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Volumn 21, Issue 2, 1997, Pages 267-274

Antipyrine and aminopyrine induce acetaldehyde accumulation from ethanol in isolated hepatocytes

Author keywords

Aldehyde Dehydrogenase; Aminopyrine; Antipyrine; Hepatocyte; Phenobarbital

Indexed keywords

4 METHYLPYRAZOLE; ACETALDEHYDE; ALDEHYDE DEHYDROGENASE; AMINOPHENAZONE; CIMETIDINE; PHENAZONE; PHENOBARBITAL;

EID: 0030900778     PISSN: 01456008     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1530-0277.1997.tb03760.x     Document Type: Article
Times cited : (3)

References (51)
  • 1
    • 0019963316 scopus 로고
    • Immunohistochemical localization of human liver alcohol dehydrogenase in liver tissue, cultured fibroblasts, and HeLa cells
    • Buehler R, Hess M, von Wartburg JP: Immunohistochemical localization of human liver alcohol dehydrogenase in liver tissue, cultured fibroblasts, and HeLa cells. Am J Pathol 108:89-99, 1982
    • (1982) Am J Pathol , vol.108 , pp. 89-99
    • Buehler, R.1    Hess, M.2    Von Wartburg, J.P.3
  • 2
    • 0015332379 scopus 로고
    • Intracellular localization of aldehyde dehydrogenase in rat liver
    • Marjanen L: Intracellular localization of aldehyde dehydrogenase in rat liver. Biochem J 127:633-639, 1972
    • (1972) Biochem J , vol.127 , pp. 633-639
    • Marjanen, L.1
  • 3
    • 0016723293 scopus 로고
    • Liver aldehyde and alcohol dehydrogenase activities in rat strains genetically selected for their ethanol preference
    • Koivula T, Koivusalo M, Lindros KO: Liver aldehyde and alcohol dehydrogenase activities in rat strains genetically selected for their ethanol preference. Biochem Pharmacol 24:1807-1811, 1975
    • (1975) Biochem Pharmacol , vol.24 , pp. 1807-1811
    • Koivula, T.1    Koivusalo, M.2    Lindros, K.O.3
  • 5
    • 0020583204 scopus 로고
    • Acetaldehyde and aldehyde dehydrogenases-central problems in the study of alcoholism
    • Lundquist F: Acetaldehyde and aldehyde dehydrogenases-central problems in the study of alcoholism. Eur J Clin Invest 13:183-184, 1983
    • (1983) Eur J Clin Invest , vol.13 , pp. 183-184
    • Lundquist, F.1
  • 6
    • 0017385404 scopus 로고
    • The rate of ethanol metabolism in isolated rat hepatocytes
    • Crow KE, Cornell NW, Veech RL: The rate of ethanol metabolism in isolated rat hepatocytes. Alcohol Clin Exp Res 1:43-50, 1977
    • (1977) Alcohol Clin Exp Res , vol.1 , pp. 43-50
    • Crow, K.E.1    Cornell, N.W.2    Veech, R.L.3
  • 7
    • 0021034969 scopus 로고
    • Elimination of artifactual acetaldehyde in the measurement of human blood acetaldehyde by the use of polyethylene glycol and sodium azide: Normal blood acetaldehyde levels in the dog and human after ethanol
    • DeMaster EG, Redfern B, Weir K, Pierpont GL, Crouse LJ: Elimination of artifactual acetaldehyde in the measurement of human blood acetaldehyde by the use of polyethylene glycol and sodium azide: normal blood acetaldehyde levels in the dog and human after ethanol. Alcohol Clin Exp Res 7:436-442, 1983
    • (1983) Alcohol Clin Exp Res , vol.7 , pp. 436-442
    • DeMaster, E.G.1    Redfern, B.2    Weir, K.3    Pierpont, G.L.4    Crouse, L.J.5
  • 9
    • 0020536806 scopus 로고
    • Determinants of blood acetaldehyde level during ethanol oxidation in chronic alcoholics
    • Nuutinen H, Lindros KO, Salaspuro M: Determinants of blood acetaldehyde level during ethanol oxidation in chronic alcoholics. Alcohol Clin Exp Res 7:163-168, 1983
    • (1983) Alcohol Clin Exp Res , vol.7 , pp. 163-168
