Table of Contents Author Guidelines Submit a Manuscript
Oxidative Medicine and Cellular Longevity
Volume 2013, Article ID 931251, 8 pages
http://dx.doi.org/10.1155/2013/931251
Review Article

Evidence in Support of Potential Applications of Lipid Peroxidation Products in Cancer Treatment

Department of Pharmacology, School of Medical Sciences, Universiti Sains Malaysia, 16150 Kubang Kerian, Kelantan, Malaysia

Received 18 May 2013; Revised 2 November 2013; Accepted 8 November 2013

Academic Editor: Peter Shaw

Copyright © 2013 Omotayo O. Erejuwa 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. V. Shulaev and D. J. Oliver, “Metabolic and proteomic markers for oxidative stress: new tools for reactive oxygen species research,” Plant Physiology, vol. 141, no. 2, pp. 367–372, 2006. View at Publisher · View at Google Scholar · View at Scopus
  2. Y. Yoshida, A. Umeno, and M. Shichiri, “Lipid peroxidation biomarkers for evaluating oxidative stress and assessing antioxidant capacity in vivo,” Journal of Clinical Biochemistry and Nutrition, vol. 52, no. 1, pp. 9–16, 2013. View at Google Scholar
  3. D. Matveychuk, S. M. Dursun, P. L. Wood, and G. B. Baker, “Reactive aldehydes and neurodegenerative disorders,” Bulletin of Clinical Psychopharmacology, vol. 21, no. 4, pp. 277–288, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. A. Catalá, “A synopsis of the process of lipid peroxidation since the discovery of the essential fatty acids,” Biochemical and Biophysical Research Communications, vol. 399, no. 3, pp. 318–323, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. 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
  6. D. A. Butterfield, M. L. Bader Lange, and R. Sultana, “Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease,” Biochimica et Biophysica Acta, vol. 1801, no. 8, pp. 924–929, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. M. Fukuda, F. Kanou, N. Shimada et al., “Elevated levels of 4-hydroxynonenal-histidine Michael adduct in the hippocampi of patients with Alzheimer's disease,” Biomedical Research, vol. 30, no. 4, pp. 227–233, 2009. View at Publisher · View at Google Scholar · View at Scopus
  8. A. Höhn and T. Grune, “Lipofuscin: formation, effects and role of macroautophagy,” Redox Biology, vol. 1, no. 1, pp. 140–144, 2013. View at Google Scholar
  9. O. O. Erejuwa, S. A. Sulaiman, M. S. Ab Wahab, K. N. S. Sirajudeen, S. Salleh, and S. Gurtu, “Honey supplementation in spontaneously hypertensive rats elicits antihypertensive effect via amelioration of renal oxidative stress,” Oxidative Medicine and Cellular Longevity, vol. 2012, Article ID 374037, 14 pages, 2012. View at Publisher · View at Google Scholar · View at Scopus
  10. D. A. Butterfield, V. Galvan, M. B. Lange et al., “In vivo oxidative stress in brain of Alzheimer disease transgenic mice: requirement for methionine 35 in amyloid β-peptide of APP,” Free Radical Biology and Medicine, vol. 48, no. 1, pp. 136–144, 2010. View at Publisher · View at Google Scholar · View at Scopus
  11. D. Zanini, R. Schmatz, L. P. Pelinson et al., “Ectoenzymes and cholinesterase activity and biomarkers of oxidative stress in patients with lung cancer,” Molecular and Cellular Biochemistry, vol. 374, no. 1-2, pp. 137–148, 2013. View at Google Scholar
