메뉴 건너뛰기




Volumn 3 NOV, Issue , 2012, Pages

The role of human aldo-keto reductases in the metabolic activation and detoxication of polycyclic aromatic hydrocarbons: Interconversion of PAH catechols and PAH o-quinones

Author keywords

Aldo keto reductases; Conjugation reactions; O quinones; Phase II metabolism; Polycyclic aromatic hydrocarbons; Redox cycling

Indexed keywords

7,8 DIHYDRO 7,8 DIHYDROXYBENZO[A]PYRENE; ALDO KETO REDUCTASE; ALDO KETO REDUCTASE 1A1; ALDO KETO REDUCTASE 1B1; ALDO KETO REDUCTASE 1B10; ALDO KETO REDUCTASE 1C1; ALDO KETO REDUCTASE 1C2; ALDO KETO REDUCTASE 1C3; ALDO KETO REDUCTASE 1C4; ALDO KETO REDUCTASE 1C9; ALDO KETO REDUCTASE 7A2; BENZO[A]PYRENE 7,8 CATECHOL; BENZO[A]PYRENE 7,8 DIONE; BENZO[A]PYRENE DERIVATIVE; CARBONYL REDUCTASE; CATECHOL METHYLTRANSFERASE; GLUCURONOSYLTRANSFERASE; OXIDOREDUCTASE; POLYCYCLIC AROMATIC HYDROCARBON CATECHOL DERIVATIVE; POLYCYCLIC AROMATIC HYDROCARBON DERIVATIVE; POLYCYCLIC AROMATIC HYDROCARBON DIHYDRODIOL; POLYCYCLIC AROMATIC HYDROCARBON O QUINONE DERIVATIVE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); SULFOTRANSFERASE; SULFOTRANSFERASE 1A1; SULFOTRANSFERASE 1A3; SULFOTRANSFERASE 1E1; UNCLASSIFIED DRUG;

EID: 84870690777     PISSN: None     EISSN: 16639812     Source Type: Journal    
DOI: 10.3389/fphar.2012.00193     Document Type: Article
Times cited : (38)

References (106)
  • 1
    • 0036293451 scopus 로고    scopus 로고
    • Catecholestrogen sulfa-tion: possible role in carcinogenesis
    • Adjei, A. A., and Weinshilboum, R. M. (2002). Catecholestrogen sulfa-tion: possible role in carcinogenesis. Biochem. Biophys. Res. Commun. 292, 402-408.
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 402-408
    • Adjei, A.A.1    Weinshilboum, R.M.2
  • 2
    • 0025374597 scopus 로고
    • Estradiol metabolism by complementary deoxyri-bonucleic acid-expressed human cytochrome P450s
    • Aoyama, T., Korzekwa, K., Nagata, K., Gillette, J., Gelboin, H. V., and Gonzalez, F. J. (1990). Estradiol metabolism by complementary deoxyri-bonucleic acid-expressed human cytochrome P450s. Endocrinology 126, 3101-3106.
    • (1990) Endocrinology , vol.126 , pp. 3101-3106
    • Aoyama, T.1    Korzekwa, K.2    Nagata, K.3    Gillette, J.4    Gelboin, H.V.5    Gonzalez, F.J.6
  • 3
    • 0013886618 scopus 로고
    • Methylation reactions in the formation and metabolism of catecholamines and other biogenic amines
    • Axelrod, J. (1966). Methylation reactions in the formation and metabolism of catecholamines and other biogenic amines. Pharmacol. Rev. 18, 95-113.
    • (1966) Pharmacol. Rev. , vol.18 , pp. 95-113
    • Axelrod, J.1
  • 4
    • 70449228544 scopus 로고
    • Enzymatic O-methylation of epi-nephrine and other catechols
    • Axelrod, J., and Tomchick, R. (1958). Enzymatic O-methylation of epi-nephrine and other catechols. J. Biol. Chem. 233, 702-705.
    • (1958) J. Biol. Chem. , vol.233 , pp. 702-705
    • Axelrod, J.1    Tomchick, R.2
  • 5
    • 70350543787 scopus 로고    scopus 로고
    • Reductive metabolism of AGE precursors: a metabolic route for preventing AGE accumulation in cardiovascular tissue
    • Baba, S. P., Barski, O. A., Ahmed, Y., O'Toole, T. E., Conklin, D. J., Bhatnagar, A., et al. (2009). Reductive metabolism of AGE precursors: a metabolic route for preventing AGE accumulation in cardiovascular tissue. Diabetes 58, 2486-2497.
    • (2009) Diabetes , vol.58 , pp. 2486-2497
    • Baba, S.P.1    Barski, O.A.2    Ahmed, Y.3    O'Toole, T.E.4    Conklin, D.J.5    Bhatnagar, A.6
  • 6
    • 0015324170 scopus 로고
    • Interactions tween estrogens and catechol amines. 3. Studies on the methy-lation of catechol estrogens, catechol amines and other catechols by the catechol-O-methyltransferases of human liver
    • Ball, P., Knuppen, R., Haupt, M., and Breuer, H. (1972). Interactions tween estrogens and catechol amines. 3. Studies on the methy-lation of catechol estrogens, catechol amines and other catechols by the catechol-O-methyltransferases of human liver. J. Clin. Endocrinol. Metab. 34, 736-746.
    • (1972) J. Clin. Endocrinol. Metab. , vol.34 , pp. 736-746
    • Ball, P.1    Knuppen, R.2    Haupt, M.3    Breuer, H.4
  • 7
    • 33746316031 scopus 로고    scopus 로고
    • /-mononucleotide adduct standards for 32P post-labeling analyses: detection of benzo[a]pyrene-7, 8-quinone-calf thymus DNA adducts
    • /-mononucleotide adduct standards for 32P post-labeling analyses: detection of benzo[a]pyrene-7, 8-quinone-calf thymus DNA adducts. Anal. Biochem. 355, 213-223.
    • (2006) Anal. Biochem. , vol.355 , pp. 213-223
    • Balu, N.1    Padgett, W.T.2    Nelson, G.B.3    Lambert, G.R.4    Ross, J.A.5    Nesnow, S.6
  • 8
    • 33845318191 scopus 로고    scopus 로고
    • Endogenous glu-tathione adducts
    • Blair, I. A. (2006). Endogenous glu-tathione adducts. Curr. Drug Metab. 7, 853-872.
    • (2006) Curr. Drug Metab. , vol.7 , pp. 853-872
    • Blair, I.A.1
  • 9
    • 75149126749 scopus 로고    scopus 로고
    • Analysis of endogenous glutathione-adducts and their metabolites
    • Blair, I. A. (2010). Analysis of endogenous glutathione-adducts and their metabolites. Biomed. Chromatogr. 24, 29-38.