    • Nuutinen, H.1    Lindros, K.O.2    Salaspuro, M.3
  • 10
    • 0024417771 scopus 로고
    • Comparative study on ethanol elimination and blood acetaldehyde between alcoholics and control subjects
    • Adachi J, Mizoi Y, Fukunaga T, Ogawa Y, Imamichi H: Comparative study on ethanol elimination and blood acetaldehyde between alcoholics and control subjects. Alcohol Clin Exp Res 13:601-604, 1989
    • (1989) Alcohol Clin Exp Res , vol.13 , pp. 601-604
    • Adachi, J.1    Mizoi, Y.2    Fukunaga, T.3    Ogawa, Y.4    Imamichi, H.5
  • 12
    • 0018881167 scopus 로고
    • Selectively reduced hepatic acetaldehyde dehydrogenase in alcoholics
    • Jenkins WJ, Peters TJ: Selectively reduced hepatic acetaldehyde dehydrogenase in alcoholics. Lancet 1:628-629, 1980
    • (1980) Lancet , vol.1 , pp. 628-629
    • Jenkins, W.J.1    Peters, T.J.2
  • 13
    • 0025826138 scopus 로고
    • The importance of alcohol dehydrogenase in regulation of ethanol metabolism in rat liver cells
    • Page RA, Kitson KE, Hardman MJ: The importance of alcohol dehydrogenase in regulation of ethanol metabolism in rat liver cells. Biochem J 278:659-665, 1991
    • (1991) Biochem J , vol.278 , pp. 659-665
    • Page, R.A.1    Kitson, K.E.2    Hardman, M.J.3
  • 14
    • 0016427486 scopus 로고
    • High blood acetaldehyde levels after ethanol administration. Difference between alcoholic and nonalcoholic subjects
    • Korsten MA, Matsuzaki S, Feinman L, Lieber CS: High blood acetaldehyde levels after ethanol administration. Difference between alcoholic and nonalcoholic subjects. N Engl J Mod 292:386-389, 1975
    • (1975) N Engl J Mod , vol.292 , pp. 386-389
    • Korsten, M.A.1    Matsuzaki, S.2    Feinman, L.3    Lieber, C.S.4
  • 15
    • 0020397426 scopus 로고
    • Effects of ethanol-derived acetaldehyde on the phosphorylation potential and on the intramitochondrial redox state in intact rat liver
    • Lindros KO, Stowell A: Effects of ethanol-derived acetaldehyde on the phosphorylation potential and on the intramitochondrial redox state in intact rat liver. Arch Biochem Biophys 218:429-437, 1982
    • (1982) Arch Biochem Biophys , vol.218 , pp. 429-437
    • Lindros, K.O.1    Stowell, A.2
  • 16
    • 0017354995 scopus 로고
    • The disulfiram-ethanol reaction: A review
    • Kitson TM: The disulfiram-ethanol reaction: A review. J Stud Alcohol 38:96-113, 1977
    • (1977) J Stud Alcohol , vol.38 , pp. 96-113
    • Kitson, T.M.1
  • 18
    • 0022552866 scopus 로고
    • Role of propiolaldehyde and other metabolites in the pargyline inhibition of rat liver aldehyde dehydrogenase
    • DeMaster EG, Shirota FN, Nagasawa HT: Role of propiolaldehyde and other metabolites in the pargyline inhibition of rat liver aldehyde dehydrogenase. Biochem Pharmacol 35:1481-1489, 1986
    • (1986) Biochem Pharmacol , vol.35 , pp. 1481-1489
    • DeMaster, E.G.1    Shirota, F.N.2    Nagasawa, H.T.3
  • 19
    • 0022255780 scopus 로고
    • Enzymatic requirement for cyanamide inactivation of rat liver aldehyde dehydrogenase
    • Svanas GW, Weiner H: Enzymatic requirement for cyanamide inactivation of rat liver aldehyde dehydrogenase. Biochem Pharmacol 34:1197-1204, 1985
    • (1985) Biochem Pharmacol , vol.34 , pp. 1197-1204
    • Svanas, G.W.1    Weiner, H.2
  • 20
    • 0019315384 scopus 로고
    • Kinetics of the reaction of cyclopropanone hydrate with yeast aldehyde dehydrogenase: A model for enzyme-substrate interaction
    • Wiseman JS, Tayrien G, Abeles RH: Kinetics of the reaction of cyclopropanone hydrate with yeast aldehyde dehydrogenase: A model for enzyme-substrate interaction. Biochemistry 19:4222-4231, 1980
