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Volumn 15, Issue 1-2, 1998, Pages 53-76

Taurine: Protective properties against ethanol-induced hepatic steatosis and lipid peroxidation during chronic ethanol consumption in rats

Author keywords

Amino acids; CYP2E1; Ethanol; Hepatic steatosis; Homocysteine; Lipid peroxidation; Methionine synthase; Protection; Taurine

Indexed keywords

ALCOHOL; ALKALINE PHOSPHATASE; BILE ACID; CYTOCHROME P450; HOMOCYSTEINE; MICROSOME ENZYME; TAURINE;

EID: 0031709570     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF01345280     Document Type: Article
Times cited : (79)

References (54)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0029839564 scopus 로고    scopus 로고
    • Bile acids produce a generalized reduction of the catalytic activity of cytochromes P-450 and other hepatic microsomal enzymes in vitro: Relevance to drug metabolism in experimental cholestasis
    • Chen J, Farrell GC (1996) Bile acids produce a generalized reduction of the catalytic activity of cytochromes P-450 and other hepatic microsomal enzymes in vitro: relevance to drug metabolism in experimental cholestasis. J Gastroenterol Hepatol 11: 870-877
    • (1996) J Gastroenterol Hepatol , vol.11 , pp. 870-877
    • Chen, J.1    Farrell, G.C.2
  • 5
    • 0029121767 scopus 로고
    • Downregulation of male-specific cytochrome P-450s 2C11 and 3A2 in bile duct-ligated male rats: Importance to reduced hepatic content of cytochrome P-450 in cholestasis
    • Chen J, Murray M, Liddle C, Jiang XM, Farrell GC (1995) Downregulation of male-specific cytochrome P-450s 2C11 and 3A2 in bile duct-ligated male rats: importance to reduced hepatic content of cytochrome P-450 in cholestasis. Hepatoloey 22: 580-587
    • (1995) Hepatoloey , vol.22 , pp. 580-587
    • Chen, J.1    Murray, M.2    Liddle, C.3    Jiang, X.M.4    Farrell, G.C.5
  • 6
    • 0023632798 scopus 로고
    • High performance liquid chromatography of hepatic thiols with electrochemical detection
    • Jakoby WB, Griffith OW (eds) Academic Press, New York
    • De Master EG, Redfern B (1987) High performance liquid chromatography of hepatic thiols with electrochemical detection. In: Jakoby WB, Griffith OW (eds) Methods of enzymology, vol 193. Academic Press, New York, pp 110
    • (1987) Methods of Enzymology , vol.193 , pp. 110
    • De Master, E.G.1    Redfern, B.2
  • 7
    • 0024546914 scopus 로고
    • Rat liver microsomal NADPH-supported oxidase activity and lipid peroxidation dependent on ethanol-inducible cytochrome P-450 (P-4502E1)
    • Ekstrom G, Ingelman-Sundberg M (1989) Rat liver microsomal NADPH-supported oxidase activity and lipid peroxidation dependent on ethanol-inducible cytochrome P-450 (P-4502E1). Biochem Pharm 38: 1313-1319
    • (1989) Biochem Pharm , vol.38 , pp. 1313-1319
    • Ekstrom, G.1    Ingelman-Sundberg, M.2
  • 8
    • 3042934967 scopus 로고
    • Tissue sulphydryl groups
    • Ellman GL (1959) Tissue sulphydryl groups. Arch Biochem Biophys 82: 70-77
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 9
    • 0024354889 scopus 로고
    • Effects of chronic ethanol consumption on carcinogen activating and detoxifying systems in rat upper alimentary tract tissue
    • Farinati F, Lieber CS, Garro AJ (1989) Effects of chronic ethanol consumption on carcinogen activating and detoxifying systems in rat upper alimentary tract tissue. Alcohol Clin Exp Res 13: 357-360
    • (1989) Alcohol Clin Exp Res , vol.13 , pp. 357-360
    • Farinati, F.1    Lieber, C.S.2    Garro, A.J.3
  • 11
    • 0028926633 scopus 로고
