Journal of Biomedicine and Biotechnology
Volume 2009 (2009), Article ID 791432, 6 pages
doi:10.1155/2009/791432
Research Article
Protective Effect of Melatonin Against Mitomycin C-Induced Genotoxic Damage in Peripheral Blood of Rats
1Department of Pharmacology and Physiology, University of Zaragoza, 50009 Zaragoza, Spain
2Departments of Neurology and Medicine, Medical College of Wisconsin, Milwaakee, WI 53226, USA
3Department of Family and Community Medicine, Medical College of Wisconsin, Milwaakee, WI 53226, USA
4Department of Human Anatomy and Histology, University of Zaragoza, 50009 Zaragoza, Spain
Received 22 May 2009; Accepted 5 August 2009
Academic Editor: Gary S. Stein
Copyright © 2009 S. Ortega-Gutiérrez 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
- C. Asche, “Antitumour quinones,” Mini-Reviews in Medicinal Chemistry, vol. 5, no. 5, pp. 449–467, 2005. View at Publisher · View at Google Scholar · View at Scopus
- M. Tomasz and Y. Palom, “The mitomycin bioreductive antitumor agents: cross-linking and alkylation of DNA as the molecular basis of their activity,” Pharmacology and Therapeutics, vol. 76, no. 1–3, pp. 73–87, 1997. View at Publisher · View at Google Scholar · View at Scopus
- Y. Palom, G. Suresh Kumar, L.-Q. Tang, et al., “Relative toxicities of DNA cross-links and monoadducts: new insights from studies of decarbamoyl mitomycin C and mitomycin C,” Chemical Research in Toxicology, vol. 15, no. 11, pp. 1398–1406, 2002. View at Publisher · View at Google Scholar · View at Scopus
- M. M. Paz, G. S. Kumar, M. Glover, M. J. Waring, and M. Tomasz, “Mitomycin dimers: polyfunctional cross-linkers of DNA,” Journal of Medicinal Chemistry, vol. 47, no. 12, pp. 3308–3319, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Y.-J. Lee, S.-J. Park, S. L. M. Ciccone, C.-R. Kim, and S.-H. Lee, “An in vivo analysis of MMC-induced DNA damage and its repair,” Carcinogenesis, vol. 27, no. 3, pp. 446–453, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. Powis, “Free radical formation by antitumor quinines,” Free Radicals in Biology and Medicine, vol. 6, pp. 63–101, 1989.
- P. L. Gutiérrez, “The metabolism of quinine-containing alkylating agents: free radical production and measurement,” Frontiers in Biosciences, vol. 5, pp. 629–638, 2000.
- S. Wakaki, H. Marumo, K. Tomiaka, et al., “Isolation of new fractions of antitumor mitomycin,” Antibiotics & Chemotherary, vol. 8, pp. 228–240, 1958.
