메뉴 건너뛰기




Volumn 41, Issue 4, 2005, Pages 925-935

Mechanisms of benzarone and benzbromarone-induced hepatic toxicity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMIODARONE; BENZARONE; BENZBROMARONE; BENZOFURAN DERIVATIVE; CYTOCHROME C; GLUTAMIC ACID; KETONE BODY; REACTIVE OXYGEN METABOLITE; SUCCINIC ACID;

EID: 16244412284     PISSN: 02709139     EISSN: None     Source Type: Journal    
DOI: 10.1002/hep.20634     Document Type: Article
Times cited : (168)

References (46)
  • 2
    • 0029127584 scopus 로고
    • Inhibition of mitochondrial beta-oxidation as a mechanism of hepatotoxicity
    • Fromenty B, Pessayre D. Inhibition of mitochondrial beta-oxidation as a mechanism of hepatotoxicity. Pharmacol Ther 1995;67:101-154.
    • (1995) Pharmacol Ther , vol.67 , pp. 101-154
    • Fromenty, B.1    Pessayre, D.2
  • 3
    • 0030985809 scopus 로고    scopus 로고
    • Fulminant liver failure in association with the emetic toxin of Bacillus cereus
    • Mahler H, Pasi A, Kramer JM, Schulte P, Scoging AC, Bar W, et al. Fulminant liver failure in association with the emetic toxin of Bacillus cereus. N Engl J Med 1997;336:1142-1148.
    • (1997) N Engl J Med , vol.336 , pp. 1142-1148
    • Mahler, H.1    Pasi, A.2    Kramer, J.M.3    Schulte, P.4    Scoging, A.C.5    Bar, W.6
  • 4
    • 0025677186 scopus 로고
    • Amiodarone inhibits the mitochondrial beta-oxidation of fatty acids and produces microvesicular steatosis of the liver in mice
    • Fromenty B, Fisch C, Labbe G, Degott C, Deschamps D, Berson A, et al. Amiodarone inhibits the mitochondrial beta-oxidation of fatty acids and produces microvesicular steatosis of the liver in mice. J Pharmacol Exp Ther 1990;255:1371-1376.
    • (1990) J Pharmacol Exp Ther , vol.255 , pp. 1371-1376
    • Fromenty, B.1    Fisch, C.2    Labbe, G.3    Degott, C.4    Deschamps, D.5    Berson, A.6
  • 5
    • 0035161962 scopus 로고    scopus 로고
    • Toxicity of amiodarone and amiodarone analogues on isolated rat liver mitochondria
    • Spaniol M, Bracher R, Ha HR, Follath F, Krahenbuhl S. Toxicity of amiodarone and amiodarone analogues on isolated rat liver mitochondria. J Hepatol 2001;35:628-636.
    • (2001) J Hepatol , vol.35 , pp. 628-636
    • Spaniol, M.1    Bracher, R.2    Ha, H.R.3    Follath, F.4    Krahenbuhl, S.5
  • 6
    • 0025599388 scopus 로고
    • Dual effect of amiodarone on mitochondrial respiration. Initial protonophoric uncoupling effect followed by inhibition of the respiratory chain at the levels of complex I and complex II
    • Fromenty B, Fisch C, Berson A, Letteron P, Larrey D, Pessayre D. Dual effect of amiodarone on mitochondrial respiration. Initial protonophoric uncoupling effect followed by inhibition of the respiratory chain at the levels of complex I and complex II. J Pharmacol Exp Ther 1990;255:1377-1384.
    • (1990) J Pharmacol Exp Ther , vol.255 , pp. 1377-1384
    • Fromenty, B.1    Fisch, C.2    Berson, A.3    Letteron, P.4    Larrey, D.5    Pessayre, D.6
  • 7
    • 0018815489 scopus 로고
    • The action of benzbromarone in relation to age, sex and accompanying diseases
    • Ferber H, Bader U, Matzkies F. The action of benzbromarone in relation to age, sex and accompanying diseases. Adv Exp Med Biol 1980;122A:287-294.
    • (1980) Adv Exp Med Biol , vol.122 A , pp. 287-294
    • Ferber, H.1    Bader, U.2    Matzkies, F.3
  • 8
    • 0028966909 scopus 로고
    • Severe hepatotoxicity related to benzarone: A report of three cases with two fatalities
    • Hautekeete ML, Henrion J, Naegels S, DeNeve A, Adler M, Deprez C, et al. Severe hepatotoxicity related to benzarone: a report of three cases with two fatalities. Liver 1995;15:25-29.