  12. O. O. Erejuwa, S. A. Sulaiman, M. S. Wahab, S. K. N. Salam, M. S. Salleh, and S. Gurtu, “Comparison of antioxidant effects of honey, glibenclamide, metformin, and their combinations in the kidneys of streptozotocin-induced diabetic rats,” International Journal of Molecular Sciences, vol. 12, no. 1, pp. 829–843, 2011. View at Publisher · View at Google Scholar · View at Scopus
  13. D. Tsikas, M. T. Suchy, J. Niemann et al., “Glutathione promotes prostaglandin H synthase (cyclooxygenase)-dependent formation of malondialdehyde and 15(S)-8-iso-prostaglandin F2alpha,” FEBS Letters, vol. 586, no. 20, pp. 3723–3730, 2012. View at Google Scholar
  14. M. Guichardant, P. Chen, M. Liu et al., “Functional lipidomics of oxidized products from polyunsaturated fatty acids,” Chemistry and Physics of Lipids, vol. 164, no. 6, pp. 544–548, 2011. View at Publisher · View at Google Scholar · View at Scopus
  15. A. C. Gasparovic, M. Jaganjac, B. Mihaljevic, S. B. Sunjic, and N. Zarkovic, “Assays for the measurement of lipid peroxidation,” Methods Molecular Biology, vol. 965, pp. 283–296, 2013. View at Google Scholar
  16. Z. Feng, W. Hu, L. J. Marnett, and M.-S. Tang, “Malondialdehyde, a major endogenous lipid peroxidation product, sensitizes human cells to UV- and BPDE-induced killing and mutagenesis through inhibition of nucleotide excision repair,” Mutation Research, vol. 601, no. 1-2, pp. 125–136, 2006. View at Publisher · View at Google Scholar · View at Scopus
  17. L. J. Niedernhofer, J. S. Daniels, C. A. Rouzer, R. E. Greene, and L. J. Marnett, “Malondialdehyde: a product of lipid peroxidation, is mutagenic in human cells,” Journal of Biological Chemistry, vol. 278, no. 33, pp. 31426–31433, 2003. View at Publisher · View at Google Scholar · View at Scopus
  18. D. Grotto, L. Santa Maria, J. Valentini et al., “Importance of the lipid peroxidation biomarkers and methodological aspects for malondialdehyde quantification,” Quimica Nova, vol. 32, no. 1, pp. 169–174, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. A. Catalá, “Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions,” Chemistry and Physics of Lipids, vol. 157, no. 1, pp. 1–11, 2009. View at Publisher · View at Google Scholar · View at Scopus
  20. T. T. Reed, W. M. Pierce, W. R. Markesbery, and D. A. Butterfield, “Proteomic identification of HNE-bound proteins in early Alzheimer disease: insights into the role of lipid peroxidation in the progression of AD,” Brain Research, vol. 1274, pp. 66–76, 2009. View at Publisher · View at Google Scholar · View at Scopus
  21. M. Perluigi, R. Coccia, and D. A. Butterfield, “4-Hydroxy-2-nonenal, a reactive product of lipid peroxidation, and neurodegenerative diseases: a toxic combination illuminated by redox proteomics studies,” Antioxidants and Redox Signaling, vol. 17, no. 11, pp. 1590–1609, 2012. View at Google Scholar
  22. J. N. Keller, Z. Pang, J. W. Geddes et al., “Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid β-peptide: role of the lipid peroxidation product 4-hydroxynonenal,” Journal of Neurochemistry, vol. 69, no. 1, pp. 273–284, 1997. View at Google Scholar · View at Scopus
  23. M. D. Neely, A. Boutte, D. Milatovic, and T. J. Montine, “Mechanisms of 4-hydroxynonenal-induced neuronal microtubule dysfunction,” Brain Research, vol. 1037, no. 1-2, pp. 90–98, 2005. View at Publisher · View at Google Scholar · View at Scopus