    • (1980) Biochemistry , vol.19 , pp. 4222-4231
    • Wiseman, J.S.1    Tayrien, G.2    Abeles, R.H.3
  • 21
    • 0018575509 scopus 로고
    • The antipyrine test in clinical pharmacology: Conceptions and misconceptions
    • Vessell ES: The antipyrine test in clinical pharmacology: Conceptions and misconceptions. Clin Pharmacol Ther 26:275-286, 1979
    • (1979) Clin Pharmacol Ther , vol.26 , pp. 275-286
    • Vessell, E.S.1
  • 22
    • 0018198673 scopus 로고
    • 14C-methyl) aminopyrine in hepatitis, cirrhosis and hepatic bilharziasis: Its relationship to aminopyrine pharmacokinetics
    • 14C-methyl) aminopyrine in hepatitis, cirrhosis and hepatic bilharziasis: Its relationship to aminopyrine pharmacokinetics. Eur J Clin Pharmacol 13:223-229, 1978
    • (1978) Eur J Clin Pharmacol , vol.13 , pp. 223-229
    • Noordhoek, J.1    Dees, J.2    Savenije Chapel, E.M.3    Wilson, J.H.4
  • 23
    • 0014322950 scopus 로고
    • Metabolism of drugs. LIX. A new metabolite of antipyrine
    • Yoshimura H, Shimeno H, Tsukamoto H: Metabolism of drugs. LIX. A new metabolite of antipyrine. Biochem Pharmacol 17:1511-1516, 1968
    • (1968) Biochem Pharmacol , vol.17 , pp. 1511-1516
    • Yoshimura, H.1    Shimeno, H.2    Tsukamoto, H.3
  • 24
    • 0015543159 scopus 로고
    • Norphenazone, a new metabolite of phenazone in human urine
    • Baty JD, Evans DA: Norphenazone, a new metabolite of phenazone in human urine. J Pharm Pharmacol 25:83-84, 1973
    • (1973) J Pharm Pharmacol , vol.25 , pp. 83-84
    • Baty, J.D.1    Evans, D.A.2
  • 25
    • 0019185860 scopus 로고
    • Antipyrine metabolism in the rat by three hepatic monooxygenases
    • Inaba T, Lucassen M, Kalow W: Antipyrine metabolism in the rat by three hepatic monooxygenases. Life Sci 26:1977-1983, 1980
    • (1980) Life Sci , vol.26 , pp. 1977-1983
    • Inaba, T.1    Lucassen, M.2    Kalow, W.3
  • 26
    • 0019938355 scopus 로고
    • Differential effects of 3-methylcholanthrene and phenobarbitone treatment on the oxidative metabolism of antipyrine in vitro by microsomal fractions of rat liver
    • Kahn GC, Boobis AR, Murray S, Davies DS: Differential effects of 3-methylcholanthrene and phenobarbitone treatment on the oxidative metabolism of antipyrine in vitro by microsomal fractions of rat liver. Xenobiotica 12:509-516, 1982
    • (1982) Xenobiotica , vol.12 , pp. 509-516
    • Kahn, G.C.1    Boobis, A.R.2    Murray, S.3    Davies, D.S.4
  • 27
    • 0025057575 scopus 로고
    • Metabolism of metronidozole and antipyrine in hepatocytes isolated from mouse and rat
    • Loft S, Poulsen HE: Metabolism of metronidozole and antipyrine in hepatocytes isolated from mouse and rat. Xenobiotica 20:185-191, 1990
    • (1990) Xenobiotica , vol.20 , pp. 185-191
    • Loft, S.1    Poulsen, H.E.2
  • 28
    • 0005822551 scopus 로고
    • The fate of aminopyrine (pyramidon) in man and methods for the estimation of aminopyrine and its metabolites in biological material
    • Brodie BB, Axelrod J: The fate of aminopyrine (pyramidon) in man and methods for the estimation of aminopyrine and its metabolites in biological material. J Pharmacol Exp Ther 99:171-184, 1950
    • (1950) J Pharmacol Exp Ther , vol.99 , pp. 171-184
    • Brodie, B.B.1    Axelrod, J.2
  • 29
    • 0023706607 scopus 로고
    • Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: Simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography
