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Volumn 24, Issue 4, 2000, Pages 544-552

Formation of malondialdehyde adducts in livers of rats exposed to ethanol: Role in ethanol mediated inhibition of cytochrome c oxidase

Author keywords

Cytochrome c Oxidase; Ethanol; Malondialdehyde; Mitochondria; Protein Adducts

Indexed keywords

4 HYDROXYNONENAL; ALCOHOL; CYTOCHROME C OXIDASE; MALONALDEHYDE;

EID: 0034060591     PISSN: 01456008     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1530-0277.2000.tb02023.x     Document Type: Article
Times cited : (79)

References (54)
  • 2
    • 0031911322 scopus 로고    scopus 로고
    • Increased circulating products of lipid peroxidation in patients with alcoholic liver disease
    • Aleynik SI, Leo MA, Aleynik MK, Lieber CS (1998) Increased circulating products of lipid peroxidation in patients with alcoholic liver disease. Alcohol Clin Exp Res 22:192-196.
    • (1998) Alcohol Clin Exp Res , vol.22 , pp. 192-196
    • Aleynik, S.I.1    Leo, M.A.2    Aleynik, M.K.3    Lieber, C.S.4
  • 3
    • 0032847556 scopus 로고    scopus 로고
    • Ethanol stimulates the production of reactive oxygen species at mitochondrial complexes I and II
    • Bailey SM, Pietsch EC, Cunningham CC (1999) Ethanol stimulates the production of reactive oxygen species at mitochondrial complexes I and II. Free Rad Biol Med 27:891-900.
    • (1999) Free Rad Biol Med , vol.27 , pp. 891-900
    • Bailey, S.M.1    Pietsch, E.C.2    Cunningham, C.C.3
  • 4
    • 0020317745 scopus 로고
    • Reaction of malondialdehyde with mitochondrial membranes
    • Balcavage WX (1982) Reaction of malondialdehyde with mitochondrial membranes. Mech Age Dev 19:159-170.
    • (1982) Mech Age Dev , vol.19 , pp. 159-170
    • Balcavage, W.X.1
  • 6
    • 0017872475 scopus 로고
    • Microsomal lipid peroxidation
    • Buege JA, Aust SD (1978) Microsomal lipid peroxidation. Methods Enzym 52:302-310.
    • (1978) Methods Enzym , vol.52 , pp. 302-310
    • Buege, J.A.1    Aust, S.D.2
  • 8
    • 0025322981 scopus 로고
    • Structure and function of cytochrome c oxidase
    • Capaldi RA (1990) Structure and function of cytochrome c oxidase. Annu Rev Biochem 59:569-596.
    • (1990) Annu Rev Biochem , vol.59 , pp. 569-596
    • Capaldi, R.A.1
  • 9
    • 0028153306 scopus 로고
    • Role of nuclear-encoded subunits of mitochondrial cytochrome c oxidase in proton pumping revealed by limited enzymatic proteolysis
    • Capitanio N, Peccarisi R, Capitanio G, Villani G, De Nitto E, Scacco S, Papa S (1994) Role of nuclear-encoded subunits of mitochondrial cytochrome c oxidase in proton pumping revealed by limited enzymatic proteolysis. Biochemistry 33:12521-12526.
    • (1994) Biochemistry , vol.33 , pp. 12521-12526
    • Capitanio, N.1    Peccarisi, R.2    Capitanio, G.3    Villani, G.4    De Nitto, E.5    Scacco, S.6    Papa, S.7
  • 10
    • 0027944443 scopus 로고
    • Alterations in mitochondrial membrane fluidity by lipid peroxidation products
    • Chen JJ, Yu BP (1994) Alterations in mitochondrial membrane fluidity by lipid peroxidation products. Free Rad Biol Med 17:411-418.
    • (1994) Free Rad Biol Med , vol.17 , pp. 411-418
    • Chen, J.J.1    Yu, B.P.2
  • 11
    • 0029165212 scopus 로고
    • Inhibition of mitochondrial adenine nucleotide translocator by lipid peroxidation products
    • Chen JJ, Bertrand AH, Yu BP (1995) Inhibition of mitochondrial adenine nucleotide translocator by lipid peroxidation products. Free Rad Biol Med 19:583-590.
