Comparison of influence of carmustine and new proline analog of nitrosourea on antioxidant system in breast carcinoma cells (MCF-7)

References

• Becker, K., Gromer, S., Schirmer, R. H., Müller, S. (2000). Thioredoxin reductase as a pathophysiological factor and drug target. Eur J Biochem 267:6118–6125.
   PubMedGoogle Scholar
• Bielawski, K., Bielawska, A., Słodownik, T., Bołkun-Skórnicka, U., Muszyńska, A. (2008). Proline-linked nitrosoureas as prolidase- convertible prodrugs in human breast cancer cells. Pharmacol Rep 60:171–182.
   PubMed Web of Science ®Google Scholar
• Bradley, A., Nathan, C. F. (1984). Glutathione metabolism as a determinant of therapeutic efficiency: a review. Cancer Res 44:4224–4232.
   PubMed Web of Science ®Google Scholar
• Cereser C, Guichard J, Drai J, Bannier E, Garcia I, Boget S, et al. (2001). Quantitation of reduced and total glutathione at the femtomole level by high-performance liquid chromatography with fluorescence detection: application to red blood cells and cultured fibroblasts. J Chromatogr B Biomed Sci Appl 752:123–132.
   PubMed Web of Science ®Google Scholar
• Colvin, O. M., Friedman, H. S. (2005). Alkylating agents. In: DeVita, V. T. (Ed.), Cancer. Principles and Practice of Oncology (332–344). Philadelphia, PA, USA: Williams & Wilkins.
   Google Scholar
• Colvin, O. M. (1994). Mechanisms of resistance to alkylating agents. Cancer Treat Res 73:249–262.
   PubMedGoogle Scholar
• Conklin, K. (2004). Chemotherapy-associated oxidative stress: impact on chemotherapeutic effectiveness. Integ Cancer Ther 3:294–300.
   PubMedGoogle Scholar
• Copper, J. A., Jr. (1997). Drug-induced lung disease. Adv Intern Med 42:231–268.
   PubMedGoogle Scholar
• Davies, K. J., Lin, S. W., Pacifici, R. E. (1987). Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein. J Biol Chem 262:9914–9920.
   PubMed Web of Science ®Google Scholar
• Davis, M. R., Kassahun, K., Jochheim, C. M., Brandt, K. M., Baillie, T. A. (1993). Glutathione and N-acetylcysteine conjugates of 2-chloroethyl isocyanate. Identification as metabolites of N,N’-bis(2-chloroethyl)-N-nitrosourea in the rat and inhibitory properties toward glutathione reductase in vitro. Chem Res Toxicol 6:376–383.
   PubMed Web of Science ®Google Scholar
• Endo, F., Tanoue, A., Nakai, H., Hata, A., Indo, Y., Titani, K., et al. (1989). Primary structure and gene localization of human prolidase. J Biol Chem 264:4476–4481.
   PubMed Web of Science ®Google Scholar
• Gadjeva, V., Tolekova, A., Vasileva, M. (2007). Effect of the spin-labeled 1-ethyl-1-nitrosourea on CCNU-induced oxidative liver injury. Pharmazie 62:608–613.
   PubMed Web of Science ®Google Scholar
• Galler, B., Winge, D. (1983). A method for distinguishing Cu,Zn- and Mn-containing superoxide dismutases. Anal Biochem 128:86–92.
   PubMed Web of Science ®Google Scholar
• Gromer, S., Schirmer, H., Becker, K. (1997). The 58-kDa mouse selenoprotein is a BCNU-sensitive thioredoxin reductase. FEBS Lett 412:318–320.
   PubMed Web of Science ®Google Scholar
• Halliwell, B., Zhao, K., Whiteman, M. (1999). Nitric oxide and peroxynitrite. The ugly, the uglier, and the not so good: a personal view of recent controversies. Free Radic Res 31:651–669.
   PubMed Web of Science ®Google Scholar
• Handley, K., Sunde, R. (2001). Selenium regulation of thioredoxin reductase activity and mRNA levels in rat liver. J Nutr Biochem 12:693–702.