    • Imaoka S, Inoue K, Funae Y: Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: Simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography. Arch Biochem Biophys 265:159-170, 1988
    • (1988) Arch Biochem Biophys , vol.265 , pp. 159-170
    • Imaoka, S.1    Inoue, K.2    Funae, Y.3
  • 30
    • 0015071504 scopus 로고
    • Aminopyrine demethylase - Multiplicity shown by dieldrin and DDT inhibition
    • Aust SD, Stevens JB: Aminopyrine demethylase - Multiplicity shown by dieldrin and DDT inhibition. Biochem Pharmacol 20:1061-1069, 1971
    • (1971) Biochem Pharmacol , vol.20 , pp. 1061-1069
    • Aust, S.D.1    Stevens, J.B.2
  • 31
    • 0014216041 scopus 로고
    • Removal of fatty acids from serum albumin by charcoal treatment
    • Chen RF: Removal of fatty acids from serum albumin by charcoal treatment, J Biol Chem 242:173-181, 1967
    • (1967) J Biol Chem , vol.242 , pp. 173-181
    • Chen, R.F.1
  • 33
    • 0014645531 scopus 로고
    • High-yield preparation of isolated rat liver parenchymal cells: A biochemical and fine structural study
    • Berry MN, Friend DS: High-yield preparation of isolated rat liver parenchymal cells: A biochemical and fine structural study. J Cell Biol 43:506-520, 1969
    • (1969) J Cell Biol , vol.43 , pp. 506-520
    • Berry, M.N.1    Friend, D.S.2
  • 34
    • 0024451118 scopus 로고
    • The characterization of perfluorosuccinate as an inhibitor of gluconeogenesis in isolated rat hepatocytes
    • Gregory RB, Berry MN: The characterization of perfluorosuccinate as an inhibitor of gluconeogenesis in isolated rat hepatocytes. Biochem Pharmacol 38:2867-2872, 1989
    • (1989) Biochem Pharmacol , vol.38 , pp. 2867-2872
    • Gregory, R.B.1    Berry, M.N.2
  • 36
    • 0022195439 scopus 로고
    • The roles of the hepato-cellular redox state and the hepatic acetaldehyde concentration in determining the ethanol elimination rate in fasted rats
    • Ryle PR, Chakraborty J, Thomson AD: The roles of the hepato-cellular redox state and the hepatic acetaldehyde concentration in determining the ethanol elimination rate in fasted rats. Biochem Pharmacol 34:3577-3583, 1985
    • (1985) Biochem Pharmacol , vol.34 , pp. 3577-3583
    • Ryle, P.R.1    Chakraborty, J.2    Thomson, A.D.3
  • 37
    • 0016231069 scopus 로고
    • Effects of bicarbonate on intercompartmental reducing-equivalent translocation in isolated parenchymal cells from rat liver
    • Berry MN, Werner HV, Kun E: Effects of bicarbonate on intercompartmental reducing-equivalent translocation in isolated parenchymal cells from rat liver. Biochem J 140:355-361, 1974
    • (1974) Biochem J , vol.140 , pp. 355-361
    • Berry, M.N.1    Werner, H.V.2    Kun, E.3
  • 38
    • 0018196525 scopus 로고
    • Effects of glucagon and N6O2′-dibutyryladenosine 3′:5′-cyclic monophosphate on calcium transport in isolated rat liver mitochondria
    • Hughes BP, Barritt GJ: Effects of glucagon and N6O2′-dibutyryladenosine 3′:5′-cyclic monophosphate on calcium transport in isolated rat liver mitochondria. Biochem J 176:295-304, 1978
    • (1978) Biochem J , vol.176 , pp. 295-304
    • Hughes, B.P.1    Barritt, G.J.2
  • 39
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall AG, Bardawill CJ, David MM: Determination of serum proteins by means of the biuret reaction. J Biol Chem 177:751-766, 1949
    • (1949) J Biol Chem , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 40
    • 77049213269 scopus 로고
    • Enzymatic dealkylation of aminopyrine (pyramidon) and other alkylamines