    • Measurement of homocysteine in the prediction of arteriosclerosis
    • Fortin L-J, Genest J (1995) Measurement of homocysteine in the prediction of arteriosclerosis. Clin Biochem 28: 155-162
    • (1995) Clin Biochem , vol.28 , pp. 155-162
    • Fortin, L.-J.1    Genest, J.2
  • 13
    • 0019167355 scopus 로고
    • Determination of glutathione and glutathione disulphide using glutathione reductase and 2-vinylpyridine
    • Griffith OW (1980) Determination of glutathione and glutathione disulphide using glutathione reductase and 2-vinylpyridine. Anal Biochem 106: 207-212
    • (1980) Anal Biochem , vol.106 , pp. 207-212
    • Griffith, O.W.1
  • 16
    • 0026595620 scopus 로고
    • Physiological actions of taurine
    • Huxtable RJ (1992) Physiological actions of taurine. Physiol Rev 72: 101-163
    • (1992) Physiol Rev , vol.72 , pp. 101-163
    • Huxtable, R.J.1
  • 17
    • 0028257971 scopus 로고
    • Effect of acute and repeated exposure to low doses of hydrazine on hepatic microsomal enzymes and biochemical parameters in vivo
    • Jenner AM, Timbrell JA (1994) Effect of acute and repeated exposure to low doses of hydrazine on hepatic microsomal enzymes and biochemical parameters in vivo. Arch Toxicol 68: 240-245
    • (1994) Arch Toxicol , vol.68 , pp. 240-245
    • Jenner, A.M.1    Timbrell, J.A.2
  • 18
    • 0024453029 scopus 로고
    • Lipid peroxidation and antioxidant defense systems in rat liver after chronic ethanol feeding
    • Kawase T, Kato S, Lieber CS (1989) Lipid peroxidation and antioxidant defense systems in rat liver after chronic ethanol feeding. Hepatology 10: 815-821
    • (1989) Hepatology , vol.10 , pp. 815-821
    • Kawase, T.1    Kato, S.2    Lieber, C.S.3
  • 19
    • 0023078621 scopus 로고
    • Selective reduction of hepatic cytochrome P-450 content in patients with intrahepatic cholestasis. A mechanism for impairment of microsomal drug oxidation
    • Kawata S, Imai Y, Inada M, Tamura S, Miyoshi S, Nishikawa M, Minami Y, Tarui S (1987) Selective reduction of hepatic cytochrome P-450 content in patients with intrahepatic cholestasis. A mechanism for impairment of microsomal drug oxidation. Gastroenterol 92: 299-303
    • (1987) Gastroenterol , vol.92 , pp. 299-303
    • Kawata, S.1    Imai, Y.2    Inada, M.3    Tamura, S.4    Miyoshi, S.5    Nishikawa, M.6    Minami, Y.7    Tarui, S.8
  • 20
    • 0031949104 scopus 로고    scopus 로고
    • The effect of ethanol and its metabolites upon methionine synthase activity in vitro
    • Kenyon SH, Nicolaou A, Gibbons WA (1998) The effect of ethanol and its metabolites upon methionine synthase activity in vitro. Alcohol 15: 305-309
    • (1998) Alcohol , vol.15 , pp. 305-309
    • Kenyon, S.H.1    Nicolaou, A.2    Gibbons, W.A.3
  • 21
    • 0003122802 scopus 로고
    • Investigations and characterization of microsomal fractions for studies of xenohiotic metabolism
    • Snell K, Mullock B (eds) IRL Press, Oxford
    • Lake BG (1987) Investigations and characterization of microsomal fractions for studies of xenohiotic metabolism. In: Snell K, Mullock B (eds) Biochemical toxicology: a practical approach. IRL Press, Oxford, pp 183-215
    • (1987) Biochemical Toxicology: A Practical Approach , pp. 183-215
    • Lake, B.G.1
  • 22
    • 0027265259 scopus 로고
    • Biochemical factors in alcoholic liver disease
    • Lieber CS (1993) Biochemical factors in alcoholic liver disease. Semin Liver Dis 13: 136-153
    • (1993) Semin Liver Dis , vol.13 , pp. 136-153
    • Lieber, C.S.1
  • 23
    • 0030935567 scopus 로고    scopus 로고
    • Cytochrome P-4502E1: Its physiological and pathological role