    • (2010) Biomed. Chromatogr. , vol.24 , pp. 29-38
    • Blair, I.A.1
  • 10
    • 38949118229 scopus 로고    scopus 로고
    • Potential mechanisms of estrogen quinone carcinogenesis
    • Bolton, J. L., and Thatcher, G. R. (2008). Potential mechanisms of estrogen quinone carcinogenesis. Chem. Res. Toxicol. 21, 93-101.
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 93-101
    • Bolton, J.L.1    Thatcher, G.R.2
  • 12
    • 0021678097 scopus 로고
    • Estrogen metabolism in rat liver microsomal and isolated hepatocyte preparations -I. Metabolite formation and irreversible binding to cellular macro-molecules
    • Brueggemeier, R. W., Kimball, J. G., and Kraft, F. (1984). Estrogen metabolism in rat liver microsomal and isolated hepatocyte preparations -I. Metabolite formation and irreversible binding to cellular macro-molecules. Biochem. Pharmacol. 33, 3853-3859.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 3853-3859
    • Brueggemeier, R.W.1    Kimball, J.G.2    Kraft, F.3
  • 13
    • 0032510704 scopus 로고    scopus 로고
    • Expression and characterization of four recombinant human dihydro-diol dehydrogenase isoforms:oxidation of trans-7, 8-dihydroxy-7, 8-dihydrobenzo[a]pyrene to the activated o-quinone metabo lite benzo[a]pyrene-7, 8-dione
    • Burczynski, M. E., Harvey, R. G., and Penning, T. M. (1998). Expression and characterization of four recombinant human dihydro-diol dehydrogenase isoforms:oxidation of trans-7, 8-dihydroxy-7, 8-dihydrobenzo[a]pyrene to the activated o-quinone metabo lite benzo[a]pyrene-7, 8-dione. Biochemistry 37, 6781-6790.
    • (1998) Biochemistry , vol.37 , pp. 6781-6790
    • Burczynski, M.E.1    Harvey, R.G.2    Penning, T.M.3
  • 14
    • 0033083205 scopus 로고    scopus 로고
    • Isoform-specific induction of a human aldo-keto reductase by polycyclic aromatic hydrocarbons (PAHs), elec-trophiles, and oxidative stress: implications for the alternative pathway of PAH activation catalyzed by human dihydrodiol dehydrogenase
    • Burczynski, M. E., Lin, H. K., and Penning, T. M. (1999). Isoform-specific induction of a human aldo-keto reductase by polycyclic aromatic hydrocarbons (PAHs), elec-trophiles, and oxidative stress: implications for the alternative pathway of PAH activation catalyzed by human dihydrodiol dehydrogenase. Cancer Res. 59, 607-614.
    • (1999) Cancer Res , vol.59 , pp. 607-614
    • Burczynski, M.E.1    Lin, H.K.2    Penning, T.M.3
  • 16
    • 0035132693 scopus 로고    scopus 로고
    • Sulfation pharmacogenetics: SULT1A1 and SULT1A2 allele frequencies in Caucasian. Chinese and African-American subjects
    • Carlini, E. J., Raftogianis, R. B., Wood, T. C., Jin, F., Zheng, W., Rebbeck, T. R., et al. (2001). Sulfation pharmacogenetics: SULT1A1 and SULT1A2 allele frequencies in Caucasian, Chinese and African-American subjects. Pharmacogenetics 11, 57-68.
    • (2001) Pharmacogenetics , vol.11 , pp. 57-68
    • Carlini, E.J.1    Raftogianis, R.B.2    Wood, T.C.3    Jin, F.4    Zheng, W.5    Rebbeck, T.R.6
  • 17
    • 0029080079 scopus 로고
    • Central role of radical cations in metabolic activation of polycyclic aromatic hydrocarbons
    • Cavalieri, E. L., and Rogan, E. G. (1995). Central role of radical cations in metabolic activation of polycyclic aromatic hydrocarbons. Xenobiotica 25, 677-688.
    • (1995) Xenobiotica , vol.25 , pp. 677-688
    • Cavalieri, E.L.1    Rogan, E.G.2
  • 19
    • 0026592966 scopus 로고
    • 8-Hydroxyguanine, an abundant form of oxidative DNA damage, causes G-T and AC substitutions
    • Cheng, K. C, Cahill, D. S., Kasai, H., Nishimura, S., and Loeb, L. A. (1992). 8-Hydroxyguanine, an abundant form of oxidative DNA damage, causes G-T and AC substitutions. J. Biol. Chem. 267, 166-172.
    • (1992) J. Biol. Chem. , vol.267 , pp. 166-172
    • Cheng, K.C.1    Cahill, D.S.2    Kasai, H.3    Nishimura, S.4    Loeb, L.A.5
  • 20
    • 0020431144 scopus 로고
    • Induction of microsomal enzymes by foreign chemicals and carcinogenesis by polycyclic aromatic hydrocarbons: G. H. A. Clowes Memorial Lecture
    • Conney, A. H. (1982). Induction of microsomal enzymes by foreign chemicals and carcinogenesis by polycyclic aromatic hydrocarbons: G. H. A. Clowes Memorial Lecture. Cancer Res. 42, 4875-4917.
    • (1982) Cancer Res , vol.42 , pp. 4875-4917
    • Conney, A.H.1
  • 21
    • 64349109466 scopus 로고    scopus 로고
    • Tobacco and estrogen metabolic polymorphisms and risk of non-small cell lung cancer in women
    • Cote, M. L., Yoo, W., Wenzlaff, A. S., Prysak, G. M., Santer, S.K., Claeys, G. B., et al. (2009). Tobacco and estrogen metabolic polymorphisms and risk of non-small cell lung cancer in women. Carcinogenesis 30, 626-635.
    • (2009) Carcinogenesis , vol.30 , pp. 626-635
    • Cote, M.L.1    Yoo, W.2    Wenzlaff, A.S.3    Prysak, G.M.4    Santer, S.K.5    Claeys, G.B.6
  • 22
    • 0032549065 scopus 로고    scopus 로고
    • Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sul-fatases
    • Coughtrie, M. W., Sharp, S., Maxwell, K., and Innes, N. P. (1998). Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sul-fatases. Chem. Biol. Interact. 109, 3-27.
    • (1998) Chem. Biol. Interact. , vol.109 , pp. 3-27
    • Coughtrie, M.W.1    Sharp, S.2    Maxwell, K.3    Innes, N.P.4
  • 23
    • 35548999251 scopus 로고    scopus 로고
    • Diesel exhaust influences carcinogenic PAH-induced genotox-icity and gene expression in human breast epithelial cells in culture
    • Courter, L. A., Pereira, C., and Baird, W. M. (2007). Diesel exhaust influences carcinogenic PAH-induced genotox-icity and gene expression in human breast epithelial cells in culture. Mutat. Res. 625, 72-82.
