메뉴 건너뛰기




Volumn 22, Issue 5, 1997, Pages 577-582

Lipid peroxidation and antioxidant systems in rat brain: Effect of chronic alcohol consumption

Author keywords

Brain; ethanol; lipid peroxidation

Indexed keywords

ANTIOXIDANT; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; THIOBARBITURIC ACID REACTIVE SUBSTANCE;

EID: 0030946271     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1022418002765     Document Type: Article
Times cited : (33)

References (42)
  • 2
    • 0022536760 scopus 로고
    • Ferritin, a physiological iron donor for microsomal lipid peroxidation
    • Koster, J. F., and Slee, R. G. 1986. Ferritin, a physiological iron donor for microsomal lipid peroxidation. FEBS Lett. 199:85-88.
    • (1986) FEBS Lett. , vol.199 , pp. 85-88
    • Koster, J.F.1    Slee, R.G.2
  • 3
    • 0023779695 scopus 로고
    • Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Is haemoglobin a biological Fenton reagent?
    • 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.
    • (1988) Biochem. J. , vol.249 , pp. 185-190
    • Puppo, A.1    Halliwell, B.2
  • 4
    • 0018145231 scopus 로고
    • Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates. Is it a mechanism for hydroxyl radical production in biochemical systems?
    • 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.
    • (1978) FEBS Lett. , vol.192 , pp. 321-326
    • Halliwell, B.1
  • 5
    • 0019876466 scopus 로고
    • Oxidation of arachidonic acid in micelles by superoxide and hydrogen peroxide
    • 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.
    • (1981) J. Biol. Chem. , vol.256 , pp. 260-265
    • Fridovich, S.E.1    Porter, N.A.2
  • 6
    • 0021265182 scopus 로고
    • Damaging effects of oxygen radicals on resealed erythrocyte ghosts
    • Girotti, A. W., and Thomas, J. P. 1984. Damaging effects of oxygen radicals on resealed erythrocyte ghosts. J. Biol. Chem. 259: 1744-1752.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1744-1752
    • Girotti, A.W.1    Thomas, J.P.2
  • 7
    • 0022853319 scopus 로고
    • The involvement of iron in lipid peroxidation
    • Braughler, J. M., Duncan, L. A., and Chase, R. L. 1986. The involvement of iron in lipid peroxidation. J. Biol. Chem. 261: 10282-10289.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10282-10289
    • Braughler, J.M.1    Duncan, L.A.2    Chase, R.L.3
  • 8
    • 0020701487 scopus 로고
    • Effect of hydrogen peroxide on the initiation of microsomal lipid peroxidation
    • 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.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 123-127
    • Morehouse, L.A.1    Tien, M.2    Bucher, J.R.3    Aust, S.D.4
  • 9
    • 0021114706 scopus 로고
    • The requirement for ferric iron in the initiation of lipid peroxidation by chelated ferrous iron
    • 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.
    • (1983) Biochem. Biophys. Res. Commun. , vol.111 , pp. 777-784
    • Bucher, J.R.1    Tien, M.2    Aust, S.D.3
  • 10
    • 0023154707 scopus 로고
    • The requirement for iron (III) in the initiation of lipid peroxidation by iron (II) and hydrogen peroxide
    • 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.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1098-1104
    • Minotti, G.1    Aust, S.D.2
  • 11
    • 0021021532 scopus 로고
    • Increased chemiluminescence and superoxide production in the liver of chronically ethanol-treated rats
    • 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.
    • (1983) Arch. Biochem. Biophys. , vol.227 , pp. 534-541
    • Boveris, A.1    Fraga, C.G.2    Varsavsky, A.I.3    Koch, O.R.4
  • 12
    • 0024546914 scopus 로고
    • Rat liver microsomal NADPH-supported oxidase activity and lipid peroxidation dependent on ethanol-inducible cytochrome P-450 (P-450 IIEI). Biochem
    • 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.
    • (1989) Pharmacol. , vol.38 , pp. 1313-1318
    • Ekstrom, G.1    Ingelman-Sundberg, M.2
  • 13
    • 0014930407 scopus 로고
    • Reduced nicotinamideadenine dinucleotide phosphate oxidase: Activity enhanced by ethanol consumption
