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The protective effects of selenoorganic compounds against peroxynitrite-induced changes in plasma proteins and lipids

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Abstract

Many selenoorganic compounds play an important role in biochemical processes and act as antioxidants, enzyme inhibitors or drugs. The effects of a new selenocompound — bis(2-aminophenyl)-diselenide on oxidative/nitrative changes in human plasma proteins induced by peroxynitrite (ONOO) were studied in vitro and compared with the those of ebselen, a well-known antioxidant. We also studied the role of the tested selenocompounds in peroxynitrite-induced plasma lipid peroxidation. Exposure of the plasma to peroxynitrite (0.1 mM) resulted in an increase in the level of carbonyl groups and nitrotyrosine residues in plasma proteins (estimated using the ELISA method and Western blot analysis). In the presence of different concentrations (0.025–0.1 mM) of the tested selenocompounds, 0.1 mM peroxynitrite caused a distinct decrease in the level of carbonyl group formation and tyrosine nitration in plasma proteins. Moreover, these selenocompounds also inhibited plasma lipid peroxidation induced by ONOO−1 (0.1 mM). The obtained results indicate that in vitro bis(2-aminophenyl)-diselenide and ebselen have very similar protective effects against peroxynitrite-induced oxidative/nitrative damage to human plasma proteins and lipids.

Abbreviations

DMSO:

dimethylsufoxide

DNPH:

dinitrophenylhydrazine

ONOO :

peroxynitrite

TBARS:

thiobarbituric acid reactive substance

References

  1. 1.

    Soriano-Garcia, M. Organoselenium compounds as potential therapeutic and chemopreventive agents: a review. Curr. Med.Chem. 11 (2004) 1657–1669.

  2. 2.

    Gromer, S., Johansson, L., Bauer, H., Arscott, L.D., Rauch, S., Ballou, D.P., Williams, C.H., Jr., Schirmer, R.H. and Arner, E.S. Active sites of thioredoxin reductases: why selenoproteins? Proc. Natl. Acad. Sci. USA 100 (2003) 12618–12623.

  3. 3.

    Rotruck, J.T., Pope, A.L., Ganther, H.E., Swanson, A.B., Hafeman, D.G. and Hoekstra, W.G. Selenium: biochemical role as a component of glutathione peroxidase. Science 179 (1973) 588–590.

  4. 4.

    Low, S.C. and Berry, M.J. Knowing when not to stop: selenocysteine incorporation in eukaryotes. Trends Biochem. Sci. 21 (1996) 203–208.

  5. 5.

    Schewe, T. Molecular actions of ebselen — an antiinflammatory antioxidant. Gen. Pharmacol. 26 (1995) 1153–1169.

  6. 6.

    Furstenau, C.R., Spier, A.P., Rucker, B., Luisa, B.S., Battastini, A.M. and Sarkis, J.J. The effect of ebselen on adenine nucleotide hydrolysis by platelets from adult rats. Chem. Biol Interact. 148 (2004) 93–99.

  7. 7.

    Lindenblatt, N., Schareck, W., Belusa, L., Nickels, R.M., Menger, M.D. and Vollmar, B. Anti-oxidant ebselen delays microvascular thrombus formation in the rat cremaster muscle by inhibiting platelet P-selectin expression. Thromb. Haemost. 90 (2003) 882–892.

  8. 8.

    Sies, H. Ebselen, a selenoorganic compound as glutathione peroxidase mimic. Free Radic. Biol Med. 14 (1993) 313–323.

  9. 9.

    Briviba, K., Roussyn, I., Sharov, V.S. and Sies, H. Attenuation of oxidation and nitration reactions of peroxynitrite by selenomethionine, selenocystine and ebselen. Biochem. J. 319 (1996) 13–15.

  10. 10.

    Beckman, J.S., Beckman, T.W., Chen, J., Marshall, P.A. and Freeman, B.A. Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc. Natl. Acad. Sci. USA 87 (1990) 1620–1624.

  11. 11.

    Pryor, W.A. and Squadrito, G.L. The chemistry of peroxynitrite: a product from the reaction of nitric oxide with superoxide. Am. J. Physiol. 268 (1995) L699–L722.

  12. 12.

    Arteel, G.E., Briviba, K. and Sies, H. Protection against peroxynitrite. FEBS Lett. 445 (1999) 226–230.

  13. 13.