    • (2007) Mutat. Res. , vol.625 , pp. 72-82
    • Courter, L.A.1    Pereira, C.2    Baird, W.M.3
  • 24
    • 0035884689 scopus 로고    scopus 로고
    • Catechol-O-methyltransferase (COMT)-mediated metabolism of catechol estrogens: comparison of wild-type and variant COMT isoforms
    • Dawling, S., Roodi, N., Mernaugh, R. L., Wang, X., and Parl, F. F. (2001). Catechol-O-methyltransferase (COMT)-mediated metabolism of catechol estrogens: comparison of wild-type and variant COMT isoforms. Cancer Res. 61, 6716-6722.
    • (2001) Cancer Res , vol.61 , pp. 6716-6722
    • Dawling, S.1    Roodi, N.2    Mernaugh, R.L.3    Wang, X.4    Parl, F.F.5
  • 25
    • 34247494222 scopus 로고    scopus 로고
    • The chemistry and analysis of large PAHs
    • Fetzer, J. C. (2007). The chemistry and analysis of large PAHs. Polycycl. Aro-mat. Compd. 27, 143-162.
    • (2007) Polycycl. Aro-mat. Compd. , vol.27 , pp. 143-162
    • Fetzer, J.C.1
  • 26
    • 0026713893 scopus 로고
    • Examination of diols and diol epoxides of polycyclic aromatic hydrocarbons as substrates for rat liver dihydrodiol dehydrogenase
    • Flowers-Geary, L., Harvey, R. G., and Penning, T. M. (1992). Examination of diols and diol epoxides of polycyclic aromatic hydrocarbons as substrates for rat liver dihydrodiol dehydrogenase. Chem. Res. Toxicol. 5, 576-583.
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 576-583
    • Flowers-Geary, L.1    Harvey, R.G.2    Penning, T.M.3
  • 27
    • 20144387888 scopus 로고    scopus 로고
    • Overexpres-sion of the aldo-keto reductase family protein AKR1B10 is highly correlated with smokers' non-small cell lung carcinomas
    • Fukumoto, S., Yamauchi, N., Moriguchi, H., Hippo, Y., Watanabe, A., Shiba-hara, J., et al. (2005). Overexpres-sion of the aldo-keto reductase family protein AKR1B10 is highly correlated with smokers' non-small cell lung carcinomas. Clin. Cancer Res. 11, 1776-1785.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 1776-1785
    • Fukumoto, S.1    Yamauchi, N.2    Moriguchi, H.3    Hippo, Y.4    Watanabe, A.5    Shiba-hara, J.6
  • 28
    • 0019074870 scopus 로고
    • Benzo[alpha]pyrene metabolism, activation and carcinogenesis: role and regulation of mixed-function oxidases and related enzymes
    • Gelboin, H. V. (1980). Benzo[alpha]pyrene metabolism, activation and carcinogenesis: role and regulation of mixed-function oxidases and related enzymes. Physiol. Rev. 60, 1107-1166.
    • (1980) Physiol. Rev. , vol.60 , pp. 1107-1166
    • Gelboin, H.V.1
  • 29
    • 0742321737 scopus 로고    scopus 로고
    • Phar-macogenetics of soluble sulfotrans-ferases (SULTs)
    • Glatt, H., and Meinl, W. (2004). Phar-macogenetics of soluble sulfotrans-ferases (SULTs). Naunyn Schmiede-bergs Arch. Pharmacol. 369, 55-68.
    • (2004) Naunyn Schmiede-bergs Arch. Pharmacol. , vol.369 , pp. 55-68
    • Glatt, H.1    Meinl, W.2
  • 30
    • 0016524263 scopus 로고
    • Polycylic aromatic hydrocarbon profile analysis of high-protein foods, oils, and fats by gas chro-matography
    • Grimmer, G., and Bohnke, H. (1975). Polycylic aromatic hydrocarbon profile analysis of high-protein foods, oils, and fats by gas chro-matography. J. Assoc. Off. Anal. Chem. 58, 725-733.
    • (1975) J. Assoc. Off. Anal. Chem. , vol.58 , pp. 725-733
    • Grimmer, G.1    Bohnke, H.2
  • 31
    • 0021934195 scopus 로고
    • Soluble and particulate forms of rat catechol-O-methyltransferase dis-tinguishedbygel electrophoresis and immune fixation
    • Grossman, M. H., Creveling, C. R., Rybczynski, R., Braverman, M., Iser-sky, C., and Breakefield, X. O. (1985). Soluble and particulate forms of rat catechol-O-methyltransferase dis-tinguishedbygel electrophoresis and immune fixation. J. Neurochem. 44, 421-432.
    • (1985) J. Neurochem. , vol.44 , pp. 421-432
    • Grossman, M.H.1    Creveling, C.R.2    Rybczynski, R.3    Braverman, M.4    Iser-sky, C.5    Breakefield, X.O.6
  • 32
    • 0026518652 scopus 로고
    • Chromosomal mapping of the human catechol-O-methyltransferase geneto22q11.1-q11. 2
    • Grossman, M. H., Emanuel, B. S., and Budarf, M. L. (1992). Chromosomal mapping of the human catechol-O-methyltransferase geneto22q11.1-q11.2. Genomics 12, 822-825.
    • (1992) Genomics , vol.12 , pp. 822-825
    • Grossman, M.H.1    Emanuel, B.S.2    Budarf, M.L.3
  • 33
    • 0037819284 scopus 로고    scopus 로고
    • Phar-macogenomics of human UDP-glucuronosyltransferase enzymes
    • Guillemette, C. (2003). Phar-macogenomics of human UDP-glucuronosyltransferase enzymes. Pharmacogenomics J. 3, 136-158.
    • (2003) Pharmacogenomics J , vol.3 , pp. 136-158
    • Guillemette, C.1
  • 34
    • 60549085049 scopus 로고    scopus 로고
    • Effects of tobacco smoke on gene expression and cellular pathways in a cellular model of oral leukoplakia
    • Gumus, Z. H., Du, B., Kacker, A., Boyle, J. O., Bocker, J. M., Mukherjee, P., et al. (2008). Effects of tobacco smoke on gene expression and cellular pathways in a cellular model of oral leukoplakia. Cancer Prev. Res. (Phila.) 1, 100-111.
    • (2008) Cancer Prev. Res. (Phila.) , vol.1 , pp. 100-111
    • Gumus, Z.H.1    Du, B.2    Kacker, A.3    Boyle, J.O.4    Bocker, J.M.5    Mukherjee, P.6
  • 35
    • 0030034858 scopus 로고    scopus 로고
    • Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells
    • Hara, A., Matsuura, K., Tamada, Y., Sato, K., Miyabe, Y., Deyashiki, Y., et al. (1996). Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells. Biochem. J. 313(PART 2), 373-376.
    • (1996) Biochem. J. , vol.313 , Issue.PART 2 , pp. 373-376
    • Hara, A.1    Matsuura, K.2    Tamada, Y.3    Sato, K.4    Miyabe, Y.5    Deyashiki, Y.6
  • 37
    • 84870685626 scopus 로고    scopus 로고
    • Identification of covalent benzo[a]pyrene-7, 8-dione-DNA adducts in human lung cells
    • Huang, M., Blair, I. A., and Penning, T. M. (2012a). Identification of covalent benzo[a]pyrene-7, 8-dione-DNA adducts in human lung cells. Toxicologist 126, 580.