    • Lieber, C. S., and De Carli, L. M. 1970. Reduced nicotinamideadenine dinucleotide phosphate oxidase: activity enhanced by ethanol consumption. Science 170:78-80.
    • (1970) Science , vol.170 , pp. 78-80
    • Lieber, C.S.1    De Carli, L.M.2
  • 14
    • 0015840893 scopus 로고
    • Induction of hepatic microsomal reduced nicotinamide adenine dinucleotide phosphate-dependent production of hydrogen peroxide by chronic prior treatment with ethanol
    • 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.
    • (1973) Mol. Pharmacol. , vol.9 , pp. 670-675
    • Thurman, R.G.1
  • 15
    • 0020416090 scopus 로고
    • Alcohol ingestion, liver glutathione and lipoperoxidation: Metabolic interrelations and pathological implications
    • Videla, L. A., and Valenzuela, A. 1982. Alcohol ingestion, liver glutathione and lipoperoxidation: metabolic interrelations and pathological implications. Life Sci. 31:2395-2407.
    • (1982) Life Sci. , vol.31 , pp. 2395-2407
    • Videla, L.A.1    Valenzuela, A.2
  • 16
    • 0026597915 scopus 로고
    • Redox cycling of iron and lipid peroxidation
    • Minotti, G., and Aust, S. 1992. Redox cycling of iron and lipid peroxidation. Lipids 27:219-226.
    • (1992) Lipids , vol.27 , pp. 219-226
    • Minotti, G.1    Aust, S.2
  • 19
    • 0017872475 scopus 로고
    • Microsomal lipid peroxidation
    • Fleischer S. and Packers (eds), Academic Press, New York
    • 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.
    • (1978) Methods in Enzymol. , vol.52 , pp. 302-310
    • Buege, J.A.1    Aust, S.D.2
  • 20
    • 0000024078 scopus 로고
    • Catalase
    • Bergmeyer HV (ed.). Academic Press Inc., New York
    • Aebi, H. E. 1974. Catalase. Pages 673-684, in Bergmeyer HV (ed.). Methods of enzymatic analysis, Academic Press Inc., New York.
    • (1974) Methods of Enzymatic Analysis , pp. 673-684
    • Aebi, H.E.1
  • 21
    • 0017067418 scopus 로고
    • Glutathione peroxidase activity in selenium-deficient rat liver
    • Lawrence, R. A., and Burk, R. F. 1976. Glutathione peroxidase activity in selenium-deficient rat liver. Biochim. Biophys. Res. Commun. 71:952-959.
    • (1976) Biochim. Biophys. Res. Commun. , vol.71 , pp. 952-959
    • Lawrence, R.A.1    Burk, R.F.2
  • 22
    • 0024991845 scopus 로고
    • Determination of superoxide dismutase activity by purely chemical system based on NAD(P)H oxidation
    • Packer L. and Glazer A. N. (eds). Academic Press. Inc., New York
    • 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.
    • (1990) Methods in Enzymol. , vol.186 , pp. 209-220
    • Paoletti, F.1    Mocali, A.2
  • 23
    • 0021307110 scopus 로고
    • Reversible inactivation of Saccharomyces cerevisiae glutathione reductase under reducing conditions
    • 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.
    • (1984) Arch. Biochem. Biophys. , vol.228 , pp. 1-12
    • Pinto, M.C.1    Mata, A.M.2    Lopez-Barea, J.3
  • 24
    • 0001152378 scopus 로고
    • Glutathione and glutathione disulphide
    • Bergmeyer H. V. (ed). Academic Press Inc, New York
    • 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.
    • (1985) Methods of Enzymatic Analysis , vol.8 , pp. 521-529
    • Griffith, O.W.1
  • 25
    • 0027425091 scopus 로고
    • Stimulation of Fe-induced lipid peroxidation in phosphatidylcholine liposomes by aluminum ions at physiological pH
    • 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.
    • (1993) Biochim. Biophys. Acta. , vol.1170 , pp. 182-188
    • Ohyashiki, T.1    Karino, T.2    Matsui, K.3
  • 26
    • 0025755648 scopus 로고
    • Changes in Cu,Zn-Superoxide Dismutase, Cytochrome c Oxidase, Glutathione Peroxidase and Glutathione Transferase activities in copper-deficient mice and rats
    • 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.
    • (1990) J. Nutr. , vol.121 , pp. 355-36333
    • Prohaska, J.1
  • 27
    • 0016436517 scopus 로고
    • A possible mechanism for the peroxidation of lipids due to chronic ethanol ingestion
    • Reitz, R. C. 1975. A possible mechanism for the peroxidation of lipids due to chronic ethanol ingestion. Biochim. Biophys. Acta. 380:145-154.
    • (1975) Biochim. Biophys. Acta. , vol.380 , pp. 145-154
    • Reitz, R.C.1
