메뉴 건너뛰기




Volumn 36, Issue 8, 1998, Pages 655-661

Effects of singly administered betaine on hepatotoxicity of chloroform in mice

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE AMINOTRANSFERASE; AMINOPYRINE N DEMETHYLASE; ASPARTATE AMINOTRANSFERASE; BETAINE; CHLOROFORM; CYTOCHROME P450 ISOENZYME; DRUG METABOLIZING ENZYME; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; IDITOL DEHYDROGENASE; OXYGENASE;

EID: 0031820524     PISSN: 02786915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0278-6915(98)00024-6     Document Type: Article
Times cited : (41)

References (36)
  • 1
    • 0024432862 scopus 로고
    • A role for the glutathione peroxidase/reductase enzyme system in the protection from paracetamol toxicity in isolated mouse hepatocytes
    • Adamson G. M., Harman A. W. A role for the glutathione peroxidase/reductase enzyme system in the protection from paracetamol toxicity in isolated mouse hepatocytes. Biochemical Pharmacology. 38:1989;3323-3330.
    • (1989) Biochemical Pharmacology , vol.38 , pp. 3323-3330
    • Adamson, G.M.1    Harman, A.W.2
  • 2
    • 0019478520 scopus 로고
    • Protective role of the glutathione redox cycle against adriamycin-mediated toxicity in isolated hepatocytes
    • Babson J. R., Abell N. S., Reed D. J. Protective role of the glutathione redox cycle against adriamycin-mediated toxicity in isolated hepatocytes. Biochemical Pharmacology. 30:1981;2299-2304.
    • (1981) Biochemical Pharmacology , vol.30 , pp. 2299-2304
    • Babson, J.R.1    Abell, N.S.2    Reed, D.J.3
  • 3
    • 0021256392 scopus 로고
    • Mechanism of chloroform nephrotoxicity: IV. phenobarbital potentiation of in vitro chloroform metabolism and toxicity in rabbit kidneys
    • Bailie M. B., Smith J. H., Newton J. F., Hook J. B. Mechanism of chloroform nephrotoxicity: IV. phenobarbital potentiation of in vitro chloroform metabolism and toxicity in rabbit kidneys. Toxicology and Applied Pharmacology. 74:1984;285-292.
    • (1984) Toxicology and Applied Pharmacology , vol.74 , pp. 285-292
    • Bailie, M.B.1    Smith, J.H.2    Newton, J.F.3    Hook, J.B.4
  • 4
    • 0030199376 scopus 로고    scopus 로고
    • Betaine, ethanol, and the liver: A review
    • Barak A. J., Bechenhauer H. C., Tuma D. J. Betaine, ethanol, and the liver: a review. Alcohol. 13:1996;395-398.
    • (1996) Alcohol , vol.13 , pp. 395-398
    • Barak, A.J.1    Bechenhauer, H.C.2    Tuma, D.J.3
  • 5
    • 0019165593 scopus 로고
    • Involvement of the cystathionine pathway in the biosynthesis of glutathione by isolated rat hepatocytes
    • Beatty P. W., Reed D. J. Involvement of the cystathionine pathway in the biosynthesis of glutathione by isolated rat hepatocytes. Archives of Biochemistry and Biophysics. 204:1980;80-87.
    • (1980) Archives of Biochemistry and Biophysics , vol.204 , pp. 80-87
    • Beatty, P.W.1    Reed, D.J.2
  • 6
    • 0024448789 scopus 로고
    • Induction of cytochrome P450IIE1 and P450IIB1 by secondary ketones and the role of P450IIE1 in chloroform metabolism
    • Brady J. F., Li D., Ishizaki H., Lee M., Ning S. M., Xiao F., Yang C. Y. Induction of cytochrome P450IIE1 and P450IIB1 by secondary ketones and the role of P450IIE1 in chloroform metabolism. Toxicology and Applied Pharmacology. 100:1989;342-349.
    • (1989) Toxicology and Applied Pharmacology , vol.100 , pp. 342-349
    • Brady, J.F.1    Li, D.2    Ishizaki, H.3    Lee, M.4    Ning, S.M.5    Xiao, F.6    Yang, C.Y.7
  • 8
    • 0015116983 scopus 로고
    • Methionine metabolism in mammals. Regulation of homocysteine methyltransferases in rat tissue
    • Finkelstein J. D., Kyle W. E., Harris B. J. Methionine metabolism in mammals. Regulation of homocysteine methyltransferases in rat tissue. Archives of Biochemistry and Biophysics. 146:1971;84-92.
    • (1971) Archives of Biochemistry and Biophysics , vol.146 , pp. 84-92
    • Finkelstein, J.D.1    Kyle, W.E.2    Harris, B.J.3
  • 10
    • 0000332535 scopus 로고
    • Sorbitol dehydrogenase
    • ed. H. U. Bergmeyer, Verlag Chemie, Weinheim
    • Gerlach U. (1983) Sorbitol dehydrogenase. In Methods of Enzymatic Analysis, ed. H. U. Bergmeyer, Vol. 3, pp. 112-117. Verlag Chemie, Weinheim.
    • (1983) In Methods of Enzymatic Analysis , vol.3 , pp. 112-117
    • Gerlach, U.1
  • 11
    • 0019167355 scopus 로고
    • Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine
    • Griffith O. W. Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Analytical Biochemistry. 106:1980;207-212.
    • (1980) Analytical Biochemistry , vol.106 , pp. 207-212
    • Griffith, O.W.1
  • 12
    • 0016275313 scopus 로고
    • Glutathione S-transferases: The first enzymatic step in mercapturic acid formation
    • Habig W. H., Pabst M. J., Jakoby W. B. Glutathione S-transferases: the first enzymatic step in mercapturic acid formation. Journal of Biological Chemistry. 249:1974;7130-7139.