    Groves, J.T. Peroxynitrite: reactive, invasive and enigmatic. Curr. Opin. Chem. Biol. 3 (1999) 226–235.

  14. 14.

    Hogg, N., Darley-Usmar, V.M., Graham, A. and Moncada, S. Peroxynitrite and atherosclerosis. Biochem. Soc. Trans. 21 (1993) 358–362.

  15. 15.

    Olas, B., Nowak, P., Kolodziejczyk, J., Ponczek, M. and Wachowicz, B. Protective effects of resveratrol against oxidative/nitrative modifications of plasma proteins and lipids exposed to peroxynitrite. J. Nutr. Biochem. 17 (2005) 96–102.

  16. 16.

    Olas, B., Nowak, P., Kolodziejczyk, J. and Wachowicz, B. The effects of antioxidants on peroxynitrite-induced changes in platelet proteins. Thromb. Res. 113 (2004) 399–406.

  17. 17.

    Khan, J., Brennand, D.M., Bradley, N., Gao, B., Bruckdorfer, R. and Jacobs, M. 3-Nitrotyrosine in the proteins of human plasma determined by an ELISA method. Biochem. J. 330 (1998) 795–801.

  18. 18.

    Buss, H., Chan, T.P., Sluis, K.B., Domigan, N.M. and Winterbourn, C.C. Protein carbonyl measurement by a sensitive ELISA method. Free Rad. Biol. Med. 23 (1997) 361–366.

  19. 19.

    Levine, R.L. Carbonyl modified proteins in cellular regulation, aging, and disease. Free Rad. Biol. Med. 32 (2002) 790–796.

  20. 20.

    Wachowicz, B. and Kustron, J. Effect of cisplatin on lipid peroxidation in pig blood platelets. Cytobios 70 (1992) 41–47.

  21. 21.

    Lupidi, G., Angeletti, M., Eleuteri, A.M., Tacconi, L., Coletta, M. and Fioretti, E. Peroxynitrite-mediated oxidation of fibrinogen inhibits clot formation. FEBS Lett. 462 (1999) 236–240.

  22. 22.

    Pignatelli, B., Li, C.Q., Boffetta, P., Chen, Q., Ahrens, W., Nyberg, F., Mukeria, A., Bruske-Hohlfeld, I., Fortes, C., Constantinescu, V., Ischiropoulos, H. and Ohshima, H. Nitrated and oxidized plasma proteins in smokers and lung cancer patients. Cancer Res. 61 (2001) 778–784.

  23. 23.

    Pannala, A.S., Rice-Evans, C.A., Halliwell, B. and Singh, S. Inhibition of peroxynitrite-mediated tyrosine nitration by catechin polyphenols. Biochem. Biophys. Res. Commun. 232 (1997) 164–168.

  24. 24.

    Radi, R., Beckman, J.S., Bush, K.M. and Freeman, B.A. Peroxynitrite-induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide. Arch. Biochem. Biophys. 288 (1991) 481–487.

  25. 25.

    Klotz, L.O. and Sies, H. Defenses against peroxynitrite: selenocompounds and flavonoids. Toxicol. Lett. 140 (2003) 125–132.

  26. 26.

    Dinis, T.C., Santosa, C.L. and Almeida, L.M. The apoprotein is the preferential target for peroxynitrite-induced LDL damage protection by dietary phenolic acids. Free Radic. Res. 36 (2002) 531–543.

  27. 27.

    Sies, H., Klotz, L.O., Sharov, V.S., Assmann, A. and Briviba, K. Protection against peroxynitrite by selenoproteins. Z. Naturforsch. 53 (1998) 228–232.

  28. 28.

    Assmann, A., Briviba, K. and Sies, H. Reduction of methionine selenoxide to selenomethionine by glutathione. Arch. Biochem. Biophys. 349 (1998) 201–203.

  29. 29.

    Mouithys-Mickalad, M.A., Faez, J.M., Chistiaens, L., Kohnen, S., Deby, C., Hoebeke, M., Lamy, M. and Deby-Dupont, G. In vitro evaluation of glutathione peroxidase (GPx)-like activity and antioxidant properties of some Ebselen analogues. Redox. Rep. 9 (2004) 81–87.

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Correspondence to Paweł Nowak.

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Key words

  • Peroxynitrite
  • Tyrosine nitration
  • Carbonyl groups
  • Selenium
  • Ebselen