    • (2012) Toxicologist , vol.126 , pp. 580
    • Huang, M.1    Blair, I.A.2    Penning, T.M.3
  • 38
    • 84861325318 scopus 로고    scopus 로고
    • Metabolism and disposition of benzo[a]pyrene-7, 8-dione (B[a]P-7, 8-dione) in human lung cells by liquid chromatog-raphy tandem mass spectrometry: detection of adenine B[a]P-7, 8-dione adduct
    • Huang, M., Liu, X., Basu, S., Zhang, L., Kushman, M., Harvey, R. G., et al. (2012b). Metabolism and disposition of benzo[a]pyrene-7, 8-dione (B[a]P-7, 8-dione) in human lung cells by liquid chromatog-raphy tandem mass spectrometry: detection of adenine B[a]P-7, 8-dione adduct. Chem. Res. Toxicol. 25, 993-1003.
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 993-1003
    • Huang, M.1    Liu, X.2    Basu, S.3    Zhang, L.4    Kushman, M.5    Harvey, R.G.6
  • 39
    • 41849104724 scopus 로고    scopus 로고
    • On the sulfation and methylation of catecholestrogens in human mammary epithelial cells and breast cancer cells
    • Hui, Y., Yasuda, S., Liu, M. Y., Wu, Y. Y., and Liu, M. C. (2008). On the sulfation and methylation of catecholestrogens in human mammary epithelial cells and breast cancer cells. Biol. Pharm. Bull. 31, 769-773.
    • (2008) Biol. Pharm. Bull. , vol.31 , pp. 769-773
    • Hui, Y.1    Yasuda, S.2    Liu, M.Y.3    Wu, Y.Y.4    Liu, M.C.5
  • 40
    • 0023724493 scopus 로고
    • Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreduc-tase. cDNA sequence and localization of gene to chromosome 16
    • Jaiswal, A. K., Mcbride, O. W., Adesnik, M., and Nebert, D. W. (1988). Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreduc-tase. cDNA sequence and localization of gene to chromosome 16. J. Biol. Chem. 263, 13572-13578.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13572-13578
    • Jaiswal, A.K.1    Mcbride, O.W.2    Adesnik, M.3    Nebert, D.W.4
  • 41
    • 0026331348 scopus 로고
    • Polycyclic aromatic hydrocarbon quinone-mediated oxidation reduction cycling catalyzed by a human placental NADPH-linked carbonyl reduc-tase
    • Jarabak, J. (1991). Polycyclic aromatic hydrocarbon quinone-mediated oxidation reduction cycling catalyzed by a human placental NADPH-linked carbonyl reduc-tase. Arch. Biochem. Biophys. 291, 334-338.
    • (1991) Arch. Biochem. Biophys. , vol.291 , pp. 334-338
    • Jarabak, J.1
  • 42
    • 0026558612 scopus 로고
    • Polycyclic aromatic hydrocarbon quinones may be either substrates for or irreversible inhibitors of the human placental NAD-linked 15-hydroxyprostaglandin dehydro-genase
    • Jarabak, J. (1992). Polycyclic aromatic hydrocarbon quinones may be either substrates for or irreversible inhibitors of the human placental NAD-linked 15-hydroxyprostaglandin dehydro-genase. Arch. Biochem. Biophys. 292, 239-243.
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 239-243
    • Jarabak, J.1
  • 43
    • 0021341783 scopus 로고
    • Characterization of membrane-bound and soluble catechol-O-methyltransferase from human frontal cortex
    • Jeffery, D. R., and Roth, J. A. (1984). Characterization of membrane-bound and soluble catechol-O-methyltransferase from human frontal cortex. J. Neurochem. 42, 826-832.
    • (1984) J. Neurochem. , vol.42 , pp. 826-832
    • Jeffery, D.R.1    Roth, J.A.2
  • 44
    • 0030876351 scopus 로고    scopus 로고
    • A new nomenclature for the aldo-keto reductase superfamily
    • Jez, J. M., Flynn, T. G., and Penning, T. M. (1997). A new nomenclature for the aldo-keto reductase superfamily. Biochem. Pharmacol. 54, 639-647.
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 639-647
    • Jez, J.M.1    Flynn, T.G.2    Penning, T.M.3
  • 45
    • 31844444754 scopus 로고    scopus 로고
    • Competing roles of aldo-keto reductase 1A1 and cytochrome P4501B1 in benzo[a]pyrene-7, 8-diol activation in human bronchoalveolar H358 cells: role of AKRs in P4501B1 induction
    • Jiang, H., Vudathala, D. K., Blair, I. A., and Penning, T. M. (2006). Competing roles of aldo-keto reductase 1A1 and cytochrome P4501B1 in benzo[a]pyrene-7, 8-diol activation in human bronchoalveolar H358 cells: role of AKRs in P4501B1 induction. Chem. Res. Toxicol. 19, 68-78.
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 68-78
    • Jiang, H.1    Vudathala, D.K.2    Blair, I.A.3    Penning, T.M.4
  • 46
    • 33847021147 scopus 로고    scopus 로고
    • Aldo-keto reductases and bioactiva-tion/detoxication
    • Jin, Y., and Penning, T. M. (2007). Aldo-keto reductases and bioactiva-tion/detoxication. Annu. Rev. Pharmacol. Toxicol. 47, 263-292.
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 263-292
    • Jin, Y.1    Penning, T.M.2
  • 47
    • 0022809670 scopus 로고
    • Formation of 8-hydroxyguanine moiety in cellular DNAbyagents producing oxygen radicals and evidence for its repair
    • Kasai, H., Crain, P. F., Kuchino, Y., Nishimura, S., Ootsuyama, A., and Tanooka, H. (1986). Formation of 8-hydroxyguanine moiety in cellular DNAbyagents producing oxygen radicals and evidence for its repair. Carcinogenesis 7, 1849-1851.
