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Volumn 40, Issue 4, 2012, Pages 788-795

Carbonyl reduction of mequindox by chicken and porcine cytosol and cloned carbonyl reductase 1

Author keywords

[No Author keywords available]

Indexed keywords

1 DEOXYMEQUINDOX; 2 ISOETHANOL 1 DEOXYMEQUINDOX; 2 ISOETHANOL MEQUINDOX; AMINO ACID; CARBADOX; CARBONYL DERIVATIVE; CARBONYL REDUCTASE; CARBONYL REDUCTASE 1; DRUG METABOLITE; MENADIONE; MEQUINDOX; OLAQUINDIOX; OXIDE; QUINOXALINE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 84863352299     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.111.043547     Document Type: Article
Times cited : (6)

References (33)
  • 1
    • 66449103252 scopus 로고    scopus 로고
    • Two nonsynonymous single nucleotide polymorphisms of human carbonyl reductase 1 demonstrate reduced in vitro metabolism of daunorubicin and doxorubicin
    • Bains OS, Karkling MJ, Grigliatti TA, Reid RE, and Riggs KW (2009) Two nonsynonymous single nucleotide polymorphisms of human carbonyl reductase 1 demonstrate reduced in vitro metabolism of daunorubicin and doxorubicin. Drug Metab Dispos 37:1107-1114.
    • (2009) Drug Metab Dispos , vol.37 , pp. 1107-1114
    • Bains, O.S.1    Karkling, M.J.2    Grigliatti, T.A.3    Reid, R.E.4    Riggs, K.W.5
  • 2
    • 0019847072 scopus 로고
    • Mutagenicity of quindoxin, its metabolites, and two substituted quinoxaline-Di-N-oxides
    • Beutin L, Preller E, and Kowalski B (1981) Mutagenicity of quindoxin, its metabolites, and two substituted quinoxaline-di-N-oxides. Antimicrob Agents Chemother 20:336-343. (Pubitemid 12225710)
    • (1981) Antimicrobial Agents and Chemotherapy , vol.20 , Issue.3 , pp. 336-343
    • Beutin, L.1    Preller, E.2    Kowalski, B.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation 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
  • 5
    • 58149483488 scopus 로고    scopus 로고
    • Investigation of the genotoxicity of quinocetone, carbadox and olaquindox in vitro using Vero cells
    • Chen Q, Tang S, Jin X, Zou J, Chen K, Zhang T, and Xiao X (2009) Investigation of the genotoxicity of quinocetone, carbadox and olaquindox in vitro using Vero cells. Food Chem Toxicol 47:328-334.
    • (2009) Food Chem Toxicol , vol.47 , pp. 328-334
    • Chen, Q.1    Tang, S.2    Jin, X.3    Zou, J.4    Chen, K.5    Zhang, T.6    Xiao, X.7
  • 6
    • 5544294631 scopus 로고    scopus 로고
    • Human carbonyl reductase catalyzes reduction of 4-oxonon-2-enal
    • DOI 10.1021/bi049136q
    • Doorn JA, Maser E, Blum A, Claffey DJ, and Petersen DR (2004) Human carbonyl reductase catalyzes reduction of 4-oxonon-2-enal. Biochemistry 43:13106-13114. (Pubitemid 39366059)
    • (2004) Biochemistry , vol.43 , Issue.41 , pp. 13106-13114
    • Doorn, J.A.1    Maser, E.2    Blum, A.3    Claffey, D.J.4    Petersen, D.R.5
  • 7
    • 59349113924 scopus 로고    scopus 로고
    • Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis
    • El-Hawari Y, Favia AD, Pilka ES, Kisiela M, Oppermann U, Martin HJ, and Maser E (2009) Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis. Chem Biol Interact 178:234-241.
    • (2009) Chem Biol Interact , vol.178 , pp. 234-241
    • El-Hawari, Y.1    Favia, A.D.2    Pilka, E.S.3    Kisiela, M.4    Oppermann, U.5    Martin, H.J.6    Maser, E.7
  • 8
    • 34250864375 scopus 로고    scopus 로고
    • Reactive carbonyls and oxidative stress: Potential for therapeutic intervention
    • Ellis EM (2007) Reactive carbonyls and oxidative stress: potential for therapeutic intervention. Pharmacol Ther 115:13-24.
    • (2007) Pharmacol Ther , vol.115 , pp. 13-24
    • Ellis, E.M.1
  • 9
    • 0034527727 scopus 로고    scopus 로고
    • Carbonyl reductase
    • DOI 10.1016/S0009-2797(00)00196-4, PII S0009279700001964
    • Forrest GL and Gonzalez B (2000) Carbonyl reductase. Chem Biol Interact 129:21-40. (Pubitemid 32061052)
    • (2000) Chemico-Biological Interactions , vol.129 , Issue.1-2 , pp. 21-40
    • Forrest, G.L.1    Gonzalez, B.2
  • 10
    • 0035947598 scopus 로고    scopus 로고
    • Porcine carbonyl reductase. Structural basis for a functional monomer in short chain dehydrogenases/reductases