    • (1995) Free Rad Biol Med , vol.19 , pp. 583-590
    • Chen, J.J.1    Bertrand, A.H.2    Yu, B.P.3
  • 12
    • 0031030464 scopus 로고    scopus 로고
    • 4-Hydroxynonenal levels are enhanced in fetal liver mitochondria by in utero ethanol exposure
    • Chen J, Schenker S, Henderson GI (1997) 4-Hydroxynonenal levels are enhanced in fetal liver mitochondria by in utero ethanol exposure. Hepatology 25:142-147.
    • (1997) Hepatology , vol.25 , pp. 142-147
    • Chen, J.1    Schenker, S.2    Henderson, G.I.3
  • 13
    • 0032496339 scopus 로고    scopus 로고
    • Inhibition of cytochrome c oxidase activity by 4-hydroxynonenal (HNE): Role of HNE adduct formation with the enzyme subunits
    • Chen J, Schenker S, Frosto TA, Henderson GI (1998) Inhibition of cytochrome c oxidase activity by 4-hydroxynonenal (HNE): Role of HNE adduct formation with the enzyme subunits. Biochim Biophys Acta 1380:336-344.
    • (1998) Biochim Biophys Acta , vol.1380 , pp. 336-344
    • Chen, J.1    Schenker, S.2    Frosto, T.A.3    Henderson, G.I.4
  • 14
    • 0032996250 scopus 로고    scopus 로고
    • Formation of 4-hydroxynonenal adducts with cytochrome c oxidase in rats following short-term ethanol intake
    • Chen J, Robinson NC, Schenker S, Frosto TA, Henderson GI (1999) Formation of 4-hydroxynonenal adducts with cytochrome c oxidase in rats following short-term ethanol intake. Hepatology 29:1792-1798.
    • (1999) Hepatology , vol.29 , pp. 1792-1798
    • Chen, J.1    Robinson, N.C.2    Schenker, S.3    Frosto, T.A.4    Henderson, G.I.5
  • 15
    • 0018092417 scopus 로고
    • The fetal alcohol syndrome
    • Clarren SK, Smith DW (1978) The fetal alcohol syndrome. N Engl J Med 298:1063-1067.
    • (1978) N Engl J Med , vol.298 , pp. 1063-1067
    • Clarren, S.K.1    Smith, D.W.2
  • 16
    • 0025909968 scopus 로고
    • Effect of ethanol consumption on hepatic mitochondrial transcription and translation
    • Coleman WB, Cunningham CC (1991) Effect of ethanol consumption on hepatic mitochondrial transcription and translation. Biochim Biophys Acta 1058:178-186.
    • (1991) Biochim Biophys Acta , vol.1058 , pp. 178-186
    • Coleman, W.B.1    Cunningham, C.C.2
  • 17
    • 0027250368 scopus 로고
    • Effect of ethanol on rat fetal hepatocytes: Studies on replication, lipid peroxidation and glutathione
    • Devi BG, Henderson GI, Frosto TA, Schenker S (1993) Effect of ethanol on rat fetal hepatocytes: Studies on replication, lipid peroxidation and glutathione. Hepatology 18:648-659.
    • (1993) Hepatology , vol.18 , pp. 648-659
    • Devi, B.G.1    Henderson, G.I.2    Frosto, T.A.3    Schenker, S.4
  • 18
    • 0028564690 scopus 로고
    • Effect of acute ethanol exposure on cultured fetal rat hepatocytes: Relation to mitochondrial function
    • Devi BG, Henderson GI, Frosto TA, Schenker S (1994) Effect of acute ethanol exposure on cultured fetal rat hepatocytes: Relation to mitochondrial function. Alcohol Clin Exp Res 18:1436-1442.
    • (1994) Alcohol Clin Exp Res , vol.18 , pp. 1436-1442
    • Devi, B.G.1    Henderson, G.I.2    Frosto, T.A.3    Schenker, S.4
  • 19
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde, and related aldehydes
    • Esterbauer H, Schaur RJ, Zollner H (1991) Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde, and related aldehydes. Free Rad Biol Med 11:81-128.