    • (1974) Journal of Biological Chemistry , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 13
    • 0019280984 scopus 로고
    • Physiological significance of the glutathione S-transferases
    • Kaplowitz N. Physiological significance of the glutathione S-transferases. American Journal of Physiology. 239:1980;G439-G444.
    • (1980) American Journal of Physiology , vol.239
    • Kaplowitz, N.1
  • 14
    • 0022494453 scopus 로고
    • Hydroxylation of p-nitrophenol by rabbit ethanol-inducible cytochrome P-450 isozyme 3a
    • Koop D. R. Hydroxylation of p-nitrophenol by rabbit ethanol-inducible cytochrome P-450 isozyme 3a. Molecular Pharmacology. 29:1986;399-404.
    • (1986) Molecular Pharmacology , vol.29 , pp. 399-404
    • Koop, D.R.1
  • 15
    • 0021216714 scopus 로고
    • Hepatic glutathione homeostasis in the rat: Efflux accounts for glutathione turnover
    • Lauterburg B. H., Adams J. D., Mitchell J. R. Hepatic glutathione homeostasis in the rat: efflux accounts for glutathione turnover. Hepatology. 4:1984;586-590.
    • (1984) Hepatology , vol.4 , pp. 586-590
    • Lauterburg, B.H.1    Adams, J.D.2    Mitchell, J.R.3
  • 19
    • 77049138167 scopus 로고
    • The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
    • Nash T. The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochemical Journal. 55:1953;416-421.
    • (1953) Biochemical Journal , vol.55 , pp. 416-421
    • Nash, T.1
  • 20
    • 0021436098 scopus 로고
    • Betaine therapy for homocystinuria
    • Betaine therapy for homocystinuria. Nutrition Reviews. 42:1984;180-182.
    • (1984) Nutrition Reviews , vol.42 , pp. 180-182
  • 21
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes
    • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. Journal of Biological Chemistry. 239:1964;2370-2378.
    • (1964) Journal of Biological Chemistry , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 22
    • 73849173955 scopus 로고
    • Hepatic triphosphopyridine nucleotide-cytochrome c reductase: Isolation, characterization and kinetic studies
    • Phillips A. H., Langdon R. G. Hepatic triphosphopyridine nucleotide-cytochrome c reductase: isolation, characterization and kinetic studies. Journal of Biological Chemistry. 237:1962;2652-2660.
    • (1962) Journal of Biological Chemistry , vol.237 , pp. 2652-2660
    • Phillips, A.H.1    Langdon, R.G.2
  • 23
    • 0019740861 scopus 로고
    • Chemical depletion of glutathione in vivo
    • ed. W. B. Jakoby, Academic Press, New York
    • Plummer J. L., Smith B. R., Sies H. and Bend J. R. (1981) Chemical depletion of glutathione in vivo. In Methods in Enzymology, ed. W. B. Jakoby, Vol. 77, pp. 50-59. Academic Press, New York.
    • (1981) In Methods in Enzymology , vol.77 , pp. 50-59
    • Plummer, J.L.1    Smith, B.R.2    Sies, H.3    Bend, J.R.4
  • 24
  • 27
    • 0018266171 scopus 로고
    • Deuterium isotope effect in bioactivation and hepatotoxicity
    • Pohl L. R., Krishna G. Deuterium isotope effect in bioactivation and hepatotoxicity. Life Sciences. 23:1978;1067-1072.
    • (1978) Life Sciences , vol.23 , pp. 1067-1072
    • Pohl, L.R.1    Krishna, G.2
  • 30
    • 66349129125 scopus 로고
    • Colorimetric method for determination of serum glutamic oxaloacetic and glutamic pyruvic transaminases
    • Reitman S., Frankel S. A. Colorimetric method for determination of serum glutamic oxaloacetic and glutamic pyruvic transaminases. American Journal of Clinical Pathology. 28:1957;56-63.
    • (1957) American Journal of Clinical Pathology , vol.28 , pp. 56-63
    • Reitman, S.1    Frankel, S.A.2
  • 32
    • 0024199997 scopus 로고
    • Assay of glutathione reductase in crude tissue homogenates using 5,5′-dithiobis(2-nitrobenzoic acid)
    • Smith I. K., Vierheller T. L., Thorne C. A. Assay of glutathione reductase in crude tissue homogenates using 5,5′-dithiobis(2-nitrobenzoic acid). Analytical Biochemistry. 175:1988;408-413.
    • (1988) Analytical Biochemistry , vol.175 , pp. 408-413
    • Smith, I.K.1    Vierheller, T.L.2    Thorne, C.A.3
  • 35
    • 0000266418 scopus 로고
    • Partial replacement of dietary methionine by cystine for purposes of growth
    • Womack M., Rose W. C. Partial replacement of dietary methionine by cystine for purposes of growth. Journal of Biological Chemistry. 141:1941;375-379.
    • (1941) Journal of Biological Chemistry , vol.141 , pp. 375-379
    • Womack, M.1    Rose, W.C.2
  • 36
    • 0029961593 scopus 로고    scopus 로고
    • Identification of betaine as an osmolyte in rat liver macrophages (Kupffer cells)
    • Zhang F., Warskulat U., Wettstein M., Häussinger D. Identification of betaine as an osmolyte in rat liver macrophages (Kupffer cells). Gastroenterology. 110:1996;1543-1552.
    • (1996) Gastroenterology , vol.110 , pp. 1543-1552
    • Zhang, F.1    Warskulat, U.2    Wettstein, M.3    Häussinger, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.