   PubMed Web of Science ®Google Scholar
• Hill, K., et al. (1997). Thioredoxin reductase activity is decreased by selenium deficiency. Biochem Biophys Res Commun 234:293–295.
   PubMed Web of Science ®Google Scholar
• Holmgren, A., Bjornstedt, M. (1995). Thioredoxin and thioredoxin reductase. Meth Enzymol 21:199–205.
   Google Scholar
• Hurley, L. H. (2002). DNA and its associated processes as targets for cancer therapy. Natl Rev Cancer 2:188–200.
   PubMed Web of Science ®Google Scholar
• Jopperi-Davis, K., Park, M. S., Rogers, L. K., Backers, C. H., Lim, I. K., Smith, C. (2004). Compartmental inhibition of hepatic glutathione reductase activities by 1,3-bis(2-chloroethyl)-1-N-nitrosourea (BCNU) in Sprague-Dawley and Fischer-344 rats. Toxicology Lett 147:219–228.
   PubMed Web of Science ®Google Scholar
• Kaufmann, S. H., Earnshaw, W. C. (2000). Induction of apoptosis by cancer chemotherapy. Exp Cell Res 256:42–49.
   PubMed Web of Science ®Google Scholar
• Kehrer, J. P. (2000). The Haber-Weiss reaction and mechanisms of toxicity. Toxicology 149:43–50.
   PubMed Web of Science ®Google Scholar
• Kinter, M., Roberts, R. J. (1996). Glutathione consumption and glutathione peroxidase inactivation in fibroblast cell lines by 4-hydroxy-2-nonenal. Free Radic Biol Med 21:457–462.
   PubMed Web of Science ®Google Scholar
• Kono, Y., Fridovich, I. (1982). Superoxide radical inhibits catalase. J Biochem 257:5751–5754.
   Google Scholar
• Kowaltowski, A. J., Vercesi, A. E. (1999). Mitochondrial damage induced by conditions of oxidative stress. Free Radic Biol Med 26:463–471.
   PubMed Web of Science ®Google Scholar
• Lemoine, A., Lucas, C., Ings, R. (1991). Metabolism of the chloroethylnitrosoureas. Xenobiotica 21:775–791.
   PubMed Web of Science ®Google Scholar
• Londero, D., Greco, P. L. (1996). Automated HPLC separating with spectrofluorometric detection of malondialdehyde- thiobarbituric acid adducts in plasma. J Chromatogr 729:207–210.
   PubMed Web of Science ®Google Scholar
• Messmer, U. K., Ankarcrona, M., Nicotera, P., Brüne, B. (1994). p53 expression in nitric oxide–induced apoptosis. FEBS Lett 355:23–26.
   PubMed Web of Science ®Google Scholar
• Misra, H., Fridovich, I. (1972). The role of superoxide anion in the auto-oxidation of epinephrine and a simple assay for superoxide dismutation. J Biol Chem 247:3170–3174.
   PubMed Web of Science ®Google Scholar
• Mittal, S., Song, X., Vig, B. S., Landanowski, C. P., Kim, I., Holfinger, J. M., et al. (2005). Prolidase, a potential enzyme target for melanoma design of proline-containing dipeptide- like prodrugs. Mol Pharm 2:37–46.
   PubMedGoogle Scholar
• Mize, C. E., Langdon, R. G. (1962). Hepatic glutathione reductase. I. Purification and general kinetic properties. J Biol Chem 237:1589–1595.
   PubMed Web of Science ®Google Scholar
• Moncada, S., Erusalimsky, J. D. (2002). Does nitric oxide modulate mitochondrial energy generation and apoptosis? Nat Rev Mol Cell Biol 3:214–220.
   PubMed Web of Science ®Google Scholar
• Nathan, C. F., Arrick, B. A., Murray, H. W., DeSantis, N. M., Cohn, Z. A. (1981). Tumor cell antioxidant defences. Inhibition of the glutathione redox cycle enhances macrophage- mediated cytolysis. J Exp Med 153:766–782.