    • (1991) Free Rad Biol Med , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 20
    • 0028868238 scopus 로고
    • Feeding S-adenosyl-L-methionine attenuates both ethanol-induced depletion of mitochondrial glutathione and mitochondrial dysfunction in periportal and perivenous rat hepatocytes
    • Garcia-Ruiz C, Morales A, Colell A, Ballesta A, Rodes J, Kaplowitz N, Fernandez-Checa JC (1995) Feeding S-adenosyl-L-methionine attenuates both ethanol-induced depletion of mitochondrial glutathione and mitochondrial dysfunction in periportal and perivenous rat hepatocytes. Hepatology 21:207-214.
    • (1995) Hepatology , vol.21 , pp. 207-214
    • Garcia-Ruiz, C.1    Morales, A.2    Colell, A.3    Ballesta, A.4    Rodes, J.5    Kaplowitz, N.6    Fernandez-Checa, J.C.7
  • 21
    • 0020490497 scopus 로고
    • Quantification of the contribution of various steps of the control of mitochondrial respiration
    • Groen AK, Wanders RJA, Westerholl HV, van der Meer R, Tager JM (1982) Quantification of the contribution of various steps of the control of mitochondrial respiration. J Biol Chem 257:2754-2757.
    • (1982) J Biol Chem , vol.257 , pp. 2754-2757
    • Groen, A.K.1    Wanders, R.J.A.2    Westerholl, H.V.3    Van Der Meer, R.4    Tager, J.M.5
  • 22
    • 0030751667 scopus 로고    scopus 로고
    • Prooxidant-initiated lipid peroxidation in isolated rat hepatocytes:Detection of 4-hydroxynonenal- and malondialdehyde-protein adducts
    • Hartley DP, Kroll DJ, Peterson DR (1997) Prooxidant-initiated lipid peroxidation in isolated rat hepatocytes:detection of 4-hydroxynonenal- and malondialdehyde-protein adducts. Chem Res Toxicol 10:895-905.
    • (1997) Chem Res Toxicol , vol.10 , pp. 895-905
    • Hartley, D.P.1    Kroll, D.J.2    Peterson, D.R.3
  • 23
    • 0026493715 scopus 로고
    • Hepatic mitochondrial glutathione depletion and progression of experimental alcoholic liver disease in rats
    • Hirano T, Kaplowitz N, Tsukamoto H, Kamimura S, Fernandez-Checa JC (1992) Hepatic mitochondrial glutathione depletion and progression of experimental alcoholic liver disease in rats. Hepatology 16:1423-1427.
    • (1992) Hepatology , vol.16 , pp. 1423-1427
    • Hirano, T.1    Kaplowitz, N.2    Tsukamoto, H.3    Kamimura, S.4    Fernandez-Checa, J.C.5
  • 24
    • 0021960813 scopus 로고
    • Structure of the cytochrome c oxidase complex of rat liver: I. Studies on nearest-neighbor relationship of polypeptides with cross-linking reagents
    • Jarausch J, Kadenbach B (1985) Structure of the cytochrome c oxidase complex of rat liver: I. Studies on nearest-neighbor relationship of polypeptides with cross-linking reagents. Eur J Biochem 146:211-217.
    • (1985) Eur J Biochem , vol.146 , pp. 211-217
    • Jarausch, J.1    Kadenbach, B.2
  • 25
    • 0031878858 scopus 로고    scopus 로고
    • Induction of cell cycle arrest by the endogenous product of lipid peroxidation, malondialdehyde
    • Ji Chuan, Touzer CA, Marnett LJ, Pietenpol, JA (1998) Induction of cell cycle arrest by the endogenous product of lipid peroxidation, malondialdehyde. Carcinogenesis 19:1275-1283.