    • Lieber CS (1997a) Cytochrome P-4502E1: its physiological and pathological role. Physiol Rev 77: 517-544
    • (1997) Physiol Rev , vol.77 , pp. 517-544
    • Lieber, C.S.1
  • 24
    • 1842409036 scopus 로고    scopus 로고
    • Role of oxidative stress and antioxidant therapy in alcoholic and nonalcoholic liver diseases
    • Lieber CS (1997b) Role of oxidative stress and antioxidant therapy in alcoholic and nonalcoholic liver diseases. Adv Pharmacol 38: 601-628
    • (1997) Adv Pharmacol , vol.38 , pp. 601-628
    • Lieber, C.S.1
  • 25
    • 0024409956 scopus 로고
    • Liquid diet technique of ethanol administration: 1989 update
    • Lieber CS, DeCarli LM (1989) Liquid diet technique of ethanol administration: 1989 update. Alcohol Alcohol 24: 197-211
    • (1989) Alcohol Alcohol , vol.24 , pp. 197-211
    • Lieber, C.S.1    DeCarli, L.M.2
  • 30
    • 0001832910 scopus 로고
    • An enzymatic assay for acetaldehyde in grape juice and wine
    • McCloskey LP, Mahaney P (1981) An enzymatic assay for acetaldehyde in grape juice and wine. Am J Enof Vitic 32: 159-162
    • (1981) Am J Enof Vitic , vol.32 , pp. 159-162
    • McCloskey, L.P.1    Mahaney, P.2
  • 32
    • 0019995325 scopus 로고
    • Role of alcohol dehydrogenase activity and of acetaldehyde in ethanol-induced ethane and pentane production by isolated perfused rat liver
    • Müller A, Sies H (1982) Role of alcohol dehydrogenase activity and of acetaldehyde in ethanol-induced ethane and pentane production by isolated perfused rat liver. Biochem J 206: 153-156
    • (1982) Biochem J , vol.206 , pp. 153-156
    • Müller, A.1    Sies, H.2
  • 33
    • 0020671118 scopus 로고
    • Therapeutic and prophylactic effects of taurine administration on experimental liver injury
    • Kuriyama K, Huxtable RJ, Iwata H (eds) Alan R Liss Inc., New York
    • Nakashima T, Takino T, Kuriyama K (1983) Therapeutic and prophylactic effects of taurine administration on experimental liver injury. In: Kuriyama K, Huxtable RJ, Iwata H (eds) Sulphur amino acids: biochemical and clinical aspects. Alan R Liss Inc., New York, pp 449-459
    • (1983) Sulphur Amino Acids: Biochemical and Clinical Aspects , pp. 449-459
    • Nakashima, T.1    Takino, T.2    Kuriyama, K.3
  • 34
    • 0030896141 scopus 로고    scopus 로고
    • The inactivation of methionine synthase in isolated rat hepatocytes by sodium nitroprusside
    • Nicolaou A, Waterfield CJ, Kenyon SH, Gibbons WA (1997) The inactivation of methionine synthase in isolated rat hepatocytes by sodium nitroprusside. Eur J Biochem 244: 876-882
    • (1997) Eur J Biochem , vol.244 , pp. 876-882
    • Nicolaou, A.1    Waterfield, C.J.2    Kenyon, S.H.3    Gibbons, W.A.4
  • 35
    • 78651165715 scopus 로고
    • The carbon monoxide binding pigment of liver microsomes. Evidence of its haemoprotein value
    • Omura T, Sato R (1964) The carbon monoxide binding pigment of liver microsomes. Evidence of its haemoprotein value. J Biol Chem 239: 2370-2378
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 36
    • 0028988584 scopus 로고
    • Antibodies made against a formaldehyde-protein adduct cross react with an acetaldehyde-protein adduct. Implications for the origin of antibodies in human serum which recognize acetaldehyde-protein adducts
    • Pietrzak ER, Shanley BC, Kroon PA (1995) Antibodies made against a formaldehyde-protein adduct cross react with an acetaldehyde-protein adduct. Implications for the origin of antibodies in human serum which recognize acetaldehyde-protein adducts. Alcohol Alcohol 30: 373-378