- P. Workman and I. J. Stratford, “The experimental development of bioreductive drugs and their role in cancer therapy,” Cancer and Metastasis Reviews, vol. 12, no. 2, pp. 73–82, 1993. View at Scopus
- A. C. Sartorelli, W. F. Hodnick, M. F. Belcourt, et al., “Mitomycin C: a prototype bioreductive agent,” Oncology Research, vol. 6, no. 10-11, pp. 501–508, 1994. View at Scopus
- K. Pors and L. H. Patterson, “DNA mismatch repair deficiency, resistance to cancer chemotherapy and the development of hypersensitive agents,” Current Topics in Medicinal Chemistry, vol. 5, no. 12, pp. 1133–1149, 2005. View at Publisher · View at Google Scholar · View at Scopus
- Y. Na, V.-S. Li, Y. Nakanishi, K. F. Bastow, and H. Kohn, “Synthesis, DNA cross-linking activity, and cytotoxicity of dimeric mitomycins,” Journal of Medicinal Chemistry, vol. 44, no. 21, pp. 3453–3462, 2001. View at Publisher · View at Google Scholar · View at Scopus
- S.-L. Wang, J.-F. Han, X.-Y. He, X.-R. Wang, and J.-Y. Hong, “Genetic variation of human cytochrome P450 reductase as a potential biomarker for mitomycin C-induced cytotoxicity,” Drug Metabolism and Disposition, vol. 35, no. 1, pp. 176–179, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. T. Dorr, “New findings in the pharmacokinetic, metabolic, and drug-resistance aspects of mitomycin C,” Seminars in Oncology, vol. 15, no. 3, supplement 4, pp. 32–41, 1988. View at Scopus
- D. L. Gustafson and C. A. Pritsos, “Oxygen radical generation and alkylating ability of mitomycin C bioactivated by xanthine dehydrogenase,” Proceedings of the Western Pharmacology Society, vol. 35, pp. 147–151, 1992. View at Scopus
- E. Offord, G. van Poppel, and R. Tyrrell, “Markers of oxidative damage and antioxidant protection: current status and relevance to disease,” Free Radical Research, vol. 33, supplement, pp. S5–S19, 2000. View at Scopus
- R. J. Reiter, “Pineal melatonin: cell biology of its synthesis and of its physiological interactions,” Endocrine Reviews, vol. 12, no. 2, pp. 151–180, 1991. View at Scopus
- A. Carrillo-Vico, R. J. Reiter, P. J. Lardone, et al., “The modulatory role of melatonin on immune responsiveness,” Current Opinion in Investigational Drugs, vol. 7, no. 5, pp. 423–431, 2006. View at Scopus
- D. X. Tan, L. D. Chen, B. Poeggeler, et al., “Melatonin: a potent, endogenous hydroxyl radical scavenger,” Endocrine Journal, vol. 1, pp. 57–60, 1993.
- S. Ortega-Gutiérrez, J. J. García, E. Martínez-Ballarín, et al., “Melatonin improves deferoxamine antioxidant activity in protecting against lipid peroxidation caused by hydrogen peroxide in rat brain homogenates,” Neuroscience Letters, vol. 323, no. 1, pp. 55–59, 2001. View at Publisher · View at Google Scholar · View at Scopus
- M.-J. Jou, T.-I. Peng, P.-Z. Yu, et al., “Melatonin protects against common deletion of mitochondrial DNA-augmented mitochondrial oxidative stress and apoptosis,” Journal of Pineal Research, vol. 43, no. 4, pp. 389–403, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. Gitto, S. Pellegrino, P. Gitto, I. Barberi, and R. J. Reiter, “Oxidative stress of the newborn in the pre- and postnatal period and the clinical utility of melatonin,” Journal of Pineal Research, vol. 46, no. 2, pp. 128–139, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. C. Erren and R. J. Reiter, “A generalized theory of carcinogenesis due to chronodisruption,” Neuroendocrinology Letters, vol. 29, no. 6, pp. 815–821, 2008. View at Scopus
- M. Karbownik, A. Lewinski, and R. J. Reiter, “Anticarcinogenic actions of melatonin which involve antioxidative processes: comparison with other
antioxidants,” International Journal of Biochemistry and Cell Biology, vol. 33, no. 8, pp. 735–753, 2001. View at Publisher · View at Google Scholar · View at Scopus
- Vijayalaxmi, C. R. Thomas Jr., R. J. Reiter, and T. S. Herman, “Melatonin: from basic research to cancer treatment clinics,” Journal of Clinical Oncology, vol. 20, no. 10, pp. 2575–2601, 2002. View at Publisher · View at Google Scholar · View at Scopus
- M. Hayashi, Y. Kodama, T. Awogi, T. Suzuki, A. O. Asita, and T. Sofuni, “The micronucleus assay using peripheral blood reticulocytes from mitomycin C- and cyclophosphamide-treated rats,” Mutation Research, vol. 278, no. 2-3, pp. 209–213, 1992. View at Scopus
- C. K. Grisolia, “A comparison between mouse and fish micronucleus test using cyclophosphamide, mitomycin C and various pesticides,” Mutation Research, vol. 518, no. 2, pp. 145–150, 2002. View at Publisher · View at Google Scholar · View at Scopus
- M. Hayashi, T. Sofuni, and M. Ishidate Jr., “An application of acridine orange fluorescent staining to the micronuclear test,” Mutation Research, vol. 120, no. 4, pp. 241–247, 1983. View at Scopus
- D. R. Janero, “Malondialdehyde and thiobarbituric acid-reactivity as diagnostic indices of lipid peroxidation and peroxidative tissue injury,” Free Radical Biology and Medicine, vol. 9, no. 6, pp. 515–540, 1990. View at Publisher · View at Google Scholar · View at Scopus
- M. M. Bradford, “A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dying binding,” Analytical Biochemistry, vol. 72, pp. 248–254, 1976.