  24. M. M. Anderson, S. L. Hazen, F. F. Hsu, and J. W. Heinecke, “Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein: a mechanism for the generation of highly reactive α-hydroxy and α,β-unsaturated aldehydes by phagocytes at sites of inflammation,” Journal of Clinical Investigation, vol. 99, no. 3, pp. 424–432, 1997. View at Google Scholar · View at Scopus
  25. M. Nakamura, H. Tomitori, T. Suzuki et al., “Inactivation of GAPDH as one mechanism of acrolein toxicity,” Biochemical and Biophysical Research Communications, vol. 430, no. 4, pp. 1265–1271, 2013. View at Google Scholar
  26. Y. J. Huang, M. H. Jin, R. B. Pi et al., “Acrolein induces Alzheimer's disease-like pathologies in vitro and in vivo,” Toxicology Letters, vol. 217, no. 3, pp. 184–191, 2013. View at Google Scholar
  27. J. D. Morrow, K. E. Hill, R. F. Burk, T. M. Nammour, K. F. Badr, and L. J. Roberts II, “A series of prostaglandin F2-like compounds are produced in vivo in humans by a non-cyclooxygenase, free radical-catalyzed mechanism,” Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 23, pp. 9383–9387, 1990. View at Publisher · View at Google Scholar · View at Scopus
  28. D. Il'yasova, P. Scarbrough, and I. Spasojevic, “Urinary biomarkers of oxidative status,” Clinica Chimica Acta, vol. 413, no. 19-20, pp. 1446–1453, 2012. View at Google Scholar
  29. S. Basu, “F2-isoprostanes in human health and diseases: from molecular mechanisms to clinical implications,” Antioxidants and Redox Signaling, vol. 10, no. 8, pp. 1405–1434, 2008. View at Publisher · View at Google Scholar · View at Scopus
  30. T. J. Montine, K. S. Montine, W. McMahan, W. R. Markesbery, J. F. Quinn, and J. D. Morrow, “F2-isoprostanes in Alzheimer and other neurodegenerative diseases,” Antioxidants and Redox Signaling, vol. 7, no. 1-2, pp. 269–275, 2005. View at Publisher · View at Google Scholar · View at Scopus
  31. M. B. Kadiiska, B. C. Gladen, D. D. Baird et al., “Biomarkers of oxidative stress study. II: are oxidation products of lipids, proteins, and DNA markers of CCl4 poisoning?” Free Radical Biology and Medicine, vol. 38, no. 6, pp. 698–710, 2005. View at Publisher · View at Google Scholar · View at Scopus
  32. J. P. Fessel, N. A. Porter, K. P. Moore, J. R. Sheller, and L. J. Roberts II, “Discovery of lipid peroxidation products formed in vivo with a substituted tetrahydrofuran ring (isofurans) that are favored by increased oxygen tension,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 26, pp. 16713–16718, 2002. View at Publisher · View at Google Scholar · View at Scopus
  33. K. S. Montine, J. F. Quinn, J. Zhang et al., “Isoprostanes and related products of lipid peroxidation in neurodegenerative diseases,” Chemistry and Physics of Lipids, vol. 128, no. 1-2, pp. 117–124, 2004. View at Publisher · View at Google Scholar · View at Scopus
  34. A. Corcoran and T. G. Cotter, “Redox regulation of protein kinases,” FEBS Journal, vol. 280, no. 9, pp. 1944–1965, 2013. View at Publisher · View at Google Scholar
  35. E. Mas, A. E. Barden, T. B. Corcoran, M. Phillips, L. J. Roberts II, and T. A. Mori, “Effects of spinal or general anesthesia on F2-isoprostanes and isofurans during ischemia/reperfusion of the leg in patients undergoing knee replacement surgery,” Free Radical Biology and Medicine, vol. 50, no. 9, pp. 1171–1176, 2011. View at Publisher · View at Google Scholar · View at Scopus
  36. K. O. Arneson and L. J. Roberts II, “Measurement of products of docosahexaenoic acid peroxidation, neuroprostanes, and neurofurans,” Methods in Enzymology, vol. 433, pp. 127–143, 2007. View at Publisher · View at Google Scholar · View at Scopus
