Skip to main content
Log in

Lipid Peroxidation and Antioxidant Systems in Rat Brain: Effect of Chronic Alcohol Consumption

  • Published:
Neurochemical Research Aims and scope Submit manuscript

Abstract

The effect of chronic ethanol exposure, in a liquid diet, on lipid peroxidation and some antioxidant systems of rat brain was investigated. Chronic ethanol administration induced a greater susceptibility to iron/ascorbate-induced lipid peroxidation, estimated as thiobarbituric reactive substances (TBARS) production, in the microsomal fraction, but a lower lipid peroxidation in the total homogenate. Glutathione (GSH) levels as well as GSH peroxidase and GSH reductase were unaffected, while the activity of Cu-Zn superoxide dismutase was decreased and that of catalase increased. Lipid peroxidation experiments performed in the presence of some hydroxyl radical scavengers suggested that a greater OH· generation may be responsible of the greater TBARS production in the microsomal fraction of ethanol treated rats; differently, in total homogenate of control and ethanol rats a relationship was found between the redox state of iron and TBARS production, suggesting that the lower lipid peroxidation in treated rats may depend on a different modulation of the iron redox state.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

REFERENCES

  1. Benzi, G. 1988. Peroxidation, energy transduction and mitochondria during aging, pp. 51–117. John Libbey Eurotext, London.

    Google Scholar 

  2. Koster, J. F., and Slee, R. G. 1986. Ferritin, a physiological iron donor for microsomal lipid peroxidation. FEBS Lett. 199:85–88.

    Google Scholar 

  3. Puppo, A., and Halliwell, B. 1988. Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Is haemoglobin a biological Fenton reagent? Biochem. J. 249:185–190.

    Google Scholar 

  4. Halliwell, B. 1978. Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates. Is it a mechanism for hydroxyl radical production in biochemical systems? FEBS Lett. 192:321–326.

    Google Scholar 

  5. Fridovich, S. E., and Porter, N. A. 1981. Oxidation of arachidonic acid in micelles by superoxide and hydrogen peroxide. J. Biol. Chem. 256:260–265.

    Google Scholar 

  6. Girotti, A. W., and Thomas, J. P. 1984. Damaging effects of oxygen radicals on resealed erythrocyte ghosts. J. Biol. Chem. 259:1744–1752.

    Google Scholar 

  7. Braughler, J. M., Duncan, L. A., and Chase, R. L. 1986. The involvement of iron in lipid peroxidation. J. Biol. Chem. 261:10282–10289.

    Google Scholar 

  8. Morehouse, L. A., Tien, M., Bucher, J. R., and Aust, S. D. 1983. Effect of hydrogen peroxide on the initiation of microsomal lipid peroxidation. Biochem. Pharmacol. 32:123–127.

    Google Scholar 

  9. Bucher, J. R., Tien, M., and Aust, S. D. 1983. The requirement for ferric iron in the initiation of lipid peroxidation by chelated ferrous iron. Biochem. Biophys. Res. Commun. 111:777–784.

    Google Scholar 

  10. Minotti, G., and Aust, S. D. 1987. The requirement for iron (III) in the initiation of lipid peroxidation by iron (II) and hydrogen peroxide. J. Biol. Chem. 262:1098–1104.

    Google Scholar 

  11. Boveris, A., Fraga, C. G., Varsavsky, A. I., and Koch, O. R. 1983. Increased chemiluminescence and superoxide production in the liver of chronically ethanol-treated rats. Arch. Biochem. Biophys. 227:534–541.

    Google Scholar 

  12. Ekstrom, G., and Ingelman-Sundberg, M. 1989. Rat liver microsomal NADPH-supported oxidase activity and lipid peroxidation dependent on ethanol-inducible cytochrome P-450 (P-450 IIEI). Biochem. Pharmacol. 38:1313–1318.

    Google Scholar 

  13. Lieber, C. S., and De Carli, L. M. 1970. Reduced nicotinamide-adenine dinucleotide phosphate oxidase: activity enhanced by ethanol consumption. Science 170:78–80.

    Google Scholar 

  14. Thurman, R. G. 1973. Induction of hepatic microsomal reduced nicotinamide adenine dinucleotide phosphate-dependent production of hydrogen peroxide by chronic prior treatment with ethanol. Mol. Pharmacol. 9:670–675.

    Google Scholar 

  15. Videla, L. A., and Valenzuela, A. 1982. Alcohol ingestion, liver glutathione and lipoperoxidation: metabolic interrelations and pathological implications. Life Sci. 31:2395–2407.

    Google Scholar 

  16. Minotti, G., and Aust, S. 1992. Redox cycling of iron and lipid peroxidation. Lipids 27:219–226.

    Google Scholar 

  17. Morgan, I., Wolfe, L., Mandel, P., and Gombos, G. 1971. Isolation of plasma membranes from rat brain. Biochim. Biophys. Acta. 241:737–751.

    Google Scholar 

  18. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. 1951. Protein measurement with Folin phenol reagent. J. Biol. Chem. 193:265–275.

    Google Scholar 

  19. Buege, J. A., and Aust, S. D. 1978. Microsomal lipid peroxidation. Pages 302–310, in Fleischer S. and Packers (eds), Methods in Enzymol. vol. 52, Academic Press, New York.

    Google Scholar 

  20. Aebi, H. E. 1974. Catalase. Pages 673–684, in Bergmeyer HV (ed.). Methods of enzymatic analysis, Academic Press Inc., New York.