    • (1995) Liver , vol.15 , pp. 25-29
    • Hautekeete, M.L.1    Henrion, J.2    Naegels, S.3    DeNeve, A.4    Adler, M.5    Deprez, C.6
  • 11
    • 0015924936 scopus 로고
    • Inhibition of enzymes of the internal mitochondrial membrane by benzbromarone
    • Kramer R, Muller MM. Inhibition of enzymes of the internal mitochondrial membrane by benzbromarone. Experientia 1973;29:391-392.
    • (1973) Experientia , vol.29 , pp. 391-392
    • Kramer, R.1    Muller, M.M.2
  • 12
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • Newmeyer DD, Ferguson-Miller S. Mitochondria: releasing power for life and unleashing the machineries of death. Cell 2003;112:481-490.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 13
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 1998;281:1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 14
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G, Reed JC. Mitochondrial control of cell death. Nat Med 2000;6:513-519.
    • (2000) Nat Med , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 15
    • 0018399518 scopus 로고
    • Riboflavin and rat hepatic cell structure and function. Mitochondrial oxidative metabolism in deficiency states
    • Hoppel C, DiMarco JP, Tandler B. Riboflavin and rat hepatic cell structure and function. Mitochondrial oxidative metabolism in deficiency states. J Biol Chem 1979;254:4164-4170.
    • (1979) J Biol Chem , vol.254 , pp. 4164-4170
    • Hoppel, C.1    DiMarco, J.P.2    Tandler, B.3
  • 16
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall AG, Bardawill GJ, David M. Determination of serum proteins by means of the biuret reaction. J Biol Chem 1949;177:751-766.
    • (1949) J Biol Chem , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, G.J.2    David, M.3
  • 17
    • 0016375598 scopus 로고
    • High-yield preparation of morphologically intact isolated parenchymal cells from rat liver
    • Berry MN. High-yield preparation of morphologically intact isolated parenchymal cells from rat liver. Methods Enzymol 1974;32:625-632.
    • (1974) Methods Enzymol , vol.32 , pp. 625-632
    • Berry, M.N.1
  • 18
    • 0027161924 scopus 로고
    • A method of determining electrical potential gradient across mitochondrial membrane in perfused rat hearts
    • Wan B, Doumen C, Duszynski J, Salama G, LaNoue KF. A method of determining electrical potential gradient across mitochondrial membrane in perfused rat hearts. Am J Physiol 1993;265:H445-H452.
    • (1993) Am J Physiol , vol.265
    • Wan, B.1    Doumen, C.2    Duszynski, J.3    Salama, G.4    LaNoue, K.F.5
  • 19
    • 75549114406 scopus 로고
    • The oxidation of citrate, isocitrate and cis-aconitate by isolated mitochondria
    • Chappell JB. The oxidation of citrate, isocitrate and cis-aconitate by isolated mitochondria. Biochem J 1964;90:225-237.
    • (1964) Biochem J , vol.90 , pp. 225-237
    • Chappell, J.B.1
  • 20
    • 0025836574 scopus 로고
    • Decreased activities of ubiquinol:ferricytochrome c oxidoreductase (complex III) and ferrocytochrome c:oxygen oxidoreductase (complex IV) in liver mitochondria from rats with hydroxycobalamin[c-lactam]-induced methylmalonic aciduria
    • Krahenbuhl S, Chang M, Brass EP, Hoppel CL. Decreased activities of ubiquinol:ferricytochrome c oxidoreductase (complex III) and ferrocytochrome c:oxygen oxidoreductase (complex IV) in liver mitochondria from rats with hydroxycobalamin[c-lactam]-induced methylmalonic aciduria. J Biol Chem 1991;266:20998-21003.
    • (1991) J Biol Chem , vol.266 , pp. 20998-21003
    • Krahenbuhl, S.1    Chang, M.2    Brass, E.P.3    Hoppel, C.L.4
  • 21
    • 77957003282 scopus 로고
    • Mitochondrial respiratory control and polarographic measurement of ADP:O ratios
    • Estabrook R. Mitochondrial respiratory control and polarographic measurement of ADP:O ratios. Methods Enzymol 1967;10:41-47.
    • (1967) Methods Enzymol , vol.10 , pp. 41-47
    • Estabrook, R.1
  • 23
    • 0015694248 scopus 로고
    • Localization of the enzymes of ketogenesis in rat liver mitochondria
    • Chapman MJ, Miller LR, Ontko JA. Localization of the enzymes of ketogenesis in rat liver mitochondria. J Cell Biol 1973;58:284-306.
    • (1973) J Cell Biol , vol.58 , pp. 284-306
    • Chapman, M.J.1    Miller, L.R.2    Ontko, J.A.3
  • 24
    • 0015085268 scopus 로고
    • An enzymatic fluorimetric micromethod for the determination of acetoacetate, hydroxybutyrate, pyruvate and lactate
    • Olsen C. An enzymatic fluorimetric micromethod for the determination of acetoacetate, hydroxybutyrate, pyruvate and lactate. Clin Chim Acta 1971;33:293-300.
