patients with Sjögren's syndrome,” Pathobiology, vol. 73, no. 5, pp. 252–260, 2007. View at Publisher · View at Google Scholar · View at Scopus
  273. C. Kurimoto, S. Kawano, G. Tsuji et al., “Thioredoxin may exert a protective effect against tissue damage caused by oxidative stress in salivary glands of patients with Sjögren's syndrome,” The Journal of Rheumatology, vol. 34, no. 10, pp. 2035–2043, 2007. View at Google Scholar · View at Scopus
  274. N. Ikuno, I. R. Mackay, J. Jois, K. Omagari, and M. J. Rowley, “Antimitochondrial autoantibodies in saliva and sera from patients with primary biliary cirrhosis,” Journal of Gastroenterology and Hepatology, vol. 16, no. 12, pp. 1390–1394, 2001. View at Publisher · View at Google Scholar · View at Scopus
  275. D. Fernandez, E. Bonilla, P. Phillips, and A. Perl, “Signaling abnormalities in systemic lupus erythematosus as potential drug targets,” Endocrine, Metabolic and Immune Disorders—Drug Targets, vol. 6, no. 4, pp. 305–311, 2006. View at Google Scholar · View at Scopus
  276. A. Perl, R. Hanczko, and E. Doherty, “Assessment of mitochondrial dysfunction in lymphocytes of patients with systemic lupus erythematosus,” Methods in Molecular Biology, vol. 900, pp. 61–89, 2012. View at Google Scholar
  277. I. Hassan, P. Sajad, S. Majid et al., “Serum antioxidant status in patients with systemic sclerosis,” Indian Journal of Dermatology, vol. 58, no. 3, p. 239, 2013. View at Google Scholar
  278. A. Zalewska, M. Knaś, E. Gińdzieńska-Sieśkiewicz et al., “Salivary antioxidants in patients with systemic sclerosis,” Journal of Oral Pathology and Medicine, vol. 43, no. 1, pp. 61–68, 2013. View at Publisher · View at Google Scholar
  279. M. P. Cruz-Domínguez, D. H. Montes-Cortes, I. M. Olivares-Corichi et al., “Oxidative stress in Mexicans with diffuse cutaneous systemic sclerosis,” Rheumatology International, vol. 33, no. 9, pp. 2261–2267, 2013. View at Google Scholar
  280. T. Ohtsuka, “Relation between elevated high-sensitivity C-reactive protein and anti-mitochondria antibody in patients with systemic sclerosis,” Journal of Dermatology, vol. 35, no. 2, pp. 70–75, 2008. View at Publisher · View at Google Scholar · View at Scopus
  281. V. A. Kostyuk, A. I. Potapovich, E. Cesareo et al., “Dysfunction of glutathione S-transferase leads to excess 4-hydroxy-2-nonenal and H(2)O(2) and impaired cytokine pattern in cultured keratinocytes and blood of vitiligo patients,” Antioxidants and Redox Signaling, vol. 13, no. 5, pp. 607–620, 2010. View at Publisher · View at Google Scholar · View at Scopus
  282. D. A. Bassiouny and M. M. Khorshied, “Glutathione S-transferase M1 and T1 genetic polymorphism in Egyptian patients with nonsegmental vitiligo,” Clinical and Experimental Dermatology, vol. 38, no. 2, pp. 160–163, 2013. View at Google Scholar
  283. M. L. Dell'Anna, M. Ottaviani, B. Bellei et al., “Membrane lipid defects are responsible for the generation of reactive oxygen species in peripheral blood mononuclear cells from vitiligo patients,” Journal of Cellular Physiology, vol. 223, no. 1, pp. 187–193, 2010. View at Publisher · View at Google Scholar · View at Scopus
  284. B. Heydari, T. Kazemi, A. Zarban et al., “Correlation of cataract with serum lipids, glucose and antioxidant activities: a case-control study,” West Indian Medical Journal, vol. 61, no. 3, pp. 230–234, 2012. View at Google Scholar
  285. B. Kisic, D. Miric, L. Zoric, A. Ilic, and I. Dragojevic, “Antioxidant capacity of lenses with age-related cataract,” Oxidative Medicine and Cellular Longevity, vol. 2012, Article ID 467130, 8 pages, 2012. View at Publisher · View at Google Scholar · View at Scopus