    • (1986) Carcinogenesis , vol.7 , pp. 1849-1851
    • Kasai, H.1    Crain, P.F.2    Kuchino, Y.3    Nishimura, S.4    Ootsuyama, A.5    Tanooka, H.6
  • 48
    • 0026451998 scopus 로고
    • Nature of cytochromes P450 involved in the 2-/4-hydroxylations of estradiol in human liver microsomes
    • Kerlan, V., Dreano, Y., Bercovici, J. P., Beaune, P. H., Floch, H. H., and Berthou, F. (1992). Nature of cytochromes P450 involved in the 2-/4-hydroxylations of estradiol in human liver microsomes. Biochem. Pharmacol. 44, 1745-1756.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 1745-1756
    • Kerlan, V.1    Dreano, Y.2    Bercovici, J.P.3    Beaune, P.H.4    Floch, H.H.5    Berthou, F.6
  • 50
    • 0028946316 scopus 로고
    • Demonstration that polyol accumulation is responsible for diabetic cataract by the use of trans-genic mice expressing the aldose reductase gene in the lens
    • Lee, A. Y., Chung, S. K., and Chung, S. S. (1995). Demonstration that polyol accumulation is responsible for diabetic cataract by the use of trans-genic mice expressing the aldose reductase gene in the lens. Proc. Natl. Acad. Sci. U.S.A. 92, 2780-2784.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 2780-2784
    • Lee, A.Y.1    Chung, S.K.2    Chung, S.S.3
  • 51
    • 0141645554 scopus 로고    scopus 로고
    • Mutations in SRD5B1 (AKR1D1), the gene encoding delta(4)-3-oxosteroid 5β-reductase, in hepatitis and liver failure in infancy
    • Lemonde, H.A., Custard, E. J., Bouquet, J., Duran, M., Overmars, H., Scambler, P. J., et al. (2003). Mutations in SRD5B1 (AKR1D1), the gene encoding delta(4)-3-oxosteroid 5β-reductase, in hepatitis and liver failure in infancy. Gut 52, 1494-1499.
    • (2003) Gut , vol.52 , pp. 1494-1499
    • Lemonde, H.A.1    Custard, E.J.2    Bouquet, J.3    Duran, M.4    Overmars, H.5    Scambler, P.J.6
  • 52
    • 0022972683 scopus 로고
    • Cytochrome P-450-mediated redox cycling of estrogens
    • Liehr, J. G., Ulubelen, A. A., and Strobel, H. W. (1986). Cytochrome P-450-mediated redox cycling of estrogens. J. Biol. Chem. 261, 16865-16870.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16865-16870
    • Liehr, J.G.1    Ulubelen, A.A.2    Strobel, H.W.3
  • 53
    • 84863136847 scopus 로고    scopus 로고
    • Epidermal growth factor induces tumour marker AKR1B10 expression through activator protein-1 signalling in hepatocellular carcinoma cells
    • Liu, Z., Yan, R., Al-Salman, A., Shen, Y., Bu, Y., Ma, J., et al. (2012). Epidermal growth factor induces tumour marker AKR1B10 expression through activator protein-1 signalling in hepatocellular carcinoma cells. Biochem. J. 442, 273-282.
    • (2012) Biochem. J. , vol.442 , pp. 273-282
    • Liu, Z.1    Yan, R.2    Al-Salman, A.3    Shen, Y.4    Bu, Y.5    Ma, J.6
  • 54
    • 43049120291 scopus 로고    scopus 로고
    • Effects of methylated chrysenes on AhR-dependent and -independent toxic events in rat liver epithelial cells
    • Machala, M., Svihalkova-Sindlerova, L., Pencikova, K., Krcmar, P., Topinka, J., Milcova, A., et al. (2008). Effects of methylated chrysenes on AhR-dependent and -independent toxic events in rat liver epithelial cells. Toxicology 247, 93-101.
    • (2008) Toxicology , vol.247 , pp. 93-101
    • Machala, M.1    Svihalkova-Sindlerova, L.2    Pencikova, K.3    Krcmar, P.4    Topinka, J.5    Milcova, A.6
  • 56
    • 0038287034 scopus 로고    scopus 로고
    • CatecholO-methyltransferase (COMT): biochemistry, molecular biology, pharmacology, and clinical efficacy of the new selective COMT inhibitors
    • Mannisto, P. T., and Kaakkola, S. (1999). CatecholO-methyltransferase (COMT): biochemistry, molecular biology, pharmacology, and clinical efficacy of the new selective COMT inhibitors. Pharmacol Rev. 51, 593-628.
    • (1999) Pharmacol Rev , vol.51 , pp. 593-628
    • Mannisto, P.T.1    Kaakkola, S.2
  • 57
    • 0027167145 scopus 로고
    • P450 enzymes of estrogen metabolism
    • Martucci, C. P., and Fishman, J. (1993). P450 enzymes of estrogen metabolism. Pharmacol Ther. 57, 237-257.
    • (1993) Pharmacol Ther , vol.57 , pp. 237-257
    • Martucci, C.P.1    Fishman, J.2
  • 58
    • 0033024560 scopus 로고    scopus 로고
    • Synthesis and characterization of polycyclic aromatic hydrocarbon o-quinone depurinating N7-guanine adducts
    • McCoull, K. D., Rindgen, D., Blair, I. A., and Penning, T. M. (1999). Synthesis and characterization of polycyclic aromatic hydrocarbon o-quinone depurinating N7-guanine adducts. Chem. Res. Toxicol 12, 237-246.
    • (1999) Chem. Res. Toxicol , vol.12 , pp. 237-246
    • McCoull, K.D.1    Rindgen, D.2    Blair, I.A.3    Penning, T.M.4
  • 59
    • 33947104150 scopus 로고    scopus 로고
    • Metabolic enzyme induction by HepG2 cells exposed to oxygenated and nonoxygenated polycyclic aromatic hydrocarbons
    • Misaki, K., Matsui, S., and Matsuda, T. (2007). Metabolic enzyme induction by HepG2 cells exposed to oxygenated and nonoxygenated polycyclic aromatic hydrocarbons. Chem. Res. Toxicol 20, 277-283.
    • (2007) Chem. Res. Toxicol , vol.20 , pp. 277-283
    • Misaki, K.1    Matsui, S.2    Matsuda, T.3
  • 60
    • 0031446380 scopus 로고    scopus 로고
    • Biological reactivity of polyphenolic-glutathione conjugates
    • Monks, T. J., and Lau, S. S. (1997). Biological reactivity of polyphenolic-glutathione conjugates. Chem. Res. Toxicol 10, 1296-1313.
    • (1997) Chem. Res. Toxicol , vol.10 , pp. 1296-1313
    • Monks, T.J.1    Lau, S.S.2
  • 61
    • 0026856194 scopus 로고
    • Characterization of mercapturic acid and glutathionyl conjugates of benzo[a]pyrene-7, 8-dione by two-dimensional NMR
    • Murty, V. S., and Penning, T.M. (1992a). Characterization of mercapturic acid and glutathionyl conjugates of benzo[a]pyrene-7, 8-dione by two-dimensional NMR. Bioconjug. Chem. 3, 218-224.
    • (1992) Bioconjug. Chem. , vol.3 , pp. 218-224
    • Murty, V.S.1    Penning, T.M.2
  • 62
    • 0026727562 scopus 로고
    • Polycyclic aromatic hydrocarbon (PAH) ortho-quinone conjugate chemistry: kinetics of thiol addition to PAH ortho-quinones and structures of thioether adducts of naphthalene-1, 2-dione
    • Murty, V. S., and Penning, T. M. (1992b). Polycyclic aromatic hydrocarbon (PAH) ortho-quinone conjugate chemistry: kinetics of thiol addition to PAH ortho-quinones and structures of thioether adducts of naphthalene-1, 2-dione. Chem. Biol Interact. 84, 169-188.