  37. H. A. Powell, B. Iyen-Omofoman, R. B. Hubbard, D. R. Baldwin, and L. J. Tata, “The association between smoking quantity and lung cancer in men and women,” Chest, vol. 143, no. 1, pp. 123–129, 2013. View at Google Scholar
  38. D. Schottenfeld, J. L. Beebe-Dimmer, P. A. Buffler, and G. S. Omenn, “Current perspective on the global and United States cancer burden attributable to lifestyle and environmental risk factors,” Annual Review of Public Health, vol. 34, pp. 97–117, 2013. View at Google Scholar
  39. B. D'Autreaux and M. B. Toledano, “ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis,” Nature Reviews Molecular Cell Biology, vol. 8, pp. 813–824, 2007. View at Google Scholar
  40. E. S. Kandel, “Mutations in circulating mitochondrial DNA: cassandra of oral cancer?” Oncotarget, vol. 3, no. 7, pp. 664–665, 2012. View at Google Scholar
  41. L. Fendt, H. Niederstätter, G. Huber et al., “Accumulation of mutations over the entire mitochondrial genome of breast cancer cells obtained by tissue microdissection,” Breast Cancer Research and Treatment, vol. 128, no. 2, pp. 327–336, 2011. View at Publisher · View at Google Scholar · View at Scopus
  42. H. Cui, Y. Kong, and H. Zhang, “Oxidative stress, mitochondrial dysfunction, and aging,” Journal of Signal Transduction, vol. 2012, Article ID 646354, 13 pages, 2012. View at Publisher · View at Google Scholar
  43. D. Trachootham, J. Alexandre, and P. Huang, “Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach?” Nature Reviews Drug Discovery, vol. 8, no. 7, pp. 579–591, 2009. View at Publisher · View at Google Scholar · View at Scopus
  44. M. S. Rodrigues, M. M. Reddy, and M. Sattler, “Cell cycle regulation by oncogenic tyrosine kinases in myeloid neoplasias: from molecular redox mechanisms to health implications,” Antioxidants and Redox Signaling, vol. 10, no. 10, pp. 1813–1848, 2008. View at Publisher · View at Google Scholar · View at Scopus
  45. V. Peddireddy, B. Siva Prasad, S. D. Gundimeda, P. R. Penagaluru, and H. P. Mundluru, “Assessment of 8-oxo-7, 8-dihydro-2′-deoxyguanosine and malondialdehyde levels as oxidative stress markers and antioxidant status in non-small cell lung cancer,” Biomarkers, vol. 17, no. 3, pp. 261–268, 2012. View at Publisher · View at Google Scholar · View at Scopus
  46. M. L. Balestrieri, A. Dicitore, R. Benevento et al., “Interplay between membrane lipid peroxidation, transglutaminase activity, and Cyclooxygenase 2 expression in the tissue adjoining to breast cancer,” Journal of Cellular Physiology, vol. 227, no. 4, pp. 1577–1582, 2012. View at Publisher · View at Google Scholar · View at Scopus
  47. S. S. Bhagat, R. A. Ghone, A. N. Suryakar, and P. S. Hundekar, “Lipid peroxidation and antioxidant vitamin status in colorectal cancer patients,” Indian Journal of Physiology and Pharmacology, vol. 55, no. 1, pp. 72–76, 2011. View at Google Scholar · View at Scopus
  48. M. O. Dillioglugil, H. Mekik, B. Muezzinoglu, T. A. Ozkan, C. G. Demir, and O. Dillioglugil, “Blood and tissue nitric oxide and malondialdehyde are prognostic indicators of localized prostate cancer,” International Urology and Nephrology, vol. 44, no. 6, pp. 1691–1696, 2012. View at Google Scholar
  49. V. Marakala, M. Malathi, and A. R. Shivashankara, “Lipid peroxidation and antioxidant vitamin status in oral cavity and oropharyngeal cancer patients,” Asian Pacific Journal of Cancer Prevention, vol. 13, no. 11, pp. 5763–5765, 2012. View at Google Scholar