    • (1971) Clin Chim Acta , vol.33 , pp. 293-300
    • Olsen, C.1
  • 25
    • 0037098941 scopus 로고    scopus 로고
    • A convenient one-step extraction of cellular ATP using boiling water for the luciferin-luciferase assay of ATP
    • Yang NC, Ho WM, Chen YH, Hu ML. A convenient one-step extraction of cellular ATP using boiling water for the luciferin-luciferase assay of ATP. Anal Biochem 2002;306:323-327.
    • (2002) Anal Biochem , vol.306 , pp. 323-327
    • Yang, N.C.1    Ho, W.M.2    Chen, Y.H.3    Hu, M.L.4
  • 26
    • 0029793298 scopus 로고    scopus 로고
    • Flux control exerted by mitochondrial outer membrane carnitine palmitoyltransferase over beta-oxidation, ketogenesis and tricarboxylic acid cycle activity in hepatocytes isolated from rats in different metabolic states
    • Drynan L, Quant PA, Zammit VA. Flux control exerted by mitochondrial outer membrane carnitine palmitoyltransferase over beta-oxidation, ketogenesis and tricarboxylic acid cycle activity in hepatocytes isolated from rats in different metabolic states. Biochem J 1996;317:791-795.
    • (1996) Biochem J , vol.317 , pp. 791-795
    • Drynan, L.1    Quant, P.A.2    Zammit, V.A.3
  • 27
    • 0030961969 scopus 로고    scopus 로고
    • The flux control coefficient of carnitine palmitoyltransferase I on palmitate beta-oxidation in rat hepatocyte cultures
    • Spurway TD, Sherratt HA, Pogson CI, Agius L. The flux control coefficient of carnitine palmitoyltransferase I on palmitate beta-oxidation in rat hepatocyte cultures. Biochem J 1997;323:119-122.
    • (1997) Biochem J , vol.323 , pp. 119-122
    • Spurway, T.D.1    Sherratt, H.A.2    Pogson, C.I.3    Agius, L.4
  • 28
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • Boveris A, Chance B. The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem J 1973;134:707-716.
    • (1973) Biochem J , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 29
    • 0036361291 scopus 로고    scopus 로고
    • Animal models for mitochondrial disease
    • Wallace DC. Animal models for mitochondrial disease. Methods Mol Biol 2002;197:3-54.
    • (2002) Methods Mol Biol , vol.197 , pp. 3-54
    • Wallace, D.C.1
  • 30
    • 0032526940 scopus 로고    scopus 로고
    • The regulation of reactive oxygen species production during programmed cell death
    • Tan S, Sagara Y, Liu Y, Maher P, Schubert D. The regulation of reactive oxygen species production during programmed cell death. J Cell Biol 1998;141:1423-1432.
    • (1998) J Cell Biol , vol.141 , pp. 1423-1432
    • Tan, S.1    Sagara, Y.2    Liu, Y.3    Maher, P.4    Schubert, D.5
  • 31
    • 0036138662 scopus 로고    scopus 로고
    • Endogenous and endobiotic induced reactive oxygen species formation by isolated hepatocytes
    • Siraki AG, Pourahmad J, Chan TS, Khan S, O'Brien PJ. Endogenous and endobiotic induced reactive oxygen species formation by isolated hepatocytes. Free Radic Biol Med 2002;32:2-10.
    • (2002) Free Radic Biol Med , vol.32 , pp. 2-10
    • Siraki, A.G.1    Pourahmad, J.2    Chan, T.S.3    Khan, S.4    O'Brien, P.J.5
  • 32
    • 0030033521 scopus 로고    scopus 로고
    • The beneficial effects of dietary restriction: Reduced oxidative damage and enhanced apoptosis
    • Wachsman JT. The beneficial effects of dietary restriction: reduced oxidative damage and enhanced apoptosis. Mutat Res 1996;350:25-34.
    • (1996) Mutat Res , vol.350 , pp. 25-34
    • Wachsman, J.T.1
  • 33
    • 0028221169 scopus 로고
    • Down-regulation of copper/zinc superoxide dismutase causes apoptotic death in PC12 neuronal cells
    • Troy CM, Shelanski ML. Down-regulation of copper/zinc superoxide dismutase causes apoptotic death in PC12 neuronal cells. Proc Natl Acad Sci U S A 1994;91:6384-6387.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 6384-6387
    • Troy, C.M.1    Shelanski, M.L.2
  • 34
    • 0031017999 scopus 로고    scopus 로고
    • Ex vivo induction of apoptosis in lymphocytes is mediated by oxidative stress: Role for lymphocyte loss in HIV infection
    • Dobmeyer TS, Findhammer S, Dobmeyer JM, Klein SA, Raffel B, Hoelzer D, et al. Ex vivo induction of apoptosis in lymphocytes is mediated by oxidative stress: role for lymphocyte loss in HIV infection. Free Radic Biol Med 1997;22:775-785.