    • (1992) Chem. Biol Interact. , vol.84 , pp. 169-188
    • Murty, V.S.1    Penning, T.M.2
  • 63
    • 33745177369 scopus 로고    scopus 로고
    • Sulfotransferase (SULT) 1A1 polymorphic variants *1, *2, and *3 are associated with altered enzymatic activity, cellular pheno-type, and protein degradation
    • Nagar, S., Walther, S., and Blanchard, R. L. (2006). Sulfotransferase (SULT) 1A1 polymorphic variants *1, *2, and *3 are associated with altered enzymatic activity, cellular pheno-type, and protein degradation. Mol Pharmacol 69, 2084-2092.
    • (2006) Mol Pharmacol , vol.69 , pp. 2084-2092
    • Nagar, S.1    Walther, S.2    Blanchard, R.L.3
  • 65
    • 80052989461 scopus 로고    scopus 로고
    • Characterization of dibenzo[a, l]pyrene-t rans-11, 12diol (dibenzo[def, p]chrysene) glucuronidation by UDPglucuronosyltransferases
    • Olson, K. C., Sun, D., Chen, G., Sharma, A. K., Amin, S., Ropson, I. J., et al. (2011). Characterization of dibenzo[a, l]pyrene-t rans-11, 12diol (dibenzo[def, p]chrysene) glucuronidation by UDPglucuronosyltransferases. Chem. Res. Toxicol. 24, 1549-1559.
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 1549-1559
    • Olson, K.C.1    Sun, D.2    Chen, G.3    Sharma, A.K.4    Amin, S.5    Ropson, I.J.6
  • 66
    • 0035845684 scopus 로고    scopus 로고
    • The ubiquitous aldehyde reductase (AKR1A1) oxidizes proximate carcinogen trans-dihydrodiols to o-quinones: potential role in poly-cyclic aromatic hydrocarbon activation
    • Palackal, N. T., Burczynski, M. E., Har-vey, R.G., and Penning, T.M.(2001). The ubiquitous aldehyde reductase (AKR1A1) oxidizes proximate carcinogen trans-dihydrodiols to o-quinones: potential role in poly-cyclic aromatic hydrocarbon activation. Biochemistry 40, 10901-10910.
    • (2001) Biochemistry , vol.40 , pp. 10901-10910
    • Palackal, N.T.1    Burczynski, M.E.2    Har-vey, R.G.3    Penning, T.M.4
  • 67
    • 0037025386 scopus 로고    scopus 로고
    • Activation of polycyclic aromatic hydrocarbon trans-dihydrodiol proximate car-cinogensbyhuman aldo-keto reduc-tase (AKR1C) enzymes and their functional overexpression in human lung carcinoma (A549) cells
    • Palackal, N. T., Lee, S. H., Harvey, R. G., Blair, I. A., and Penning, T. M. (2002). Activation of polycyclic aromatic hydrocarbon trans-dihydrodiol proximate car-cinogensbyhuman aldo-keto reduc-tase (AKR1C) enzymes and their functional overexpression in human lung carcinoma (A549) cells. J. Biol. Chem. 277, 24799-24808.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24799-24808
    • Palackal, N.T.1    Lee, S.H.2    Harvey, R.G.3    Blair, I.A.4    Penning, T.M.5
  • 68
    • 44349169635 scopus 로고    scopus 로고
    • Evidence for the aldo-keto reductase pathway of polycyclic aromatic trans-dihydrodiol activation in human lung A549 cells
    • Park, J. H., Mangal, D., Tacka, K. A., Quinn, A. M., Harvey, R. G., Blair, I. A., et al. (2008). Evidence for the aldo-keto reductase pathway of polycyclic aromatic trans-dihydrodiol activation in human lung A549 cells. Proc. Natl. Acad. Sci. U.S.A. 105, 6846-6851.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6846-6851
    • Park, J.H.1    Mangal, D.2    Tacka, K.A.3    Quinn, A.M.4    Harvey, R.G.5    Blair, I.A.6
  • 69
    • 33744503917 scopus 로고    scopus 로고
    • Poly-cyclic aromatic hydrocarbon (PAH) o-quinones produced by the aldo-keto-reductases (AKRs) generate abasic sites, oxidized pyrimidines, and 8-oxo-dGuo via reactive oxygen species
    • Park, J. H., Troxel, A. B., Harvey, R. G., and Penning, T. M. (2006). Poly-cyclic aromatic hydrocarbon (PAH) o-quinones produced by the aldo-keto-reductases (AKRs) generate abasic sites, oxidized pyrimidines, and 8-oxo-dGuo via reactive oxygen species. Chem. Res. Toxicol. 19, 719-728.
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 719-728
    • Park, J.H.1    Troxel, A.B.2    Harvey, R.G.3    Penning, T.M.4
  • 70
    • 1342346696 scopus 로고    scopus 로고
    • Aldo-keto reduc-tases and formation of polycyclic aromatic hydrocarbon o-quinones
    • Penning, T.M. (2004). Aldo-keto reduc-tases and formation of polycyclic aromatic hydrocarbon o-quinones. Meth. Enzymol. 378, 31-67.
    • (2004) Meth. Enzymol. , vol.378 , pp. 31-67
    • Penning, T.M.1
  • 71
    • 0032937593 scopus 로고    scopus 로고
    • Dihy-drodiol dehydrogenases and poly-cyclic aromatic hydrocarbon activation: generation of reactive and redox active o-quinones
    • Penning, T.M., Burczynski, M.E., Hung, C. F., Mccoull, K. D., Palackal, N. T., and Tsuruda, L. S. (1999). Dihy-drodiol dehydrogenases and poly-cyclic aromatic hydrocarbon activation: generation of reactive and redox active o-quinones. Chem. Res. Toxicol. 12, 1-18.
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 1-18
    • Penning, T.M.1    Burczynski, M.E.2    Hung, C.F.3    Mccoull, K.D.4    Palackal, N.T.5    Tsuruda, L.S.6
  • 72
    • 0034287545 scopus 로고    scopus 로고
    • Human 3α-hydroxysteroid dehydrogenase iso-forms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inac-tivation and formation of male and female sex hormones
    • Penning, T. M., Burczynski, M. E., Jez, J. M., Hung, C. F., Lin, H. K., Ma, H., et al. (2000). Human 3α-hydroxysteroid dehydrogenase iso-forms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inac-tivation and formation of male and female sex hormones. Biochem. J. 351, 67-77.
    • (2000) Biochem. J. , vol.351 , pp. 67-77
    • Penning, T.M.1    Burczynski, M.E.2    Jez, J.M.3    Hung, C.F.4    Lin, H.K.5    Ma, H.6
  • 73
    • 61649103983 scopus 로고    scopus 로고
    • Steroid hormonetransforming aldo-keto reductases and cancer
    • Penning, T.M., and Byrns, M.C. (2009). Steroid hormonetransforming aldo-keto reductases and cancer. Ann. N. Y. Acad. Sci. 1155, 33-42.