  • 28
    • 0025040813 scopus 로고
    • Cytochrome P 450-dependent formation of oxygen radicals. Isoenzyme-specific inhibition of P 450 mediated reduction of oxygen and carbon tetrachloride
    • 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.
    • (1990) Xenobiotica , vol.20 , pp. 887-900
    • Persson, J.O.1    Terelius, Y.2    Ingelman-Sundberg, M.3
  • 30
    • 0025356936 scopus 로고
    • Regional distribution of ethanol-inducible cytochrome P 450 IIEI in the rat central nervous system
    • 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.
    • (1990) Neuroscience , vol.34 , pp. 451-463
    • Hansson, T.1    Tindberg, N.2    Ingelman-Sundberg, M.3    Kuhler, C.4
  • 31
    • 0028332490 scopus 로고
    • Increased production of reactive oxygen species by rat liver mitochondria after chronic ethanol treatment
    • 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.
    • (1994) Archives Biochem. Biophys. , vol.309 , pp. 377-386
    • Kukielka, E.1    Dicker, E.2    Cederbaum, A.3
  • 32
    • 0016816804 scopus 로고
    • The interaction of bovine erythrocyte Superoxide Dismutase with hydrogen peroxide: Inactivation of the enzyme
    • 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.
    • (1975) Biochemistry , vol.14 , pp. 5294-5299
    • Hodgson, E.K.1    Fridovich, I.2
  • 33
    • 0019414662 scopus 로고
    • Superoxide dismutase activity in rat brain during acute and chronic alcohol intoxication
    • 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.
    • (1981) Neurochem. Res. , vol.6 , pp. 385-391
    • Ledig, M.1    M'Paria, J.R.2    Mandel, P.3
  • 34
    • 0029161895 scopus 로고
    • Liver antioxidant defenses in mice fed ethanol and the AIN-76A diet
    • 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.
    • (1995) Alcohol , vol.12 , pp. 453-457
    • Chen, L.H.1    Xi, S.2    Cohen, D.A.3
  • 35
    • 0029074301 scopus 로고
    • Antioxidant defense mechanisms in the female rat: Interactions with alcohol, copper, and type of dietary carbohydrate
    • 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.
    • (1995) Alcohol , vol.12 , pp. 227-231
    • Fields, M.1    Lewis, C.G.2
  • 36
    • 0021183055 scopus 로고
    • Liver Superoxide dismutases and catalase during ethanol inhalation and withdrawal
    • Ribiere, C., Sinaceur, J., and Nordmann, R. 1983. Liver Superoxide dismutases and catalase during ethanol inhalation and withdrawal. Pharmacol. Biochem. Behav. 18:263-266.
    • (1983) Pharmacol. Biochem. Behav. , vol.18 , pp. 263-266
    • Ribiere, C.1    Sinaceur, J.2    Nordmann, R.3
  • 37
    • 0021884007 scopus 로고
    • Effects of chronic ethanol feeding on glutathione turnover in the rat
    • Morton, S., and Mitchell, M. C. 1985. Effects of chronic ethanol feeding on glutathione turnover in the rat. Biochem. Pharmacol. 34:1559-1563.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 1559-1563
    • Morton, S.1    Mitchell, M.C.2
  • 38
    • 0025952695 scopus 로고
    • Autoradiographic study of iron-binding sites in the rat brain: Distribution and relationship to aging
    • 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.
    • (1991) J. Neurosci. Res. , vol.29 , pp. 390-395
    • Barkai, A.I.1    Durkin, M.2    Dwork, A.J.3    Nelson, H.D.4
  • 39
    • 0028799569 scopus 로고
    • Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake
    • 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.
    • (1995) Archiv. Biochem. Biophys. , vol.316 , pp. 128-134
    • Martins, E.A.1    Robalinho, R.L.2    Meneghini, R.3
  • 40
    • 0024994241 scopus 로고
    • On the limited ability of superoxide to release iron from ferritin
    • 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.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 899-904
    • Bolann, B.J.1    Ulvik, R.J.2
  • 41
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • 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.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 42
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich, I. 1995. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64:97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.