  50. H. Czeczot, D. Scibior-Bentkowska, M. Skrzycki, and M. Podsiad, “Assessment of lipid peroxidation level in serum of patients with gastrointestinal tract tumors,” Wiadomości Lekarskie, vol. 63, no. 3, pp. 180–187, 2010. View at Google Scholar · View at Scopus
  51. M. Epplein, A. A. Franke, R. V. Cooney et al., “Association of plasma micronutrient levels and urinary isoprostane with risk of lung cancer: the multiethnic cohort study,” Cancer Epidemiology Biomarkers and Prevention, vol. 18, no. 7, pp. 1962–1970, 2009. View at Publisher · View at Google Scholar · View at Scopus
  52. D. A. Barocas, S. Motley, M. S. Cookson et al., “Oxidative stress measured by urine F2-isoprostane level is associated with prostate cancer,” Journal of Urology, vol. 185, no. 6, pp. 2102–2107, 2011. View at Publisher · View at Google Scholar · View at Scopus
  53. A. W. Asombang, V. Kayamba, M. Mwanza-Lisulo et al., “Gastric cancer in Zambian adults: a prospective case-control study that assessed dietary intake and antioxidant status by using urinary isoprostane excretion,” The American Journal of Clinical Nutrition, vol. 97, no. 5, pp. 1029–1035, 2013. View at Publisher · View at Google Scholar
  54. E. Germain, V. Chajes, S. Cognault, C. Lhuillery, and P. Bougnoux, “Enhancement of doxorubicin cytotoxicity by polyunsaturated fatty acids in the human breast tumor cell line MDA-MB-231: relationship to lipid peroxidation,” International Journal of Cancer, vol. 75, no. 4, pp. 578–583, 1998. View at Google Scholar
  55. X. X. Wu, O. Ogawa, and Y. Kakehi, “Enhancement of arsenic trioxide-induced apoptosis in renal cell carcinoma cells by L-buthionine sulfoximine,” International Journal of Oncology, vol. 24, no. 6, pp. 1489–1497, 2004. View at Google Scholar · View at Scopus
  56. M. Baumgartner, S. Sturlan, E. Roth, B. Wessner, and T. Bachleitner-Hofmann, “Enhancement of arsenic trioxide-mediated apoptosis using docosahexaenoic acid in arsenic trioxide-resistant solid tumor cells,” International Journal of Cancer, vol. 112, no. 4, pp. 707–712, 2004. View at Publisher · View at Google Scholar · View at Scopus
  57. J. F. Fahrmann and W. E. Hardman, “Omega 3 fatty acids increase the chemo-sensitivity of B-CLL-derived cell lines EHEB and MEC-2 and of B-PLL-derived cell line JVM-2 to anti-cancer drugs doxorubicin, vincristine and fludarabine,” Lipids in Health and Disease, vol. 12, article 36, 2013. View at Google Scholar
  58. G. Benais-Pont, Y. M. Dupertuis, M. P. Kossovsky et al., “ω-3 Polyunsaturated fatty acids and ionizing radiation: combined cytotoxicity on human colorectal adenocarcinoma cells,” Nutrition, vol. 22, no. 9, pp. 931–939, 2006. View at Publisher · View at Google Scholar · View at Scopus
  59. P. K. Rudra and H. E. Krokan, “Acrolein cytotoxicity and glutathione depletion in n-3 fatty acid sensitive- and resistant human tumor cells,” Anticancer Research, vol. 19, no. 1, pp. 461–469, 1999. View at Google Scholar · View at Scopus
  60. E. S. Yang, S. M. Woo, K. S. Choi, and T. K. Kwon, “Acrolein sensitizes human renal cancer Caki cells to TRAIL-induced apoptosis via ROS-mediated up-regulation of death receptor-5 (DR5) and down-regulation of Bcl-2,” Experimental Cell Research, vol. 317, no. 18, pp. 2592–2601, 2011. View at Publisher · View at Google Scholar · View at Scopus