  286. Y. Zhang, L. Zhang, D. Sun, Z. Li, L. Wang, and P. Liu, “Genetic polymorphisms of superoxide dismutases, catalase, and glutathione peroxidase in age-related cataract,” Molecular Vision, vol. 17, pp. 2325–2332, 2011. View at Google Scholar · View at Scopus
  287. S. G. Jarrett, A. S. Lewin, and M. E. Boulton, “The importance of Mitochondria in age-related and inherited eye disorders,” Ophthalmic Research, vol. 44, no. 3, pp. 179–190, 2010. View at Publisher · View at Google Scholar · View at Scopus
  288. W. Lee, T. Wells, and M. Kantorow, “Localization and H(2)O(2)-specific induction of PRDX3 in the eye lens,” Molecular Vision, vol. 13, pp. 1469–1474, 2007. View at Google Scholar · View at Scopus
  289. S. Bagis, L. Tamer, G. Sahin et al., “Free radicals and antioxidants in primary fibromyalgia: an oxidative stress disorder?” Rheumatology International, vol. 25, no. 3, pp. 188–190, 2005. View at Publisher · View at Google Scholar · View at Scopus
  290. O. Altindag and H. Celik, “Total antioxidant capacity and the severity of the pain in patients with fibromyalgia,” Redox Report, vol. 11, no. 3, pp. 131–135, 2006. View at Publisher · View at Google Scholar · View at Scopus
  291. M. D. Cordero, E. Alcocer-Gómez, F. J. Cano-García et al., “Clinical symptoms in Fibromyalgia are better associated to lipid peroxidation levels in blood mononuclear cells rather than in plasma,” PLoS ONE, vol. 6, no. 10, Article ID e26915, 2011. View at Publisher · View at Google Scholar · View at Scopus
  292. M. D. Cordero, M. de Miguel, A. M. Moreno Fernández et al., “Mitochondrial dysfunction and mitophagy activation in blood mononuclear cells of fibromyalgia patients: implications in the pathogenesis of the disease,” Arthritis Research and Therapy, vol. 12, no. 1, article R17, 2010. View at Publisher · View at Google Scholar · View at Scopus
  293. M. D. Cordero, E. Díaz-Parrado, A. M. Carrión et al., “Is inflammation a mitochondrial dysfunction-dependent event in fibromyalgia?” Antioxidants and Redox Signaling, vol. 18, no. 7, pp. 800–807, 2013. View at Google Scholar
  294. S. Običan and A. R. Scialli, “Teratogenic exposures,” American Journal of Medical Genetics C: Seminars in Medical Genetics, vol. 157, no. 3, pp. 150–169, 2011. View at Publisher · View at Google Scholar · View at Scopus
  295. P. G. Wells, Y. Bhuller, C. S. Chen et al., “Molecular and biochemical mechanisms in teratogenesis involving reactive oxygen species,” Toxicology and Applied Pharmacology, vol. 207, no. 2, supplement, pp. S354–S366, 2005. View at Publisher · View at Google Scholar · View at Scopus
  296. P. Kovacic and R. Somanathan, “Mechanism of teratogenesis: electron transfer, reactive oxygen species, and antioxidants,” Birth Defects Research C—Embryo Today: Reviews, vol. 78, no. 4, pp. 308–325, 2006. View at Publisher · View at Google Scholar · View at Scopus
  297. X. Zheng, M. Su, L. Pei et al., “Metabolic signature of pregnant women with neural tube defects in offspring,” Journal of Proteome Research, vol. 10, no. 10, pp. 4845–4854, 2011. View at Publisher · View at Google Scholar · View at Scopus
  298. J. Dong, K. K. Sulik, and S. Chen, “The role of NOX enzymes in ethanol-induced oxidative stress and apoptosis in mouse embryos,” Toxicology Letters, vol. 193, no. 1, pp. 94–100, 2010. View at Publisher · View at Google Scholar · View at Scopus
  299. A. G. Fantel and R. E. Person, “Involvement of mitochondria and other free radical sources in normal and abnormal fetal development,” Annals of the New York Academy of Sciences, vol. 959, pp. 424–433, 2002. View at Google Scholar · View at Scopus