    Google Scholar 

  21. Lawrence, R. A., and Burk, R. F. 1976. Glutathione peroxidase activity in selenium-deficient rat liver. Biochim. Biophys. Res. Commun. 71:952–959.

    Google Scholar 

  22. Paoletti, F., and Mocali, A. 1990. Determination of superoxide dismutase activity by purely chemical system based on NAD(P)H oxidation. Pages 209–220, in Packer L. and Glazer A. N. (eds). Methods in Enzymol., vol 186, Academic Press. Inc., New York.

    Google Scholar 

  23. Pinto, M. C., Mata A. M., and Lopez-Barea, J. 1984. Reversible inactivation of Saccharomyces cerevisiae glutathione reductase under reducing conditions. Arch. Biochem. Biophys. 228:1–12.

    Google Scholar 

  24. Griffith, O. W. 1985. Glutathione and glutathione disulphide. Pages 521–529, in Bergmeyer H. V. (ed). Methods of enzymatic analysis., vol VIII, Academic Press Inc, New York.

    Google Scholar 

  25. Ohyashiki, T., Karino, T., and Matsui, K. 1993. Stimulation of Fe-induced lipid peroxidation in phosphatidylcholine liposomes by aluminum ions at physiological pH. Biochim. Biophys. Acta. 1170:182–188.

    Google Scholar 

  26. Prohaska, J. 1990. Changes in Cu,Zn-Superoxide Dismutase, Cytochrome c Oxidase, Glutathione Peroxidase and Glutathione Transferase activities in copper-deficient mice and rats. J. Nutr. 121:355–363.33.

    Google Scholar 

  27. Reitz, R. C. 1975. A possible mechanism for the peroxidation of lipids due to chronic ethanol ingestion. Biochim. Biophys. Acta. 380:145–154.

    Google Scholar 

  28. Persson, J. O., Terelius, Y., and Ingelman-Sundberg, M. 1990. Cytochrome P 450-dependent formation of oxygen radicals. Isoenzyme-specific inhibition of P 450 mediated reduction of oxygen and carbon tetrachloride. Xenobiotica 20:887–900.

    Google Scholar 

  29. Montoliu, C., Sancho-Tello, M. Azorin, I., Burgal, M., Vallés, S., Renau-Piqueras, J., and Guerri, C. 1995. Ethanol increases Cytochrome P4502E1 and induces oxidative stress in astrocytes. J. Neurochem. 65:2561–2570.

    Google Scholar 

  30. Hansson, T., Tindberg, N., Ingelman-Sundberg, M., and Kuhler, C. 1990. Regional distribution of ethanol-inducible cytochrome P 450 IIEI in the rat central nervous system. Neuroscience 34:451–463.

    Google Scholar 

  31. Kukielka, E., Dicker, E., and Cederbaum, A. 1994. Increased production of reactive oxygen species by rat liver mitochondria after chronic ethanol treatment. Archives Biochem. Biophys. 309:377–386.

    Google Scholar 

  32. Hodgson, E. K., and Fridovich, I. 1975. The interaction of bovine erythrocyte Superoxide Dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 14:5294–5299.

    Google Scholar 

  33. Ledig, M., M'Paria, J. R., and Mandel, P. 1981. Superoxide dismutase activity in rat brain during acute and chronic alcohol intoxication. Neurochem. Res. 6:385–391.

    Google Scholar 

  34. Chen, L. H., Xi, S., and Cohen, D. A. 1995. Liver antioxidant defenses in mice fed ethanol and the AIN-76A diet. Alcohol. 12:453–457.

    Google Scholar 

  35. Fields, M., and Lewis, C. G. 1995. Antioxidant defense mechanisms in the female rat: interactions with alcohol, copper, and type of dietary carbohydrate. Alcohol. 12:227–231.

    Google Scholar 

  36. Ribiere, C., Sinaceur, J., and Nordmann, R. 1983. Liver Superoxide dismutases and catalase during ethanol inhalation and withdrawal. Pharmacol. Biochem. Behav. 18:263–266.

    Google Scholar 

  37. Morton, S., and Mitchell, M. C. 1985. Effects of chronic ethanol feeding on glutathione turnover in the rat. Biochem. Pharmacol. 34:1559–1563.

    Google Scholar 

  38. Barkai, A. I., Durkin, M., Dwork, A. J., and Nelson, H. D. 1991. Autoradiographic study of iron-binding sites in the rat brain: distribution and relationship to aging. J. Neurosci. Res. 29:390–395.

    Google Scholar 

  39. Martins, E. A., Robalinho, R. L., and Meneghini, R. 1995. Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake. Archiv. Biochem. Biophys. 316:128–134.

    Google Scholar 

  40. Bolann, B. J., and Ulvik, R. J. 1990. On the limited ability of superoxide to release iron from ferritin. Eur. J. Biochem. 193:899–904.

    Google Scholar 

  41. Flint, D. H., Tuminello, J. F., and Emptage, M. H. 1993. The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J. Biol. Chem. 268:22369–22376.

    Google Scholar 

  42. Fridovich, I. 1995. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64:97–112.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Omodeo-Sale', F., Gramigna, D. & Campaniello, R. Lipid Peroxidation and Antioxidant Systems in Rat Brain: Effect of Chronic Alcohol Consumption. Neurochem Res 22, 577–582 (1997). https://doi.org/10.1023/A:1022418002765

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1022418002765

Navigation