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Effect of Se-methylselenocysteine on the Antioxidant System in Rat Tissues

  • Received : 2010.10.08
  • Accepted : 2010.11.26
  • Published : 2010.12.31

Abstract

We assessed the effect of Se-methylselenocysteine (MSC) treatment, at a dose of 0.75 mg/rat/day for 1 or 2 weeks, on the activities of antioxidant systems in Sprague-Dawley rat tissues. Significant changes in glutathione and antioxidant enzyme activities, with different patterns among tissues, were evidenced. Glutathione content and its reduction state in the liver, lung, and kidney were elevated upon MSC treatment, whereas they were significantly lowered in the spleen. Among the tissues exhibiting glutathione increase, there were different enzymatic responses: $\gamma$-glutamylcysteine ligase activity, the rate-limiting enzyme in the glutathione synthesis pathway, was increased in the liver, whereas the activities of the enzymes associated with glutathione recycling, namely, glutathione peroxidase, glutathione reductase, and glucose 6-phosphate dehydrogenase, were significantly increased in the lung and the kidney. The superoxide dismutase activity was decreased in all tissues upon MSC treatment, whereas catalase activity was increased in all tissues but the liver. Lipid peroxidation level was transiently increased at 1 week in the lung and the kidney, whereas it was persistently increased in the spleen. The increase was not evident in the liver. The results indicate that the MSC treatment results in an increase in the antioxidant capacity of the liver, lung, and kidney principally via an increase in glutathione content and reduction, which appeared to be a result of increased synthesis or recycling of glutathione via tissue-dependent adaptive response to oxidative stress triggered by MSC. The spleen appeared to be very sensitive to oxidative stress, and therefore, the adaptive response could not provide protection against oxidative damage.