  61. P. Pettazzoni, S. Pizzimenti, C. Toaldo et al., “Induction of cell cycle arrest and DNA damage by the HDAC inhibitor panobinostat (LBH589) and the lipid peroxidation end product 4-hydroxynonenal in prostate cancer cells,” Free Radical Biology and Medicine, vol. 50, no. 2, pp. 313–322, 2011. View at Publisher · View at Google Scholar · View at Scopus
  62. M. Nagai, N. H. Vo, L. Shin Ogawa et al., “The oncology drug elesclomol selectively transports copper to the mitochondria to induce oxidative stress in cancer cells,” Free Radical Biology and Medicine, vol. 52, no. 10, pp. 2142–2150, 2012. View at Google Scholar
  63. A. Rasul, R. Bao, M. Malhi et al., “Induction of apoptosis by costunolide in bladder cancer cells is mediated through ROS generation and mitochondrial dysfunction,” Molecules, vol. 18, no. 2, pp. 1418–1433, 2013. View at Google Scholar
  64. S. Zhang, Y. He, Q. Tong, Q. Chen, X. Wu, and W. Huang, “Deltonin induces apoptosis in MDAMB231 human breast cancer cells via reactive oxygen speciesmediated mitochondrial dysfunction and ERK/AKT signaling pathways,” Molecular Medicine Reports, vol. 7, no. 3, pp. 1038–1044, 2013. View at Google Scholar
  65. M. J. Gonzalez, R. A. Schemmel, J. I. Gray, L. Dugan Jr., L. G. Sheffield, and C. W. Welsch, “Effect of dietary fat on growth of MCF-7 and MDA-MB231 human breast carcinomas in athymic nude mice: relationship between carcinoma growth and lipid peroxidation product levels,” Carcinogenesis, vol. 12, no. 7, pp. 1231–1235, 1991. View at Google Scholar · View at Scopus
  66. Y. Shao, L. Pardini, and R. S. Pardini, “Dietary menhaden oil enhances mitomycin C antitumor activity toward human mammary carcinoma MX-1,” Lipids, vol. 30, no. 11, pp. 1035–1045, 1995. View at Publisher · View at Google Scholar · View at Scopus
  67. T. Tsuzuki, Y. Tokuyama, M. Igarashi, and T. Miyazawa, “Tumor growth suppression by α-eleostearic acid, a linolenic acid isomer with a cunjugated triene system, via lipid peroxidation,” Carcinogenesis, vol. 25, no. 8, pp. 1417–1425, 2004. View at Publisher · View at Google Scholar · View at Scopus
  68. S. Kumar, R. A. Kokate, M. Sahu et al., “Inhibition of mercapturic acid pathway-mediated disposal of 4-hydroxynonenal causes complete and sustained remission of human cancer xenografts in nude mice,” Indian Journal of Experimental Biology, vol. 49, no. 11, pp. 817–825, 2011. View at Google Scholar · View at Scopus
  69. R. Salzman, L. Pácal, J. Tomandl et al., “Elevated malondialdehyde correlates with the extent of primary tumor and predicts poor prognosis of oropharyngeal cancer,” Anticancer Research, vol. 29, no. 10, pp. 4227–4231, 2009. View at Google Scholar · View at Scopus
  70. R. H. Chole, R. N. Patil, A. Basak, K. Palandurkar, and R. Bhowate, “Estimation of serum malondialdehyde in oral cancer and precancer and its association with healthy individuals, gender, alcohol, and tobacco abuse,” Journal of Cancer Research and Therapeutics, vol. 6, no. 4, pp. 487–491, 2010. View at Publisher · View at Google Scholar · View at Scopus
  71. 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
  72. P. Karihtala, S. Kauppila, U. Puistola, and A. Jukkola-Vuorinen, “Divergent behaviour of oxidative stress markers 8-hydroxydeoxyguanosine (8-OHdG) and 4-hydroxy-2-nonenal (HNE) in breast carcinogenesis,” Histopathology, vol. 58, no. 6, pp. 854–862, 2011. View at Publisher · View at Google Scholar · View at Scopus
