Se-methylselenocysteine modulates antioxidant response of rat spleen to ionizing radiation

Anno, G. H., Young, R. W., Bloom, R. M. & Mercier, J. R. Dose response relationships for acute ionizingradiation lethality. Health Phys. 84, 565–575 (2003). Mehrotra, S., Pecaut, M. J. & Gridley, D. S. Effects of minocycline on hematopoietic recovery after wholebody irradiation. In Vivo 27, 11–28 (2013). Greenberger, J. S. Radioprotection. In Vivo 23, 323–336 (2009). Rayman, M. P. Selenium and human health. Lancet 379, 1256–1268 (2012). Brozmanova, J., Manikova, D., Vlckova, V. & Chovanec, M. Selenium: a double-edged sword for defense and offence in cancer. Arch. Toxicol. 84, 919–938 (2010). Kunwar, A. et al. In vivo radioprotection studies of 3,3′-diselenodipropionic acid, a selenocystine derivative. Free Radic. Biol. Med. 48, 399–410 (2010). Tak, J. K. & Park, J. W. The use of ebselen for radioprotection in cultured cells and mice. Free Radic. Biol. Med. 46, 1177–1185 (2009). Kumar, B. S. et al. In vitro radioprotection studies of organoselenium compounds: differences between mono- and diselenides. Radiat. Environ. Biophy. 48, 379–384 (2009). Lyi, S. M. et al. Molecular and biochemical characterization of the selenocysteine Se-methyltransferase gene and Se-methylselenocysteine synthesis in broccoli. Plant Physiol. 138, 409–420 (2005). Christensen, M. J. et al. Combination effects of dietary soy and methylselenocysteine in a mouse model of prostate cancer. Prostate 73, 986–995 (2013). El-Bayoumy, K. & Sinha, R. Mechanisms of mammary cancer chemoprevention by organoselenium compounds. Mutat. Res. 551, 181–197 (2004). Azrak, R. G. et al. Efficacy of increasing the therapeutic index of irinotecan, plasma and tissue selenium concentrations is methylselenocysteine dose dependent. Biochem. Pharmacol. 73, 1280–1287 (2007). Li, Z. et al. Combination of methylselenocysteine with tamoxifen inhibits MCF-7 breast cancer xenografts in nude mice through elevated apoptosis and reduced angiogenesis. Breast Cancer Res. Treat. 118, 33–43 (2009). Niehaus, W. G., Jr. & Samuelsson, B. Formation of malonaldehyde from phospholipid arachidonate during microsomal lipid peroxidation. Eur. J. Biochem. 6, 126–130 (1968). Abdalla, M. Y., Hassan, I. M., Mustafa, N. H., Tahtamouni, L. H. & Ahmad, I. M. Total body glutathione depletion induces oxidative stress and disrupts the immune function in mice. Toxicol. Environ. Chem. 93, 157–170 (2011). Genovese, T. et al. Role of endogenous glutathione in the secondary damage in experimental spinal cord injury in mice. Neurosci. Lett. 423, 41–46 (2007). Weekley, C. M., Aitken, J. B., Musgrave, I. F. & Harris, H. H. Methylselenocysteine treatment leads to diselenide formation in human cancer cells: evidence from X-ray absorption spectroscopy studies. Biochemistry 51, 736–738 (2012). El-Sayed, W. M., Aboul-Fadl, T., Lamb, J. G., Roberts, J. C. & Franklin, M. R. Effect of selenium-containing compounds on hepatic chemoprotective enzymes in mice. Toxicology 220, 179–188 (2006). Gozzelino, R., Jeney, V. & Soares, M. P. Mechanisms of cell protection by heme oxygenase-1. Annu. Rev. Pharmacol. Toxicol. 50, 323–354 (2010). Stocker, R., Yamamoto, Y., McDonagh, A. F., Glazer, A. N. & Ames, B. N. Bilirubin is an antioxidant of possible physiological importance. Science 235, 1043–1046 (1987). Berberat, P. O. et al. Inhibition of heme oxygenase-1 increases responsiveness of pancreatic cancer cells to anticancer treatment. Clin. Cancer Res. 11, 3790–3798 (2005). Pajaud, J., Kumar, S., Rauch, C., Morel, F. & Aninat, C. Regulation of signal transduction by glutathione transferases. Int. J. Hepatol. 