    • (2009) Ann. N. Y. Acad. Sci. , vol.1155 , pp. 33-42
    • Penning, T.M.1    Byrns, M.C.2
  • 74
    • 59049105837 scopus 로고    scopus 로고
    • Genomics of smoking exposure and cessation: lessons for cancer prevention and treatment
    • Penning, T. M., and Lerman, C. (2008). Genomics of smoking exposure and cessation: lessons for cancer prevention and treatment. Cancer Prev. Res. (Phila.) 1, 80-83.
    • (2008) Cancer Prev. Res. (Phila.) , vol.1 , pp. 80-83
    • Penning, T.M.1    Lerman, C.2
  • 75
    • 13544273915 scopus 로고    scopus 로고
    • Regulation of progesterone levels during pregnancy and parturition by signal transducer and activator of transcription 5 and 20α-hydroxysteroid dehydrogenase
    • Piekorz, R. P., Gingras, S., Hoffmeyer, A., Ihle, J. N., and Weinstein, Y. (2005). Regulation of progesterone levels during pregnancy and parturition by signal transducer and activator of transcription 5 and 20α-hydroxysteroid dehydrogenase. Mol. Endocrinol. 19, 431-440.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 431-440
    • Piekorz, R.P.1    Gingras, S.2    Hoffmeyer, A.3    Ihle, J.N.4    Weinstein, Y.5
  • 76
    • 57449083407 scopus 로고    scopus 로고
    • Oxidation of PAH trans-dihydrodiols by human aldo-keto reductase AKR1B10
    • Quinn, A. M., Harvey, R. G., and Penning, T. M. (2008). Oxidation of PAH trans-dihydrodiols by human aldo-keto reductase AKR1B10. Chem. Res. Toxicol. 21, 2207-2215.
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 2207-2215
    • Quinn, A.M.1    Harvey, R.G.2    Penning, T.M.3
  • 77
    • 47549097394 scopus 로고    scopus 로고
    • Comparisons of (±)-benzo[a]pyrene-trans-7, 8-dihydrodiol activation by human cytochrome P450 and aldo-keto reductase enzymes: effect of redox state and expression levels
    • Quinn, A. M., and Penning, T. M. (2008). Comparisons of (±)-benzo[a]pyrene-trans-7, 8-dihydrodiol activation by human cytochrome P450 and aldo-keto reductase enzymes: effect of redox state and expression levels. Chem. Res. Toxicol. 21, 1086-1094.
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 1086-1094
    • Quinn, A.M.1    Penning, T.M.2
  • 78
    • 0033567437 scopus 로고    scopus 로고
    • Human phenol sulfotransferases SULT1A2 and SULT1A1: genetic polymorphisms, allozyme properties, and human liver genotype-phenotype correlations
    • Raftogianis, R. B., Wood, T. C., and Weinshilboum, R. M. (1999). Human phenol sulfotransferases SULT1A2 and SULT1A1: genetic polymorphisms, allozyme properties, and human liver genotype-phenotype correlations. Biochem. Pharmacol. 58, 605-616.
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 605-616
    • Raftogianis, R.B.1    Wood, T.C.2    Weinshilboum, R.M.3
  • 79
    • 0021352552 scopus 로고
    • Antie-strogen action of 2-hydroxyestrone on MCF-7 human breast cancer cells
    • Schneider, J., Huh, M. M., Bradlow, H. L., and Fishman, J. (1984). Antie-strogen action of 2-hydroxyestrone on MCF-7 human breast cancer cells. J. Biol. Chem. 259, 4840-4845.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4840-4845
    • Schneider, J.1    Huh, M.M.2    Bradlow, H.L.3    Fishman, J.4
  • 80
    • 33845257339 scopus 로고    scopus 로고
    • Comparison of p53 mutations induced by PAH o-quinones with those caused by anti-benzo[a]pyrene diol epoxide in vitro: role of reactive oxygen and biological selection
    • Shen, Y. M., Troxel, A. B., Vedan-tam, S., Penning, T. M., and Field, J. (2006). Comparison of p53 mutations induced by PAH o-quinones with those caused by anti-benzo[a]pyrene diol epoxide in vitro: role of reactive oxygen and biological selection. Chem. Res. Tox-icol. 19, 1441-1450.
    • (2006) Chem. Res. Tox-icol. , vol.19 , pp. 1441-1450
    • Shen, Y.M.1    Troxel, A.B.2    Vedan-tam, S.3    Penning, T.M.4    Field, J.5
  • 81
    • 0027281455 scopus 로고
    • Reactivity of benzo[a]pyrene-7, 8-dione with DNA. Evidence for the formation of deoxyguanosine adducts
    • Shou, M., Harvey, R. G., and Penning, T. M. (1993). Reactivity of benzo[a]pyrene-7, 8-dione with DNA. Evidence for the formation of deoxyguanosine adducts. Carcino-genesis 14, 475-482.
    • (1993) Carcino-genesis , vol.14 , pp. 475-482
    • Shou, M.1    Harvey, R.G.2    Penning, T.M.3
  • 82
    • 0031418653 scopus 로고    scopus 로고
    • Role of human hepatic cytochrome P450 1A2 and 3A4 in the metabolic activation of estrone
    • Shou, M., Korzekwa, K. R., Brooks, E. N., Krausz, K. W., Gonzalez, F. J., and Gelboin, H. V. (1997). Role of human hepatic cytochrome P450 1A2 and 3A4 in the metabolic activation of estrone. Carcinogenesis 18, 207-214.
    • (1997) Carcinogenesis , vol.18 , pp. 207-214
    • Shou, M.1    Korzekwa, K.R.2    Brooks, E.N.3    Krausz, K.W.4    Gonzalez, F.J.5    Gelboin, H.V.6
  • 83
    • 41849093368 scopus 로고    scopus 로고
    • Fjord-region benzo[g]chrysene11, 12-dihydrodiol and benzo[c]phenanthrene-3, 4 dihydrodiol as substrates for rat liver dihydrodiol dehydrogenase (AKR1C9): structural basis for stereochemical preference
    • Shultz, C. A., Palackal, N. T., Man-gal, D., Harvey, R. G., Blair, I. A., and Penning, T. M. (2008). Fjord-region benzo[g]chrysene11, 12-dihydrodiol and benzo[c]phenanthrene-3, 4 dihydrodiol as substrates for rat liver dihydrodiol dehydrogenase (AKR1C9): structural basis for stereochemical preference. Chem. Res. Toxicol. 21, 668-677.