    • Ghosh D, Sawicki M, Pletnev V, Erman M, Ohno S, Nakajin S, and Duax WL (2001) Porcine carbonyl reductase. Structural basis for a functional monomer in short chain dehydrogenases/reductases. J Biol Chem 276:18457-18463.
    • (2001) J Biol Chem , vol.276 , pp. 18457-18463
    • Ghosh, D.1    Sawicki, M.2    Pletnev, V.3    Erman, M.4    Ohno, S.5    Nakajin, S.6    Duax, W.L.7
  • 11
    • 34249009348 scopus 로고    scopus 로고
    • A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity
    • DOI 10.1124/dmd.107.014779
    • Gonzalez-Covarrubias V, Ghosh D, Lakhman SS, Pendyala L, and Blanco JG (2007) A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity. Drug Metab Dispos 35:973-980. (Pubitemid 46798608)
    • (2007) Drug Metabolism and Disposition , vol.35 , Issue.6 , pp. 973-980
    • Gonzalez-Covarrubias, V.1    Ghosh, D.2    Lakhman, S.S.3    Pendyala, L.4    Blanco, J.G.5
  • 12
    • 70449523001 scopus 로고    scopus 로고
    • Long-term dose-dependent response of Mequindox on aldosterone, corticosterone and five steroidogenic enzyme mRNAs in the adrenal of male rats
    • Huang XJ, Ihsan A, Wang X, Dai MH, Wang YL, Su SJ, Xue XJ, and Yuan ZH (2009) Long-term dose-dependent response of Mequindox on aldosterone, corticosterone and five steroidogenic enzyme mRNAs in the adrenal of male rats. Toxicol Lett 191:167-173.
    • (2009) Toxicol Lett , vol.191 , pp. 167-173
    • Huang, X.J.1    Ihsan, A.2    Wang, X.3    Dai, M.H.4    Wang, Y.L.5    Su, S.J.6    Xue, X.J.7    Yuan, Z.H.8
  • 15
    • 79954629408 scopus 로고    scopus 로고
    • Long-term mequindox treatment induced endocrine and reproductive toxicity via oxidative stress in male Wistar rats
    • Ihsan A, Wang X, Liu Z, Wang Y, Huang X, Liu Y, Yu H, Zhang H, Li T, Yang C, et al. (2011) Long-term mequindox treatment induced endocrine and reproductive toxicity via oxidative stress in male Wistar rats. Toxicol Appl Pharmacol 252:281-288.
    • (2011) Toxicol Appl Pharmacol , vol.252 , pp. 281-288
    • Ihsan, A.1    Wang, X.2    Liu, Z.3    Wang, Y.4    Huang, X.5    Liu, Y.6    Yu, H.7    Zhang, H.8    Li, T.9    Yang, C.10
  • 17
    • 77949602182 scopus 로고    scopus 로고
    • Metabolism of mequindox in liver microsomes of rats, chicken and pigs
    • Liu ZY, Huang LL, Chen DM, and Yuan ZH (2010) Metabolism of mequindox in liver microsomes of rats, chicken and pigs. Rapid Commun Mass Spectrom 24:909-918.
    • (2010) Rapid Commun Mass Spectrom , vol.24 , pp. 909-918
    • Liu, Z.Y.1    Huang, L.L.2    Chen, D.M.3    Yuan, Z.H.4
  • 20
    • 41549117154 scopus 로고    scopus 로고
    • Metabolism of olaquindox in rat liver microsomes: Structural elucidation of metabolites by high-performance liquid chromatography combined with ion trap/time-of-flight mass spectrometry
    • DOI 10.1002/rcm.3422
    • Liu Z, Huang L, Dai M, Chen D, Wang Y, Tao Y, and Yuan Z (2008) Metabolism of olaquindox in rat liver microsomes: structural elucidation of metabolites by high-performance liquid chromatography combined with ion trap/time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 22:1009-1016. (Pubitemid 351468256)
    • (2008) Rapid Communications in Mass Spectrometry , vol.22 , Issue.7 , pp. 1009-1016
    • Liu, Z.1    Huang, L.2    Dai, M.3    Chen, D.4    Wang, Y.5    Tao, Y.6    Yuan, Z.7
  • 21
    • 0028797794 scopus 로고
    • Xenobiotic carbonyl reduction and physiological steroid oxidoreduction. The pluripotency of several hydroxysteroid dehydrogenases
    • Maser E (1995) Xenobiotic carbonyl reduction and physiological steroid oxidoreduction. The pluripotency of several hydroxysteroid dehydrogenases. Biochem Pharmacol 49:421-440.
    • (1995) Biochem Pharmacol , vol.49 , pp. 421-440
    • Maser, E.1
  • 22
    • 33645963469 scopus 로고    scopus 로고
    • Multiplicity of mammalian reductases for xenobiotic carbonyl compounds
    • Matsunaga T, Shintani S, and Hara A (2006) Multiplicity of mammalian reductases for xenobiotic carbonyl compounds. Drug Metab Pharmacokinet 21:1-18.
    • (2006) Drug Metab Pharmacokinet , vol.21 , pp. 1-18
    • Matsunaga, T.1    Shintani, S.2    Hara, A.3
  • 23