   PubMed Web of Science ®Google Scholar
• Paglia, D. E., Valentine, W. N. (1967). Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70:158–169.
   PubMed Web of Science ®Google Scholar
• Pennington, J. D., Jacobs, K. M., Sun, L., Bar-Sela, G., Mishra, M., Gius, D. (2007). Thioredoxin and thioredoxin reductase as redox-sensitive molecular targets for cancer therapy. Curr Pharm Des 13:3368–3377.
   PubMed Web of Science ®Google Scholar
• Petak, I., Mihalik, R., Bauer, P., Suli-Vargha, H., Sebestyen, A., Kopper, L. (1998). BCNU is a caspase-mediated inhibitor of drug-induced apoptosis. Cancer Res 58:614–618.
   PubMed Web of Science ®Google Scholar
• Petros, W. P., Broadwater, G., Berry, G., et al. (2002). Association of high-dose cyclophosphamide, cisplatin, and carmustine pharmacokinetics with survival, toxicity, and dosing weight in patients with primary breast cancer. Clin Cancer Res 8:698–705.
   PubMed Web of Science ®Google Scholar
• Rice-Evans, C. A., et al. (1996). Structure-antioxidant activity relationships of flavonoids and phenolic acids. Free Radic Biol Med 20:933–956.
   PubMed Web of Science ®Google Scholar
• Rice-Evans, C. A., Diplock, A. T., Symons, M. (1991). Techniques in Free Radical Research. Amsterdam, The Netherlands: Elsevier.
   Google Scholar
• Rybczyńska, M. (1994). Biochemical aspects of free radical– mediated tissue injury. Postępy Hig Med Dosw 48:419–441.
   PubMedGoogle Scholar
• Smart, D. K., Ortiz, K. L., Mattson, D., Bradbury, C. M., Bisht, K. S., Sieck, L. K., et al. Thioredoxin reductase as a potential molecular target for anticancer agents that induce oxidative stress. Cancer Res 64:6716–6724.
   PubMed Web of Science ®Google Scholar
• Spector, A., Yan, G. Z., Huang, R. R., McDermott, M. J., Gascoyne, P. R., Pigiet, V. (1988). The effect of H2O2 upon thioredoxin-enriched lens epithelial cells. J Biol Chem 263:4984–4990.
   PubMed Web of Science ®Google Scholar
• Stahl, W., Lenhardt, S., Przybylski, M., Eisenbrand, G. (1992). Mechanism of glutathione-mediated DNA damage by the antineoplastic agent, 1,3-bis(2-chloroethyl)-N-nitrosourea. Chem Res Toxicol 5:106–109.
   PubMed Web of Science ®Google Scholar
• Sykes, J. A., McCormac, F. X., O’Breien, T. J. 1978. Preliminary study of the superoxide dismutase content of some human tumors. Cancer Res 38:2759–2762.
   PubMed Web of Science ®Google Scholar
• Urig, S., Becker, K. (2006). On the potential of thioredoxin reductase inhibitors for cancer therapy. Sem Cancer Biol 16:452–465.
   PubMed Web of Science ®Google Scholar
• Watson, W., Yang, X., Choi, Y. E., Jones, D. P., Kehrer, J. P. (2004). Thioredoxin and its role in toxicology. Toxicol Sci 78:3–14.
   PubMed Web of Science ®Google Scholar
• Weydert, C., Zhang, Y., Sun, W., et al. (2008). Increased oxidative stress created by adenoviral Mn-SOD or Cu,Zn-SOD plus BCNU (1,3-bis(2-chloroethyl)-1-nitrosourea) inhibits breast cancer cell gowth. Free Radic Biol Med 44:856–867.
   PubMed Web of Science ®Google Scholar
• Wiencke, J. K., Wiemels, J. (1995). Genotoxicity of 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU). Mutat Res 339:91–119.
   PubMed Web of Science ®Google Scholar
• Wolff, S. P., Garner, A., Dean, R. T. (1986). Free radicals, lipids, and protein degradation. FEBS Lett 11:27–31.
   Google Scholar