  300. Y. Xu, P. Liu, and Y. Li, “Impaired development of mitochondria plays a role in the central nervous system defects of fetal alcohol syndrome,” Birth Defects Research A—Clinical and Molecular Teratology, vol. 73, no. 2, pp. 83–91, 2005. View at Publisher · View at Google Scholar · View at Scopus
  301. D. Harman, “Aging: a theory based on free radical and radiation chemistry,” The Journal of Gerontology, vol. 11, no. 3, pp. 298–300, 1956. View at Google Scholar · View at Scopus
  302. D. Harman, “Free radical theory of aging: dietary implications,” The American Journal of Clinical Nutrition, vol. 25, no. 8, pp. 839–843, 1972. View at Google Scholar · View at Scopus
  303. K. Przyklenk and R. A. Kloner, “Effect of oxygen-derived free radical scavengers on infarct size following six hours of permanent coronary artery occlusion: salvage or delay of myocyte necrosis?” Basic Research in Cardiology, vol. 82, no. 2, pp. 146–158, 1987. View at Google Scholar · View at Scopus
  304. S. P. Wolff, Z. A. Bascal, and J. V. Hunt, “‘Autoxidative glycosylation’: free radicals and glycation theory,” Progress in Clinical and Biological Research, vol. 304, pp. 259–275, 1989. View at Google Scholar · View at Scopus
  305. J. Clausen, “Demential syndromes and the lipid metabolism,” Acta Neurologica Scandinavica, vol. 70, no. 5, pp. 345–355, 1984. View at Google Scholar · View at Scopus
  306. F. P. Zemlan, O. J. Thienhaus, and H. B. Bosmann, “Superoxide dismutase activity in Alzheimer's disease: possible mechanism for paired helical filament formation,” Brain Research, vol. 476, no. 1, pp. 160–162, 1989. View at Google Scholar · View at Scopus
  307. C. Vives-Bauza and S. Przedborski, “Mitophagy: the latest problem for Parkinson's disease,” Trends in Molecular Medicine, vol. 17, no. 3, pp. 158–165, 2011. View at Publisher · View at Google Scholar · View at Scopus
  308. E. Wołyniec, J. Karpińska, S. Losiewska et al., “Determination of lipoic acid by flow-injection and high-performance liquid chromatography with chemiluminescence detection,” Talanta, vol. 96, pp. 223–229, 2012. View at Google Scholar
  309. G. Pagano and G. Castello, “Oxidative stress and mitochondrial dysfunction in down syndrome,” Advances in Experimental Medicine and Biology, vol. 724, pp. 291–299, 2012. View at Publisher · View at Google Scholar · View at Scopus
  310. J. Liu, “The effects and mechanisms of mitochondrial nutrient alpha-lipoic acid on improving age-associated mitochondrial and cognitive dysfunction: an overview,” Neurochemical Research, vol. 33, no. 1, pp. 194–203, 2008. View at Google Scholar
  311. M. A. Tarnopolsky, “The mitochondrial cocktail: rationale for combined nutraceutical therapy in mitochondrial cytopathies,” Advanced Drug Delivery Reviews, vol. 60, no. 13-14, pp. 1561–1567, 2008. View at Publisher · View at Google Scholar · View at Scopus
  312. C. J. McMackin, M. E. Widlansky, N. M. Hamburg et al., “Effect of combined treatment with alpha-Lipoic acid and acetyl-L-carnitine on vascular function and blood pressure in patients with coronary artery disease,” Journal of Clinical Hypertension, vol. 9, no. 4, pp. 249–255, 2007. View at Google Scholar · View at Scopus
  313. S. Parikh, A. Goldstein, M. K. Koenig et al., “Practice patterns of mitochondrial disease physicians in North America, part 2: treatment, care and management,” Mitochondrion, vol. 13, no. 6, pp. 681–687, 2013. View at Google Scholar
  314. G. Pagano, A. Aiello Talamanca, G. Castello et al., “Mitochondrial nutrients in disorders featuring oxidative stress and mitochondrial dysfunction: current experience and rational design of chemoprevention trials,” Submitted.