  73. L. M. Mosina, T. V. Tarasova, E. M. Soldatova, S. M. Chibisov, O. I. Avdeǐkina, and A. A. Kotliarov, “Parameters of oxidative stress in patients with gastric cancer,” Klinicheskaia Meditsina, vol. 89, no. 3, pp. 50–53, 2011. View at Google Scholar · View at Scopus
  74. P. Misthos, S. Katsaragakis, N. Milingos et al., “Postresectional pulmonary oxidative stress in lung cancer patients. The role of one-lung ventilation,” European Journal of Cardio-thoracic Surgery, vol. 27, no. 3, pp. 379–383, 2005. View at Publisher · View at Google Scholar · View at Scopus
  75. B. Surinenaite, G. Prasmickiene, V. Milašiene, E. Stratilatovas, and J. Didžiapetriene, “The influence of surgical treatment and red blood cell transfusion on changes in antioxidative and immune system parameters in colorectal cancer patients,” Medicina, vol. 45, no. 10, pp. 785–791, 2009. View at Google Scholar · View at Scopus
  76. D. Liu and Y. Xu, “P53: oxidative stress, and aging,” Antioxidants and Redox Signaling, vol. 15, no. 6, pp. 1669–1678, 2011. View at Publisher · View at Google Scholar · View at Scopus
  77. J. Wei, E. Zaika, and A. Zaika, “p53 family: role of protein isoforms in human cancer,” Journal of Nucleic Acids, vol. 2012, Article ID 687359, 19 pages, 2012. View at Publisher · View at Google Scholar
  78. S. Laurora, E. Tamagno, F. Briatore et al., “4-Hydroxynonenal modulation of p53 family gene expression in the SK-N-BE neuroblastoma cell line,” Free Radical Biology and Medicine, vol. 38, no. 2, pp. 215–225, 2005. View at Publisher · View at Google Scholar · View at Scopus
  79. K. A. Lewis and D. S. Wuttke, “Telomerase and telomere-associated proteins: structural insights into mechanism and evolution,” Structure, vol. 20, no. 1, pp. 28–39, 2012. View at Publisher · View at Google Scholar · View at Scopus
  80. S. Pizzimenti, F. Briatore, S. Laurora et al., “4-Hydroxynonenal inhibits telomerase activity and hTERT expression in human leukemic cell lines,” Free Radical Biology and Medicine, vol. 40, no. 9, pp. 1578–1591, 2006. View at Publisher · View at Google Scholar · View at Scopus
  81. S. Pizzimenti, E. Menegatti, D. Berardi et al., “4-Hydroxynonenal, a lipid peroxidation product of dietary polyunsaturated fatty acids, has anticarcinogenic properties in colon carcinoma cell lines through the inhibition of telomerase activity,” Journal of Nutritional Biochemistry, vol. 21, no. 9, pp. 818–826, 2010. View at Publisher · View at Google Scholar · View at Scopus
  82. T. Berg, “Small-molecule modulators of c-Myc/Max and Max/Max interactions,” Current Topics in Microbiology and Immunology, vol. 348, pp. 139–149, 2011. View at Publisher · View at Google Scholar · View at Scopus
  83. J. R. Whitfield and L. Soucek, “Tumor microenvironment: becoming sick of Myc,” Cellular and Molecular Life Sciences, vol. 69, no. 6, pp. 931–934, 2012. View at Publisher · View at Google Scholar · View at Scopus
  84. C. V. Dang, “MYC on the path to cancer,” Cell, vol. 149, no. 1, pp. 22–35, 2012. View at Publisher · View at Google Scholar · View at Scopus
  85. O. Vafa, M. Wade, S. Kern et al., “c-Myc can induce DNA damage, increase reactive oxygen species, and mitigate p53 function: a mechanism for oncogene-induced genetic instability,” Molecular Cell, vol. 9, no. 5, pp. 1031–1044, 2002. View at Publisher · View at Google Scholar · View at Scopus