    • (1998) Carcinogenesis , vol.19 , pp. 1275-1283
    • Chuan, J.1    Touzer, C.A.2    Marnett, L.J.3    Pietenpol, J.A.4
  • 26
    • 0026717172 scopus 로고
    • Increased 4-hydroxynonenal levels in experimental alcoholic liver disease: Association of lipid peroxidation with liver fibrogenesis
    • Kamimura S, Gaal K, Britton RS, Bacon RB, Triadofilopaulos C, Tsukamoto H (1992) Increased 4-hydroxynonenal levels in experimental alcoholic liver disease: Association of lipid peroxidation with liver fibrogenesis. Hepatology 16:448-453.
    • (1992) Hepatology , vol.16 , pp. 448-453
    • Kamimura, S.1    Gaal, K.2    Britton, R.S.3    Bacon, R.B.4    Triadofilopaulos, C.5    Tsukamoto, H.6
  • 27
    • 0027256279 scopus 로고
    • Ventricular mitochondrial gene expression during development and following embryonic ethanol exposure
    • Kennedy JM, Kelley SW, Meehan JM (1993) Ventricular mitochondrial gene expression during development and following embryonic ethanol exposure. J Mol Cell Cardiol 25:117-131.
    • (1993) J Mol Cell Cardiol , vol.25 , pp. 117-131
    • Kennedy, J.M.1    Kelley, S.W.2    Meehan, J.M.3
  • 28
    • 0026657468 scopus 로고
    • The effect of chronic ethanol consumption on NADH- and NADPH-dependent generation of reactive oxygen intermediates by isolated rat liver nuclei
    • Kukielka E, Cederbaum AI (1992) The effect of chronic ethanol consumption on NADH- and NADPH-dependent generation of reactive oxygen intermediates by isolated rat liver nuclei. Alcohol 27:233-239.
    • (1992) Alcohol , vol.27 , pp. 233-239
    • Kukielka, E.1    Cederbaum, A.I.2
  • 29
    • 0028332490 scopus 로고
    • Increased production of reactive oxygen species by rat liver mitochondria after chronic ethanol treatment
    • Kukielka E, Dicher E, Cederbaum AI (1994) Increased production of reactive oxygen species by rat liver mitochondria after chronic ethanol treatment. Arch Biochem Biophys 309:377-386.
    • (1994) Arch Biochem Biophys , vol.309 , pp. 377-386
    • Kukielka, E.1    Dicher, E.2    Cederbaum, A.I.3
  • 30
    • 0030820474 scopus 로고    scopus 로고
    • Acetaldehyde-modified and 4-hydroxynonenal-modified proteins in the livers of rats with alcoholic liver disease
    • Li CJ, Nanji AA, Siakotos AN, Lin RC (1997) Acetaldehyde-modified and 4-hydroxynonenal-modified proteins in the livers of rats with alcoholic liver disease. Hepatology 26:650-657.
    • (1997) Hepatology , vol.26 , pp. 650-657
    • Li, C.J.1    Nanji, A.A.2    Siakotos, A.N.3    Lin, R.C.4
  • 33
    • 0025061009 scopus 로고
    • Effect of changing the detergent bound to bovine cytochrome c oxidase upon its individual electrontransfer steps
    • Mahapatro SN, Robinson NC (1990) Effect of changing the detergent bound to bovine cytochrome c oxidase upon its individual electrontransfer steps. Biochemistry 29:764-770.
    • (1990) Biochemistry , vol.29 , pp. 764-770
    • Mahapatro, S.N.1    Robinson, N.C.2
  • 35
    • 0032407770 scopus 로고    scopus 로고
    • Early alcoholic liver injury: Formation of protein adducts with acetaldehyde and lipid peroxidation products, and expression of CYP2E1 and CYP3A
    • Niemela O, Parkkila S, Pasanen M, Iimur Y, Bradford B, Thurman RG (1998) Early alcoholic liver injury: Formation of protein adducts with acetaldehyde and lipid peroxidation products, and expression of CYP2E1 and CYP3A. Alcohol Clin Exp Res 22:2118-2124.