Keywords

References

  1. Alissa EM, Bahijri SM, Ferns GA. 2003. The controversy surrounding selenium and cardiovascular disease: a review of the evidence. Med Sci Monit 9: RA9-18.
  2. Ellis DR, Salt DE. 2003. Plants, selenium and human health. Curr Opin Plant Biol 6: 273-279. https://doi.org/10.1016/S1369-5266(03)00030-X
  3. Pagmantidis V, Meplan C, van Schothorst EM, Keijer J, Hesketh JE. 2008. Supplementation of healthy volunteers with nutritionally relevant amounts of selenium increases the expression of lymphocyte protein biosynthesis genes. Am J Clin Nutr 87: 181-189.
  4. Clark LC, Combs GF Jr, Turnbull BW, Slate EH, Chalker DK, Chow J, Davis LS, Glover RA, Graham GF, Gross EG, Krongrad A, Lesher JL Jr, Park HK, Sanders BB Jr, Smith CL, Taylor JR. 1996. Effects of selenium supplementation for cancer prevention in patients with carcinoma of the skin. A randomized controlled trial. Nutritional Prevention of Cancer Study Group. JAMA 276: 1957-1963. https://doi.org/10.1001/jama.276.24.1957
  5. Combs GF Jr, Gray WP. 1998. Chemopreventive agents: selenium. Pharmacol Ther 79: 179-192. https://doi.org/10.1016/S0163-7258(98)00014-X
  6. Ip C. 1998. Lessons from basic research in selenium and cancer prevention. J Nutr 128: 1845-1854.
  7. Sinha R, El-Bayoumy K. 2004. Apoptosis is a critical cellular event in cancer chemoprevention and chemotherapy by selenium compounds. Curr Cancer Drug Targets 4: 13-28. https://doi.org/10.2174/1568009043481614
  8. Gartner R, Albrich W, Angstwurm MW. 2001. The effect of a selenium supplementation on the outcome of patients with severe systemic inflammation, burn and trauma. Biofactors 14: 199-204. https://doi.org/10.1002/biof.5520140125
  9. Tirosh O, Levy E, Reifen R. 2007. High selenium diet protects against TNBS-induced acute inflammation, mitochondrial dysfunction, and secondary necrosis in rat colon. Nutrition 23: 878-886. https://doi.org/10.1016/j.nut.2007.08.019
  10. Azrak RG, Cao S, Pendyala L, Durrani FA, Fakih M, Combs GF Jr, Prey J, Smith PF, Rustum YM. 2007. Efficacy of increasing the therapeutic index of irinotecan, plasma and tissue selenium concentrations is methylselenocysteine dose dependent. Biochem Pharmacol 73: 1280-1287. https://doi.org/10.1016/j.bcp.2006.12.020
  11. Li Z, Carrier L, Belame A, Thiyagarajah A, Salvo VA, Burow ME, Rowan BG. 2009. 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. https://doi.org/10.1007/s10549-008-0216-x
  12. Irons R, Carlson BA, Hatfield DL, Davis CD. 2006. Both selenoproteins and low molecular weight selenocompounds reduce colon cancer risk in mice with genetically impaired selenoprotein expression. J Nutr 136: 1311-1317.
  13. Letavayova L, Vlckova V, Brozmanova J. 2006. Selenium: from cancer prevention to DNA damage. Toxicology 227: 1-14. https://doi.org/10.1016/j.tox.2006.07.017
  14. Ip C, Birringer M, Block E, Kotrebai M, Tyson JF, Uden PC, Lisk DJ. 2000. Chemical speciation influences comparative activity of selenium-enriched garlic and yeast in mammary cancer prevention. J Agric Food Chem 48: 2062-2070. https://doi.org/10.1021/jf000051f
  15. Whanger PD. 2002. Selenocompounds in plants and animals and their biological significance. J Am Coll Nutr 21: 223-232. https://doi.org/10.1080/07315724.2002.10719214
  16. Zeng H, Briske-Anderson M, Idso JP, Hunt CD. 2006. The selenium metabolite methylselenol inhibits the migration and invasion potential of HT1080 tumor cells. J Nutr 136: 1528-1532.
  17. Jackson MI, Combs GF Jr. 2008. Selenium and anticarcinogenesis: underlying mechanisms. Curr Opin Clin Nutr Metab Care 11: 718-726. https://doi.org/10.1097/MCO.0b013e3283139674
  18. Zhuo H, Smith AH, Steinmaus C. 2004. Selenium and lung cancer: a quantitative analysis of heterogeneity in the current epidemiological literature. Cancer Epidemiol Biomarkers Prev 13: 771-778.
  19. Nam TI, Park JJ, Choi EM. 2009. Prevention of alloxan-induced diabetes by Se-methylselenocysteine pretreatment in rats: The effect on antioxidant system in pancreas. J Food Sci Nutr 14: 95-101. https://doi.org/10.3746/jfn.2009.14.2.095
  20. Reed DJ, Babson JR, Beatty PW, Brodie AE, Ellis WW, Potter DW. 1980. High-performance liquid chromatography analysis of nanomole levels of glutathione, glutathione disulfide, and related thiols and disulfides. Anal Biochem 106: 55-62. https://doi.org/10.1016/0003-2697(80)90118-9
  21. Seelig GF, Meister A. 1984. Gamma-glutamylcysteine synthetase from erythrocytes. Anal Biochem 141: 510-514. https://doi.org/10.1016/0003-2697(84)90079-4
  22. Paglia DE, Valentine WN. 1967. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70: 158-169.
  23. Cohen MB, Duvel DL. 1988. 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. https://doi.org/10.1016/0006-2952(88)90645-4
  24. Bautista JM, Mason PJ, Luzzatto L. 1992. Purification and properties of human glucose-6-phosphate dehydrogenase made in E. coli. Biochim Biophys Acta 1119: 74-80. https://doi.org/10.1016/0167-4838(92)90237-8
  25. Misra HP, Fridovich I. 1972. The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. J Biol Chem 247: 3170-3175.
  26. Aebi H. 1984. Catalase in vitro. Methods Enzymol 105: 121-126. https://doi.org/10.1016/S0076-6879(84)05016-3
  27. Ohkawa H, Ohishi N, Yagi K. 1979. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 95: 351-358. https://doi.org/10.1016/0003-2697(79)90738-3
  28. Mueller AS, Pallauf J, Rafael J. 2003. The chemical form of selenium affects insulinomimetic properties of the trace element: investigations in type II diabetic dbdb mice. J Nutr Biochem 14: 637-647. https://doi.org/10.1016/j.jnutbio.2003.08.001
  29. Park EM, Ramnath N, Yang GY, Ahn JY, Park YR, Lee TY, Shin HS, Yu JH, Ip C, Park YM. 2007. High superoxide dismutase and low glutathione peroxidase activities in red blood cells predict susceptibility of lung cancer patients to radiation pneumonitis. Free Radic Biol Med 42: 280-287. https://doi.org/10.1016/j.freeradbiomed.2006.10.044
  30. Pinho RA, Andrades ME, Oliveira MR, Pirola AC, Zago MS, Silveira PCL, Dal-Pizzol F, Moreira JC. 2006. Imbalance in SOD/CAT activities in rat skeletal muscles submitted to treadmill training exercise. Cell Biol Int 30: 848-853. https://doi.org/10.1016/j.cellbi.2006.03.011
  31. Lauterburg BH, Adams JD, Mitchell JR. 1984. Hepatic glutathione homeostasis in the rat: efflux accounts for glutathione turnover. Hepatology 4: 586-590. https://doi.org/10.1002/hep.1840040402
  32. Lash LH, Jones DP. 1984. Renal glutathione transport. Characteristics of the sodium-dependent system in the basal-lateral membrane. J Biol Chem 259: 14508-14514.
  33. Kinnula VL, Paakko P, Soini Y. 2004. Antioxidant enzymes and redox regulating thiol proteins in malignancies of human lung. FEBS Lett 569: 1-6. https://doi.org/10.1016/j.febslet.2004.05.045
  34. van Klaveren RJ, Demedts M, Nemery B. 1997. Cellular glutathione turnover in vitro, with emphasis on type II pneumocytes. Eur Respir J 10: 1392-1400. https://doi.org/10.1183/09031936.97.10061392
  35. Drake EN. 2006. Cancer chemoprevention: selenium as a prooxidant, not an antioxidant. Med Hypotheses 67: 318-322. https://doi.org/10.1016/j.mehy.2006.01.058
  36. Spallholz JE. 1997. Free radical generation by selenium compounds and their prooxidant toxicity. Biomed Environ Sci 10: 260-270.
  37. Calder PC. 1997. N-3 polyunsaturated fatty acids and immune cell function. Adv Enzyme Regul 37: 197-237. https://doi.org/10.1016/S0065-2571(96)00004-0