    • (1995) Alcohol Alcohol , vol.30 , pp. 373-378
    • Pietrzak, E.R.1    Shanley, B.C.2    Kroon, P.A.3
  • 37
    • 0017831699 scopus 로고
    • Fleischer S, Packer L (eds) Academic Press, New York
    • Prough RA, Burke MD, Mayer RT (1978) In: Fleischer S, Packer L (eds) Methods in enzymology, vol 52. Academic Press, New York, pp 372-377
    • (1978) Methods in Enzymology , vol.52 , pp. 372-377
    • Prough, R.A.1    Burke, M.D.2    Mayer, R.T.3
  • 38
    • 0023488842 scopus 로고
    • Reactive free radical generation in vivo in heart and liver of ethanol-fed rats: Correlation with radical formation in vitro
    • Reinke LA, Lai EK, DuBose CM, McCay PB (1987) Reactive free radical generation in vivo in heart and liver of ethanol-fed rats: correlation with radical formation in vitro. Proc Natl Acad Sci USA 84: 9223-9227
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 9223-9227
    • Reinke, L.A.1    Lai, E.K.2    DuBose, C.M.3    McCay, P.B.4
  • 39
    • 0000020508 scopus 로고
    • Comparison of spectrophotometric and spectrophotofluorometric methods for the determination of malonaldehyde
    • Sawicki E, Stanley TW, Johnson H (1963) Comparison of spectrophotometric and spectrophotofluorometric methods for the determination of malonaldehyde. Anal Chem 35: 199-205
    • (1963) Anal Chem , vol.35 , pp. 199-205
    • Sawicki, E.1    Stanley, T.W.2    Johnson, H.3
  • 41
    • 0030880509 scopus 로고    scopus 로고
    • Modulation of taurine levels in the rat liver alters methylene dianiline hepatotoxicity
    • Seabra V, Timbrell JA (1997) Modulation of taurine levels in the rat liver alters methylene dianiline hepatotoxicity. Toxicology 122: 193-204
    • (1997) Toxicology , vol.122 , pp. 193-204
    • Seabra, V.1    Timbrell, J.A.2
  • 42
    • 0019511768 scopus 로고
    • Ethanol-induced lipid peroxidation: Potentiation by long-term alcohol feeding and attenuation by methionine
    • Shaw S, Jayatilleke E, Ross WA (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
  • 43
    • 0024159641 scopus 로고
    • Lipid peroxidation as a mechanism of alcoholic liver injury: Role of iron mobilization and microsomal induction
    • Shaw S, Jayatilleke E, Lieber CS (1988) Lipid peroxidation as a mechanism of alcoholic liver injury: role of iron mobilization and microsomal induction. Alcohol 5: 135-140
    • (1988) Alcohol , vol.5 , pp. 135-140
    • Shaw, S.1    Jayatilleke, E.2    Lieber, C.S.3
  • 44
    • 0028921717 scopus 로고
    • The in vivo and in vitro protective properties of taurine
    • Timbrell JA, Seabra V, Waterfield CJ (1995) The in vivo and in vitro protective properties of taurine. Gen Pharmac 26: 453-462
    • (1995) Gen Pharmac , vol.26 , pp. 453-462
    • Timbrell, J.A.1    Seabra, V.2    Waterfield, C.J.3
  • 45
    • 0027682832 scopus 로고
    • The effect of ethanol on one-carbon metabolism: Increased methionine catabolism and lipotrope methyl-group wastage
    • Trimble KC, Molloy AM, Scott JM, Weir DG (1993) The effect of ethanol on one-carbon metabolism: increased methionine catabolism and lipotrope methyl-group wastage. Hepatology 18: 984-989
    • (1993) Hepatology , vol.18 , pp. 984-989
    • Trimble, K.C.1    Molloy, A.M.2    Scott, J.M.3    Weir, D.G.4
  • 46
    • 0030890528 scopus 로고    scopus 로고
    • Acute renal failure after binge drinking of alcohol and nonsteroidal anti-inflammatory drug ingestion
    • Tsuboi N, Yoshida H, Shibamura K, Hikita M, Tomonari H, Kuriyama S, Sakai O (1997) Acute renal failure after binge drinking of alcohol and nonsteroidal anti-inflammatory drug ingestion. Intern Med 36: 102-106