    • (1998) Alcohol Clin Exp Res , vol.22 , pp. 2118-2124
    • Niemela, O.1    Parkkila, S.2    Pasanen, M.3    Iimur, Y.4    Bradford, B.5    Thurman, R.G.6
  • 36
    • 0026554148 scopus 로고
    • Implications of free radical mechanisms in ethanol-induced cellular injury
    • Nordmann R, Ribiere C, Rouach H (1992) Implications of free radical mechanisms in ethanol-induced cellular injury. Free Rad Biol Med 12:219-240.
    • (1992) Free Rad Biol Med , vol.12 , pp. 219-240
    • Nordmann, R.1    Ribiere, C.2    Rouach, H.3
  • 39
    • 0017278865 scopus 로고
    • Studies on cytochrome oxidase
    • Phan SH, Mahler HR (1976) Studies on cytochrome oxidase. J Biol Chem 251:257-269.
    • (1976) J Biol Chem , vol.251 , pp. 257-269
    • Phan, S.H.1    Mahler, H.R.2
  • 40
    • 0023726683 scopus 로고
    • Measurement of cytochrome c oxidase activity in human liver specimens obtained by needle biopsy
    • Sakai Y, Tanaka A, Ikai I, Yamaoka Y, Ozawa K, Orii Y (1988) Measurement of cytochrome c oxidase activity in human liver specimens obtained by needle biopsy. Clin Chim Acta 176:343-346.
    • (1988) Clin Chim Acta , vol.176 , pp. 343-346
    • Sakai, Y.1    Tanaka, A.2    Ikai, I.3    Yamaoka, Y.4    Ozawa, K.5    Orii, Y.6
  • 42
    • 0033016131 scopus 로고    scopus 로고
    • Dose- and time-dependent effects of ethanol on plasma antioxidant system in rat
    • Schlorff EC, Husain K, Somani SM (1999) Dose- and time-dependent effects of ethanol on plasma antioxidant system in rat. Alcohol 17(2): 97-105.
    • (1999) Alcohol , vol.17 , Issue.2 , pp. 97-105
    • Schlorff, E.C.1    Husain, K.2    Somani, S.M.3
  • 43
    • 0028143826 scopus 로고
    • Differential susceptibility of plasma proteins to oxidative modification. Examination by western blot immunoassay
    • Shacter E, Williams JA, Lim M, Levine RL (1994) Differential susceptibility of plasma proteins to oxidative modification. Examination by Western blot immunoassay. Free Rad Biol Med 17:429-437.
    • (1994) Free Rad Biol Med , vol.17 , pp. 429-437
    • Shacter, E.1    Williams, J.A.2    Lim, M.3    Levine, R.L.4
  • 44
    • 0019511768 scopus 로고
    • Ethanol-induced lipid peroxidation: Potentiation by long-term alcohol feeding and attenuation by methionine
    • Shaw S, Jayatilleke E, Ross WA, Gordon ER, Lieber CS (1981) Ethanol-induced lipid peroxidation: Potentiation by long-term alcohol feeding and attenuation by methionine. J Lab Clin Med 98:417-424.
    • (1981) J Lab Clin Med , vol.98 , pp. 417-424
    • Shaw, S.1    Jayatilleke, E.2    Ross, W.A.3    Gordon, E.R.4    Lieber, C.S.5
  • 45
    • 0023650072 scopus 로고
    • Bovine cytochrome c oxidase, purified from heart, skeletal muscle, liver and kidney, differ in the small subunits but show the same reaction kinetics with cytochrome c
    • Sinjorgo KMA, Durak I, Dekker HL, Edel CM, Hakvoort TBM, van Gelder BF, Muijsers AO (1987) Bovine cytochrome c oxidase, purified from heart, skeletal muscle, liver and kidney, differ in the small subunits but show the same reaction kinetics with cytochrome c. Biochim Biophys Acta 893:251-258.
    • (1987) Biochim Biophys Acta , vol.893 , pp. 251-258
    • Sinjorgo, K.M.A.1    Durak, I.2    Dekker, H.L.3    Edel, C.M.4    Hakvoort, T.B.M.5    Van Gelder, B.F.6    Muijsers, A.O.7
  • 46
    • 0023472381 scopus 로고
    • Control of state 3 respiration in liver mitochondria from rats subjected to chronic ethanol consumption
    • Spach PI, Cunningham CC (1987) Control of state 3 respiration in liver mitochondria from rats subjected to chronic ethanol consumption. Biochim Biophys Acta 894:460-467.