- M. Hayashi, T. Morita, Y. Kodama, T. Sofuni, and M. Ishidate Jr., “The micronucleus assay with mouse peripheral blood reticulocytes using acridine orange-coated slides,” Mutation Research, vol. 245, no. 4, pp. 245–249, 1990. View at Scopus
- P. Morales-Ramírez, Y. Vallarino-Kelly, V. L. Cruz-Vallejo, et al., “In vivo kinetics of micronuclei induction by dysfunctional alkylating antineoplastics,” Mutagenesis, vol. 19, pp. 207–213, 2004.
- G. R. Fisher, L. H. Patterson, and P. L. Gutiérrez, “A comparison of free radical formation by quinone antitumor agents in MCF-7 cells and the role of NAD(P)H
(quinone-acceptor) oxidoreductase (DT-diaphorase),” Chemico-Biological Interactions, vol. 88, pp. 137–153, 1993.
- B. K. Sinha and E. G. Mimnaugh, “Free radicals and anticancer drug resistance: oxygen free radicals in the mechanisms of drug cytotoxicity and resistance by certain tumors,” Free Radical Biology and Medicine, vol. 8, no. 6, pp. 567–581, 1990. View at Publisher · View at Google Scholar · View at Scopus
- K. Sato, T. Akaike, Y. Kojima, M. Ando, M. Nagao, and H. Maeda, “Evidence of direct generation of oxygen free radicals from heterocyclic amines by NADPH/Cytochrome P-450 reductase in vitro,” Japanese Journal of Cancer Research, vol. 83, no. 11, pp. 1204–1209, 1992. View at Scopus
- M. M. Paz, A. Das, and M. Tomasz, “Mitomycin C linked to DNA minor groove binding agents: synthesis, reductive activation, DNA binding and cross-linking properties and in vitro antitumor activity,” Bioorganic and Medicinal Chemistry, vol. 7, no. 12, pp. 2713–2726, 1999. View at Publisher · View at Google Scholar · View at Scopus
- J. Cummings, V. J. Spanswick, and J. F. Smyth, “Re-evaluation of the molecular pharmacology of mitomycin C,” European Journal of Cancer, vol. 31, no. 12, pp. 1928–1933, 1995. View at Publisher · View at Google Scholar · View at Scopus
- J. Cummings, V. J. Spanswick, M. Tomasz, and J. F. Smyth, “Enzymology of mitomycin C metabolic activation in tumour tissue,” Biochemical Pharmacology, vol. 56, no. 4, pp. 405–414, 1998. View at Publisher · View at Google Scholar · View at Scopus
- P. Wang, Y. Song, L. Zhang, et al., “Quinone methane derivates: important intermediates to DNA alkylating and DNA cross-linking actions,” Current Medicinal Chemistry, vol. 12, pp. 2893–2913, 2005.