    • 0028786479 scopus 로고
    • Direct expression of pig testicular 3 alpha/beta (20 beta)-hydroxysteroid dehydrogenase in Escherichia coli
    • Nakajin S, Nakajima T, Uchida M, Ohno S, and Shinoda M (1995) Direct expression of pig testicular 3 alpha/beta (20 beta)-hydroxysteroid dehydrogenase in Escherichia coli. J Steroid Biochem Mol Biol 54:257-264.
    • (1995) J Steroid Biochem Mol Biol , vol.54 , pp. 257-264
    • Nakajin, S.1    Nakajima, T.2    Uchida, M.3    Ohno, S.4    Shinoda, M.5
  • 24
    • 0031390072 scopus 로고    scopus 로고
    • Carbonyl reductase activity exhibited by pig testicular 20beta- hydroxysteroid dehydrogenase
    • Nakajin S, Tamura F, Takase N, and Toyoshima S (1997) Carbonyl reductase activity exhibited by pig testicular 20 beta-hydroxysteroid dehydrogenase. Biol Pharm Bull 20:1215-1218. (Pubitemid 28543275)
    • (1997) Biological and Pharmaceutical Bulletin , vol.20 , Issue.11 , pp. 1215-1218
    • Nakajin, S.1    Tamura, F.2    Takase, N.3    Toyoshima, S.4
  • 25
    • 33846945701 scopus 로고    scopus 로고
    • Carbonyl reductases: The complex relationships of mammalian carbonyland quinone-reducing enzymes and their role in physiology
    • Oppermann U (2007) Carbonyl reductases: the complex relationships of mammalian carbonyland quinone-reducing enzymes and their role in physiology. Annu Rev Pharmacol Toxicol 47:293-322.
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 293-322
    • Oppermann, U.1
  • 26
    • 0034600004 scopus 로고    scopus 로고
    • Molecular and structural aspects of xenobiotic carbonyl metabolizing enzymes. Role of reductases and dehydrogenases in xenobiotic phase I reactions
    • DOI 10.1016/S0300-483X(99)00192-4, PII S0300483X99001924
    • Oppermann UC and Maser E (2000) Molecular and structural aspects of xenobiotic carbonyl metabolizing enzymes. Role of reductases and dehydrogenases in xenobiotic phase I reactions. Toxicology 144:71-81. (Pubitemid 30201622)
    • (2000) Toxicology , vol.144 , Issue.1-3 , pp. 71-81
    • Oppermann, U.C.T.1    Maser, E.2
  • 28
    • 29344462467 scopus 로고    scopus 로고
    • Differences in catalytic activity between rat testicular and ovarian carbonyl reductases are due to two amino acids
    • DOI 10.1016/j.febslet.2005.11.049, PII S0014579305014195
    • Sciotti MA, Tam S, Wermuth B, and Baker ME (2006) Differences in catalytic activity between rat testicular and ovarian carbonyl reductases are due to two amino acids. FEBS Lett 580:67-71. (Pubitemid 43005314)
    • (2006) FEBS Letters , vol.580 , Issue.1 , pp. 67-71
    • Sciotti, M.A.1    Tam, S.2    Wermuth, B.3    Baker, M.E.4
  • 29
    • 2442500823 scopus 로고    scopus 로고
    • 3alpha/beta,20beta-Hydroxysteroid dehydrogenase (porcine testicular carbonyl reductase) also has a cysteine residue that is involved in binding of cofactor NADPH
    • DOI 10.1016/j.jsbmb.2003.12.013, PII S096007600400038X
    • Sugiyama T, Ohno S, Ghosh D, and Nakajin S (2004) 3alpha/beta,20beta- hydroxysteroid dehydrogenase (porcine testicular carbonyl reductase) also has a cysteine residue that is involved in binding of cofactor NADPH. J Steroid Biochem Mol Biol 88:393-398. (Pubitemid 38625604)
    • (2004) Journal of Steroid Biochemistry and Molecular Biology , vol.88 , Issue.4-5 , pp. 393-398
    • Sugiyama, T.1    Ohno, S.2    Ghosh, D.3    Nakajin, S.4
  • 31
  • 32
    • 0037165491 scopus 로고    scopus 로고
    • Teratogenic assessment of carbadox in rats
    • Yoshimura H (2002) Teratogenic assessment of carbadox in rats. Toxicol Lett 129:115-118.
    • (2002) Toxicol Lett , vol.129 , pp. 115-118
    • Yoshimura, H.1
  • 33
    • 80053947167 scopus 로고    scopus 로고
    • The mechanism of enzymatic and non-enzymatic N-oxide reductive metabolism of cyadox in pig liver
    • Zheng M, Jiang J, Wang J, Tang X, Ouyang M, and Deng Y (2011) The mechanism of enzymatic and non-enzymatic N-oxide reductive metabolism of cyadox in pig liver. Xenobiotica 41: 964-971.
    • (2011) Xenobiotica , vol.41 , pp. 964-971
    • Zheng, M.1    Jiang, J.2    Wang, J.3    Tang, X.4    Ouyang, M.5    Deng, Y.6


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