    • La Du BN, Gaudette L, Trousof N, Brodie BB: Enzymatic dealkylation of aminopyrine (pyramidon) and other alkylamines. J Biol Chem 214:741-752, 1955
    • (1955) J Biol Chem , vol.214 , pp. 741-752
    • La Du, B.N.1    Gaudette, L.2    Trousof, N.3    Brodie, B.B.4
  • 41
    • 0014460337 scopus 로고
    • Pyrazole inhibition and kinetic studies of ethanol and retinol oxidation catalyzed by rat liver alcohol dehydrogcnase
    • Reynier M: Pyrazole inhibition and kinetic studies of ethanol and retinol oxidation catalyzed by rat liver alcohol dehydrogcnase. Acta Chem Scand 23:1119-1129, 1969
    • (1969) Acta Chem Scand , vol.23 , pp. 1119-1129
    • Reynier, M.1
  • 42
    • 0014455297 scopus 로고
    • Human liver alcohol dehydrogenase: Inhibition by pyrazole and pyrazole analogs
    • Li TK, Theorell H: Human liver alcohol dehydrogenase: Inhibition by pyrazole and pyrazole analogs. Acta Chem Scand 23:892-902, 1969
    • (1969) Acta Chem Scand , vol.23 , pp. 892-902
    • Li, T.K.1    Theorell, H.2
  • 44
    • 0018949006 scopus 로고
    • The effect of cimetidine on in vitro and in vivo microsomal drug metabolism in the rat
    • Pelkonen O, Puurunen J: The effect of cimetidine on in vitro and in vivo microsomal drug metabolism in the rat. Biochem Pharmacol 29:3075-3080, 1980
    • (1980) Biochem Pharmacol , vol.29 , pp. 3075-3080
    • Pelkonen, O.1    Puurunen, J.2
  • 45
    • 0020041376 scopus 로고
    • Drug metabolism by rat and human hepatic microsomes in response to interaction with H2-receptor antagonists
    • Knodell RG, Holtzman JL, Crankshaw DL, Steele NM, Stanley LN: Drug metabolism by rat and human hepatic microsomes in response to interaction with H2-receptor antagonists. Gastroenterology 82:84-88, 1982
    • (1982) Gastroenterology , vol.82 , pp. 84-88
    • Knodell, R.G.1    Holtzman, J.L.2    Crankshaw, D.L.3    Steele, N.M.4    Stanley, L.N.5
  • 46
  • 47
    • 0027970952 scopus 로고
    • Characterisation of praziquantel metabolism by rat liver microsomes using cytochrome P450 inhibitors
    • Masimirembwa CM, Hasler JA: Characterisation of praziquantel metabolism by rat liver microsomes using cytochrome P450 inhibitors. Biochem Pharmacol 48:1779-1783, 1994
    • (1994) Biochem Pharmacol , vol.48 , pp. 1779-1783
    • Masimirembwa, C.M.1    Hasler, J.A.2
  • 48
    • 0014415077 scopus 로고
    • Studies on microsomal hydroxylation and the demonstration of a new carbon monoxide binding pigment in liver microsomes
    • Kuntzman R, Levin W, Jacobson M, Conney AH: Studies on microsomal hydroxylation and the demonstration of a new carbon monoxide binding pigment in liver microsomes. Life Sci 7:215-224, 1968
    • (1968) Life Sci , vol.7 , pp. 215-224
    • Kuntzman, R.1    Levin, W.2    Jacobson, M.3    Conney, A.H.4
  • 49
    • 0014815050 scopus 로고
    • Aminopyrine demethylase. Kinetic evidence for multiple microsomal activities
    • Pederson TC, Aust SD: Aminopyrine demethylase. Kinetic evidence for multiple microsomal activities. Biochem Pharmacol 19:2221-2230, 1970
    • (1970) Biochem Pharmacol , vol.19 , pp. 2221-2230
    • Pederson, T.C.1    Aust, S.D.2
  • 51
    • 0021948738 scopus 로고
    • Aldehyde dehydrogenase activity as the rate-limiting factor for acetaldehyde metabolism in rat liver
    • Svanas GW, Weiner H: Aldehyde dehydrogenase activity as the rate-limiting factor for acetaldehyde metabolism in rat liver. Arch Biochem Biophys 236:36-46, 1985
    • (1985) Arch Biochem Biophys , vol.236 , pp. 36-46
    • Svanas, G.W.1    Weiner, H.2


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