- P. L. Gutiérrez, “The role of NAD(P)H oxidoreductase (DT-Diaphorase) in the bioactivation of quinone-containing antitumor agents: a review,” Free Radical Biology and Medicine, vol. 29, no. 3-4, pp. 263–275, 2000. View at Publisher · View at Google Scholar · View at Scopus
- A. D. Bolzan and M. S. Bianchi, “Genotoxicity of streptonigrin: a review,” Mutation Research, vol. 488, no. 1, pp. 25–37, 2001. View at Publisher · View at Google Scholar · View at Scopus
- W. G. De Graff, L. S. Myers Jr., J. B. Mitchell, and S. M. Hahn, “Protection against Adriamycin cytotoxicity and inhibition of DNA topoisomerase II activity by 3,4-dihydroxybenzoic acid,” International Journal of Oncology, vol. 23, no. 1, pp. 159–163, 2003. View at Scopus
- T. J. Monks, R. P. Hanzlik, G. M. Cohen, D. Ross, and D. G. Graham, “Quinone chemistry and toxicity,” Toxicology and Applied Pharmacology, vol. 112, no. 1, pp. 2–16, 1992. View at Publisher · View at Google Scholar · View at Scopus
- Y. Li, P. Kuppusamy, J. L. Zweier, and M. A. Trush, “Role of Cu/Zn-superoxide dismutase in xenobiotic activation. I. Chemical reactions involved in the Cu/Zn-superoxide dismutase-accelerated oxidation of the benzene metabolite 1,4-hydroquinone,” Molecular Pharmacology, vol. 49, no. 3, pp. 404–411, 1996. View at Scopus
- P. Kovacic and J. A. Osuna Jr., “Mechanisms of anti-cancer agents: emphasis on oxidative stress and electron transfer,” Current Pharmaceutical Design, vol. 6, no. 3, pp. 277–309, 2000. View at Scopus
- Vijayalaxmi, M. L. Meltz, R. J. Reiter, and T. S. Herman, “Melatonin and protection from genetic damage in blood and bone marrow: whole-body irradiation studies in mice,” Journal of Pineal Research, vol. 27, no. 4, pp. 221–225, 1999. View at Publisher · View at Google Scholar · View at Scopus
- M. C. Krishna, W. DeGraff, S. Tamura, et al., “Mechanisms of hypoxic and aerobic cytotoxicity of mitomycin C in Chinese hamster V79 cells,” Cancer Research, vol. 51, no. 24, pp. 6622–6628, 1991. View at Scopus
- S. M. Hahn, F. J. Sullivan, A. M. DeLuca, et al., “Protection of mitomycin C induced skin extravation with the nitroxide, 3-carbamoyl-proxyl (3-CP),” International Journal of Oncology, vol. 10, pp. 119–123, 1997.
- V. Santini, “Amifostine: chemotherapeutic and radiotherapeutic protective effects,” Expert Opinion on Pharmacotherapy, vol. 2, no. 3, pp. 479–489, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Sriswasdi, S. Jootar, and F. J. Giles, “Amifostine and hematologic effects,” Journal of the Medical Association of Thailand, vol. 83, no. 4, pp. 374–382, 2000. View at Scopus
- E. Selvakumar, C. Prahalathan, P. T. Sudharsan, and P. Varalakshmi, “Protective effect of lipoic acid on micronuclei induction by cyclophosphamide,” Archives of Toxicology, vol. 80, no. 2, pp. 115–119, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. A. Elmegeed, W. K. B. Khalil, A. A. Raouf, and M. M. Abdelhalim, “Synthesis and in vivo anti-mutagenic activity of novel melatonin derivatives,” European Journal of Medicinal Chemistry, vol. 43, no. 4, pp. 763–770, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. G. Ortiz, R. J. Reiter, G. Zúñiga, et al., “Genotoxicity of paraquat: micronuclei induced in bone marrow and peripheral blood are inhibited by melatonin,” Mutation Research, vol. 464, no. 2, pp. 239–245, 2000. View at Publisher · View at Google Scholar · View at Scopus
- S. A. Musatov, V. N. Anisimov, V. André, et al., “Modulatory effects of melatonin on genotoxic response of reference mutagens in the Ames test and the comet
assay,” Mutation Research, vol. 417, no. 2-3, pp. 75–84, 1998. View at Publisher · View at Google Scholar · View at Scopus
- C. M. Cagnoli, C. Atabay, E. Kharlamova, and H. Manev, “Melatonin protects neurons from singlet oxygen-induced apoptosis,” Journal of Pineal Research, vol. 18, no. 4, pp. 222–226, 1995. View at Scopus
- D. X. Tan, R. J. Reiter, L. C. Manchester, et al., “Chemical and physical properties and potential mechanisms: melatonin as a broad spectrum antioxidant and free radical scavenger,” Current Topics in Medicinal Chemistry, vol. 2, no. 2, pp. 181–197, 2002. View at Scopus
- E. Gilad, S. Cuzzocrea, B. Zingarelli, et al., “Melatonin is a scavenger of peroxinitrite,” Life Sciences, vol. 60, pp. PL169–PL174, 1997.