    • (1997) Intern Med , vol.36 , pp. 102-106
    • Tsuboi, N.1    Yoshida, H.2    Shibamura, K.3    Hikita, M.4    Tomonari, H.5    Kuriyama, S.6    Sakai, O.7
  • 47
    • 0021554745 scopus 로고
    • Acute and chronic effects of ethanol on biliary secretion of bilirubin and bile acids
    • Vendemiale G, Lieber CS (1984) Acute and chronic effects of ethanol on biliary secretion of bilirubin and bile acids. Subst Alcohol Actions Misuse 5: 307-317
    • (1984) Subst Alcohol Actions Misuse , vol.5 , pp. 307-317
    • Vendemiale, G.1    Lieber, C.S.2
  • 48
    • 0018148486 scopus 로고
    • The biochemical basis for the conjugation of bile acids with either glycine or taurine
    • Vessey DA (1978) The biochemical basis for the conjugation of bile acids with either glycine or taurine. Biochem J 174: 621-626
    • (1978) Biochem J , vol.174 , pp. 621-626
    • Vessey, D.A.1
  • 49
    • 0022405097 scopus 로고
    • Lowering of liver acetaldehyde but not ethanol concentrations by pretreatment with taurine in ethanol-loaded rats
    • Watanabe A, Hobara N, Nagashima H (1985) Lowering of liver acetaldehyde but not ethanol concentrations by pretreatment with taurine in ethanol-loaded rats. Experientia 41: 1421-1422
    • (1985) Experientia , vol.41 , pp. 1421-1422
    • Watanabe, A.1    Hobara, N.2    Nagashima, H.3
  • 50
    • 0028217493 scopus 로고
    • Determination of taurine in biological samples and isolated hepatocytes by high performance liquid chromatography with fluorimetric detection
    • Waterfield CJ (1994) Determination of taurine in biological samples and isolated hepatocytes by high performance liquid chromatography with fluorimetric detection. J Chromatography 657: 37-45
    • (1994) J Chromatography , vol.657 , pp. 37-45
    • Waterfield, C.J.1
  • 51
    • 0027535740 scopus 로고
    • Reduction of liver taurine in rats by β-alanine treatment increases carbon tetrachloride toxicity
    • Waterfield CJ, Turton JA, Scales MDC, Timbrell JA (1993a) Reduction of liver taurine in rats by β-alanine treatment increases carbon tetrachloride toxicity. Toxicology 77: 7-20
    • (1993) Toxicology , vol.77 , pp. 7-20
    • Waterfield, C.J.1    Turton, J.A.2    Scales, M.D.C.3    Timbrell, J.A.4
  • 52
    • 0027161423 scopus 로고
    • Investigations into the effects of various hepatotoxin compounds on urinary and liver taurine levels in rats
    • Waterfield CJ, Turton JA, Scales MDC, Timbrell JA (1993b) Investigations into the effects of various hepatotoxin compounds on urinary and liver taurine levels in rats. Arch Toxicol 67: 244-254
    • (1993) Arch Toxicol , vol.67 , pp. 244-254
    • Waterfield, C.J.1    Turton, J.A.2    Scales, M.D.C.3    Timbrell, J.A.4
  • 53
    • 0013563189 scopus 로고    scopus 로고
    • Does urinary taurine reflect changes in protein metabolism? A study with cycloheximide in rats
    • Waterfield CJ, Asker DA, Timbrell JA (1996) Does urinary taurine reflect changes in protein metabolism? A study with cycloheximide in rats. Biomarkers 1: 107-114
    • (1996) Biomarkers , vol.1 , pp. 107-114
    • Waterfield, C.J.1    Asker, D.A.2    Timbrell, J.A.3
  • 54
    • 0027529709 scopus 로고
    • Effect of taurine levels on liver lipid metabolism: An in vivo study in the rat
    • Yan CC, Bravo E, Cantafora A (1993) Effect of taurine levels on liver lipid metabolism: an in vivo study in the rat. Proc Soc Exp Biol Med 202: 88-96
    • (1993) Proc Soc Exp Biol Med , vol.202 , pp. 88-96
    • Yan, C.C.1    Bravo, E.2    Cantafora, A.3


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