    • (1997) Free Radic Biol Med , vol.22 , pp. 775-785
    • Dobmeyer, T.S.1    Findhammer, S.2    Dobmeyer, J.M.3    Klein, S.A.4    Raffel, B.5    Hoelzer, D.6
  • 35
    • 0032535016 scopus 로고    scopus 로고
    • Involvement of caspases in neutrophil apoptosis: Regulation by reactive oxygen species
    • Fadeel B, Ahlin A, Henter JI, Orrenius S, Hampton MB. Involvement of caspases in neutrophil apoptosis: regulation by reactive oxygen species. Blood 1998;92:4808-4818.
    • (1998) Blood , vol.92 , pp. 4808-4818
    • Fadeel, B.1    Ahlin, A.2    Henter, J.I.3    Orrenius, S.4    Hampton, M.B.5
  • 36
    • 0029162485 scopus 로고
    • The role of oxidative stress in HIV disease
    • Pace GW, Leaf CD. The role of oxidative stress in HIV disease. Free Radic Biol Med 1995;19:523-528.
    • (1995) Free Radic Biol Med , vol.19 , pp. 523-528
    • Pace, G.W.1    Leaf, C.D.2
  • 38
    • 0035083741 scopus 로고    scopus 로고
    • Monitoring of ascorbate at a constant rate in cell culture: Effect on cell growth
    • Chepda T, Cadau M, Girin P, Frey J, Chamson A. Monitoring of ascorbate at a constant rate in cell culture: effect on cell growth. In Vitro Cell Dev Biol Anim 2001;37:26-30.
    • (2001) In Vitro Cell Dev Biol Anim , vol.37 , pp. 26-30
    • Chepda, T.1    Cadau, M.2    Girin, P.3    Frey, J.4    Chamson, A.5
  • 39
    • 0037458090 scopus 로고    scopus 로고
    • Apoptosis: Mitochondrial membrane permeabilization-the (w)hole story?
    • Zamzami N, Kroemer G. Apoptosis: mitochondrial membrane permeabilization-the (w)hole story? Curr Biol 2003;13:R71-R73.
    • (2003) Curr Biol , vol.13
    • Zamzami, N.1    Kroemer, G.2
  • 40
    • 0032437405 scopus 로고    scopus 로고
    • Intracellular ATP a switch in the decision between apoptosis and necrosis
    • Nicotera P, Leist M, Ferrando-May E. Intracellular ATP, a switch in the decision between apoptosis and necrosis. Toxicol Lett 1998;102-103:139-142.
    • (1998) Toxicol Lett , vol.102-103 , pp. 139-142
    • Nicotera, P.1    Leist, M.2    Ferrando-May, E.3
  • 42
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport chain
    • Liu Y, Fiskum G, Schubert D. Generation of reactive oxygen species by the mitochondrial electron transport chain. J Neurochem 2002;80:780-787.
    • (2002) J Neurochem , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 43
    • 0036718504 scopus 로고    scopus 로고
    • Reactive oxygen species production by the mitochondrial respiratory chain in isolated rat hepatocytes and liver mitochondria: Studies using myxothiazol
    • Young TA, Cunningham CC, Bailey SM. Reactive oxygen species production by the mitochondrial respiratory chain in isolated rat hepatocytes and liver mitochondria: studies using myxothiazol. Arch Biochem Biophys 2002;405:65-72.
    • (2002) Arch Biochem Biophys , vol.405 , pp. 65-72
    • Young, T.A.1    Cunningham, C.C.2    Bailey, S.M.3
  • 44
    • 0034668791 scopus 로고    scopus 로고
    • Mitochondrial intermembrane junctional complexes and their role in cell death
    • Crompton M. Mitochondrial intermembrane junctional complexes and their role in cell death. J Physiol 2000;529:11-21.
    • (2000) J Physiol , vol.529 , pp. 11-21
    • Crompton, M.1
  • 45
    • 0030915587 scopus 로고    scopus 로고
    • Intracellular ATP levels determine cell death fate by apoptosis or necrosis
    • Eguchi Y, Shimizu S, Tsujimoto Y. Intracellular ATP levels determine cell death fate by apoptosis or necrosis. Cancer Res 1997;57:1835-1840.
    • (1997) Cancer Res , vol.57 , pp. 1835-1840
    • Eguchi, Y.1    Shimizu, S.2    Tsujimoto, Y.3
  • 46
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis
    • Leist M, Single B, Castoldi AF, Kuhnle S, Nicotera P. Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis. J Exp Med 1997;185:1481-1486.
    • (1997) J Exp Med , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3    Kuhnle, S.4    Nicotera, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.