    • (1987) Biochim Biophys Acta , vol.894 , pp. 460-467
    • Spach, P.I.1    Cunningham, C.C.2
  • 47
    • 0024603895 scopus 로고
    • Beyond cholesterol: Modification of low density lipoprotein that increases its atherogenicity
    • Steinberg D, Parthasarathy S, Carew TE, Khoo JC, Witztum JL (1989) Beyond cholesterol: Modification of low density lipoprotein that increases its atherogenicity. N Eng J Med 320:915-924.
    • (1989) N Eng J Med , vol.320 , pp. 915-924
    • Steinberg, D.1    Parthasarathy, S.2    Carew, T.E.3    Khoo, J.C.4    Witztum, J.L.5
  • 48
    • 0022539785 scopus 로고
    • Immunochemical evidence for an inactive form of cytochrome oxidase in mitochondria membranes of ethanol-fed rats
    • Thayer WS, Rubin E (1986) Immunochemical evidence for an inactive form of cytochrome oxidase in mitochondria membranes of ethanol-fed rats. Biochim Biophys Acta 849:366-373.
    • (1986) Biochim Biophys Acta , vol.849 , pp. 366-373
    • Thayer, W.S.1    Rubin, E.2
  • 49
    • 0029144666 scopus 로고
    • Roles of oxidative stress in activation of Kupffer and ito cells in liver fibrogenesis
    • Tsukamoto H, Rippe R, Niemela O, Lin M (1995a) Roles of oxidative stress in activation of Kupffer and Ito cells in liver fibrogenesis. J Gastroenterol Hepatol(Suppl) 10:S50-S53.
    • (1995) J Gastroenterol Hepatol(suppl) , vol.10
    • Tsukamoto, H.1    Rippe, R.2    Niemela, O.3    Lin, M.4
  • 51
    • 0030001945 scopus 로고    scopus 로고
    • Acetaldehyde and malondialdehyde react together to generate distinct protein adducts in the liver during long-term ethanol administration
    • Tuma DJ, Thiele GM, Xu D, Klassen LW, Sorrell MF (1996) Acetaldehyde and malondialdehyde react together to generate distinct protein adducts in the liver during long-term ethanol administration. Hepatology 23:872-880.
    • (1996) Hepatology , vol.23 , pp. 872-880
    • Tuma, D.J.1    Thiele, G.M.2    Xu, D.3    Klassen, L.W.4    Sorrell, M.F.5
  • 52
    • 0026606054 scopus 로고
    • Modification of histidine residues in proteins by reaction with 4-hydroxynonenal
    • Uchida K, Stadtman ER (1992) Modification of histidine residues in proteins by reaction with 4-hydroxynonenal. Proc Natl Acad Sci USA 89:4544-4548.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4544-4548
    • Uchida, K.1    Stadtman, E.R.2
  • 53
    • 0033535440 scopus 로고    scopus 로고
    • Analysis of DNA-protein crosslinking activity of malondialdehyde in vitro
    • Voitkun V, Zhitkovich A (1999) Analysis of DNA-protein crosslinking activity of malondialdehyde in vitro. Mutation Res 424:97-106.
    • (1999) Mutation Res , vol.424 , pp. 97-106
    • Voitkun, V.1    Zhitkovich, A.2
  • 54
    • 0032491195 scopus 로고    scopus 로고
    • Novel function of the regulatory subunit of protein kinase a: Regulation of cytochrome c oxidase activity and cytochrome c release
    • Yang WL, Iacono L, Tang WM, Chin KV (1998) Novel function of the regulatory subunit of protein kinase A: Regulation of cytochrome c oxidase activity and cytochrome c release. Biochemistry 37:14175-14180.
    • (1998) Biochemistry , vol.37 , pp. 14175-14180
    • Yang, W.L.1    Iacono, L.2    Tang, W.M.3    Chin, K.V.4


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