- I. Antolín, C. Rodríguez, R. M. Sáinz, et al., “Neurohormone melatonin prevents cell damage: effect on gene expression for antioxidant enzymes,” FASEB Journal, vol. 10, no. 8, pp. 882–890, 1996. View at Scopus
- S. Ortega-Gutiérrez, L. Fuentes-Broto, J. J. García, et al., “Melatonin reduces protein and lipid oxidative damage induced by homocysteine in rat brain homogenates,” Journal of Cellular Biochemistry, vol. 102, no. 3, pp. 729–735, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. C. Burcham, “Genotoxic lipid peroxidation products: their DNA damaging properties and role in formation of endogenous DNA adducts,” Mutagenesis, vol. 13, no. 3, pp. 287–305, 1998. View at Publisher · View at Google Scholar · View at Scopus
- D. E. Blask, R. T. Dauchy, L. A. Sauer, and J. A. Krause, “Melatonin uptake and growth prevention in rat hepatoma 7288CTC in response to dietary melatonin: melatonin receptor-mediated inhibition of tumor linoleic acid metabolism to the growth signaling molecule 13-hydroxyoctadecadienoic acid and the potential role of phytomelatonin,” Carcinogenesis, vol. 25, no. 6, pp. 951–960, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. M. León-Blanco, J. M. Guerrero, R. J. Reiter, J. R. Calvo, and D. Pozo, “Melatonin inhibits telomerase activity in the MCF-7 tumor cell line both in vivo and in vitro,” Journal of Pineal Research, vol. 35, no. 3, pp. 204–211, 2003. View at Publisher · View at Google Scholar · View at Scopus
- E. Mazzon, E. Esposito, C. Crisafulli, et al., “Melatonin modulates signal transduction pathways and apoptosis in experimental colitis,” Journal of Pineal Research, vol. 41, no. 4, pp. 363–373, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. Kilic, Ü. Kilic, R. J. Reiter, C. L. Bassetti, and D. M. Hermann, “Prophylactic use of melatonin protects against focal cerebral ischemia in mice: role of endothelin converting enzyme-1,” Journal of Pineal Research, vol. 37, no. 4, pp. 247–251, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. Grant, M. Loizidou, and I. Taylor, “Endothelin-I: a multifunctional molecule in cancer,” British Journal of Cancer, vol. 88, no. 2, pp. 163–166, 2003. View at Publisher · View at Google Scholar · View at Scopus
- P. T. Ram, L. Yuan, J. Dai, et al., “Differential responsiveness of MCF-7 human breast cancer cell line stocks to the pineal hormone, melatonin,” Journal of Pineal Research, vol. 28, no. 4, pp. 210–218, 2000. View at Scopus
- Y. Kanishi, Y. Kobayashi, S. Noda, B. Ishizuka, and K. Saito, “Differential growth inhibitory effect of melatonin on two endometrial cancer cell lines,” Journal of Pineal Research, vol. 28, no. 4, pp. 227–233, 2000. View at Scopus
- R. Girgert, C. Bartsch, S. M. Hill, R. Kreienberg, and V. Hanf, “Tracking the elusive antiestrogenic effect of melatonin: a new methodological approach,” Neuroendocrinology Letters, vol. 24, no. 6, pp. 440–444, 2003. View at Scopus