2012, 137676 (2012). Yusuf, M. A., Chuang, T., Bhat, G. J. & Srivenugopal, K. S. Cys-141 glutathionylation of human p53: Studies using specific polyclonal antibodies in cancer samples and cell lines. Free Radic. Biol. Med. 49, 908–917 (2010). Smith-Pearson, P. S. et al. Decreasing peroxiredoxin II expression decreases glutathione, alters cell cycle distribution, and sensitizes glioma cells to ionizing radiation and H2O2. Free Radic. Biol. Med. 45, 1178–1189 (2008). Zhang, B. et al. Involvement of peroxiredoxin I in protecting cells from radiation-induced death. J. Radiat. Res. 46, 305–312 (2005). Nguyen, T., Nioi, P. & Pickett, C. B. The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress. J. Biol. Chem. 284, 13291–13295 (2009). Moi, P., Chan, K., Asunis, I., Cao, A. & Kan, Y. W. Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the betaglobin locus control region. Proc. Natl. Acad. Sci. USA 91, 9926–9930 (1994). Chen, X. L. et al. Activation of Nrf2/ARE pathway protects endothelial cells from oxidant injury and inhibits inflammatory gene expression. Am. J. Physiol. Heart Circ. Physiol. 290, H1862–1870 (2006). Zhu, H., Itoh, K., Yamamoto, M., Zweier, J. L. & Li, Y. Role of Nrf2 signaling in regulation of antioxidants and phase 2 enzymes in cardiac fibroblasts: protection against reactive oxygen and nitrogen species-induced cell injury. FEBS Lett. 579, 3029–3036 (2005). Suzuki, K. T., Tsuji, Y., Ohta, Y. & Suzuki, N. Preferential organ distribution of methylselenol source Se-methylselenocysteine relative to methylseleninic acid. Toxicol. Appl. Pharmacol. 227, 76–83 (2008). Zhang, J., Wang, X. & Xu, T. Elemental selenium at nano size (Nano-Se) as a potential chemopreventive agent with reduced risk of selenium toxicity: comparison with se-methylselenocysteine in mice. Toxicol. Sci. 101, 22–31 (2008). Johnson, W. D., Morrissey, R. L., Kapetanovic, I., Crowell, J. A. & McCormick, D. L. Subchronic oral toxicity studies of Se-methylselenocysteine, an organoselenium compound for breast cancer prevention. Food Chem. Toxicol. 46, 1068–1078 (2008). Bolus, N. E. Basic review of radiation biology and terminology. J. Nucl. Med. Technol. 29, 67–73 (2001). Ohkawa, H., Ohishi, N. & Yagi, K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem. 95, 351–358 (1979). Tietze, F. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27, 502–522 (1969). Seelig, G. F. & Meister, A. Gamma-glutamylcysteine synthetase from erythrocytes. Anal. Biochem. 141, 510–514 (1984). Paglia, D. E. & Valentine, W. N. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J. Lab. Clin. Med. 70, 158–169 (1967). Cohen, M. B. & Duvel, D. L. Characterization of the inhibition of glutathione reductase and the recovery of enzyme activity in exponentially growing murine leukemia (L1210) cells treated with 1,3-bis(2-chloroethyl)-1-nitrosourea. Biochem. Pharmacol. 37, 3317–3320 (1988). Bautista, J. M., Mason, P. J. & Luzzatto, L. Purification and properties of human glucose-6-phosphate dehydrogenase made in E. coli. Biochim. Biophys. Acta 1119, 74–80 (1992). Misra, H. P. & Fridovich, I. The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. J. Biol. Chem. 247, 3170–3175 (1972). Aebi, H. Catalase in vitro. Methods Enzymol. 105, 121–126 (1984). Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248–254 (1976). Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275 (1951).