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 668-677
    • Shultz, C.A.1    Palackal, N.T.2    Man-gal, D.3    Harvey, R.G.4    Blair, I.A.5    Penning, T.M.6
  • 84
    • 84055223064 scopus 로고    scopus 로고
    • Specificity of human aldo-keto reductases, NAD(P)H:quinone oxidoreduc-tase, and carbonyl reductases to redox-cycle polycyclic aromatic hydrocarbon diones and 4-Hydroxyequilenin-o-quinone
    • Shultz, C. A., Quinn, A. M., Park, J. H., Harvey, R. G., Bolton, J. L., Maser, E., et al. (2011). Specificity of human aldo-keto reductases, NAD(P)H:quinone oxidoreduc-tase, and carbonyl reductases to redox-cycle polycyclic aromatic hydrocarbon diones and 4-Hydroxyequilenin-o-quinone. Chem. Res. Toxicol. 24, 2153-2166.
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 2153-2166
    • Shultz, C.A.1    Quinn, A.M.2    Park, J.H.3    Harvey, R.G.4    Bolton, J.L.5    Maser, E.6
  • 85
    • 0022974550 scopus 로고
    • Regioand stereospecificity of homogeneous 3α-hydroxysteroid-dihydrodiol dehydrogenase for trans-dihydrodiol metabolites of polycyclic aromatic hydrocarbons
    • Smithgall, T. E., Harvey, R. G., and Penning, T. M. (1986). Regioand stereospecificity of homogeneous 3α-hydroxysteroid-dihydrodiol dehydrogenase for trans-dihydrodiol metabolites of polycyclic aromatic hydrocarbons. J. Biol. Chem. 261, 6184-6191.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6184-6191
    • Smithgall, T.E.1    Harvey, R.G.2    Penning, T.M.3
  • 86
    • 0023907050 scopus 로고
    • Spec-troscopic identification of ortho-quinones as the products of poly-cyclic aromatic trans-dihydrodiol oxidation catalyzed by dihydro-diol dehydrogenase. A potential route of proximate carcinogen metabolism
    • Smithgall, T. E., Harvey, R. G., and Penning, T. M. (1988). Spec-troscopic identification of ortho-quinones as the products of poly-cyclic aromatic trans-dihydrodiol oxidation catalyzed by dihydro-diol dehydrogenase. A potential route of proximate carcinogen metabolism. J. Biol. Chem. 263, 1814-1820.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1814-1820
    • Smithgall, T.E.1    Harvey, R.G.2    Penning, T.M.3
  • 87
    • 0029680465 scopus 로고    scopus 로고
    • Molecular characteristics of catechol estrogen quinones in reactions with deoxyribonu-cleosides
    • Stack, D. E., Byun, J., Gross, M. L., Rogan, E. G., and Cavalieri, E. L. (1996). Molecular characteristics of catechol estrogen quinones in reactions with deoxyribonu-cleosides. Chem. Res. Toxicol. 9, 851-859.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 851-859
    • Stack, D.E.1    Byun, J.2    Gross, M.L.3    Rogan, E.G.4    Cavalieri, E.L.5
  • 88
    • 0042309876 scopus 로고    scopus 로고
    • Recent studies of aldose reductase enzyme inhibition for diabetic complications
    • Suzen, S., and Buyukbingol, E. (2003). Recent studies of aldose reductase enzyme inhibition for diabetic complications. Curr. Med. Chem. 10, 1329-1352.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1329-1352
    • Suzen, S.1    Buyukbingol, E.2
  • 89
    • 0030904954 scopus 로고    scopus 로고
    • Genetic polymorphism of catechol-Omethyltransferase (COMT): correlation of genotype with individual variation of S-COMT activity and comparison of the allele frequencies in the normal population and parkinsonian patients in Finland
    • Syvanen, A. C., Tilgmann, C., Rinne, J., and Ulmanen, I. (1997). Genetic polymorphism of catechol-Omethyltransferase (COMT): correlation of genotype with individual variation of S-COMT activity and comparison of the allele frequencies in the normal population and parkinsonian patients in Finland. Pharmacogenetics 7, 65-71.
    • (1997) Pharmacogenetics , vol.7 , pp. 65-71
    • Syvanen, A.C.1    Tilgmann, C.2    Rinne, J.3    Ulmanen, I.4
  • 90
    • 65549117476 scopus 로고    scopus 로고
    • Aldose reduc-tase deficiency in mice prevents azoxymethane-induced colonic pre-neoplastic aberrant crypt foci formation
    • Tammali, R., Reddy, A. B., Ramana, K. V., Petrash, J. M., and Srivas-tava, S. K. (2009). Aldose reduc-tase deficiency in mice prevents azoxymethane-induced colonic pre-neoplastic aberrant crypt foci formation. Carcinogenesis 30, 799-807.
    • (2009) Carcinogenesis , vol.30 , pp. 799-807
    • Tammali, R.1    Reddy, A.B.2    Ramana, K.V.3    Petrash, J.M.4    Srivas-tava, S.K.5
  • 91
    • 0042858525 scopus 로고    scopus 로고
    • Conjugation of catechols by recombi-nant human sulfotransferases, UDP-glucuronosyltransferases, and soluble catechol O-methyltransferase: structure-conjugation relationships and predictive models
    • Taskinen, J., Ethell, B. T., Pihlavisto, P., Hood, A. M., Burchell, B., and Coughtrie, M. W. (2003). Conjugation of catechols by recombi-nant human sulfotransferases, UDP-glucuronosyltransferases, and soluble catechol O-methyltransferase: structure-conjugation relationships and predictive models. Drug Metab. Dispos. 31, 1187-1197.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 1187-1197
    • Taskinen, J.1    Ethell, B.T.2    Pihlavisto, P.3    Hood, A.M.4    Burchell, B.5    Coughtrie, M.W.6
  • 92
    • 0027964721 scopus 로고
    • Genomic organization of the human cate-chol O-methyltransferase gene and its expression from two distinct promoters
    • Tenhunen, J., Salminen, M., Lundstrom, K., Kiviluoto, T., Savolainen, R., and Ulmanen, I. (1994). Genomic organization of the human cate-chol O-methyltransferase gene and its expression from two distinct promoters. Eur. J. Biochem. 223, 1049-1059.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 1049-1059
    • Tenhunen, J.1    Salminen, M.2    Lundstrom, K.3    Kiviluoto, T.4    Savolainen, R.5    Ulmanen, I.6
  • 93
    • 0027717355 scopus 로고
    • Production of rat soluble and membrane-bound catechol O-methyltransferase forms from bifunctional mRNAs
    • Tenhunen, J., and Ulmanen, I. (1993). Production of rat soluble and membrane-bound catechol O-methyltransferase forms from bifunctional mRNAs. Biochem. J. 296(Pt 3), 595-600.
    • (1993) Biochem. J. , vol.296 , Issue.PART 3 , pp. 595-600
    • Tenhunen, J.1    Ulmanen, I.2
  • 94
    • 0034128936 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: metabolism, expression, and disease
    • Tukey, R. H., and Strassburg, C. P. (2000). Human UDP-glucuronosyltransferases: metabolism, expression, and disease. Annu. Rev. Pharmacol. Toxicol. 40, 581-616.
    • (2000) Annu. Rev. Pharmacol. Toxicol. , vol.40 , pp. 581-616
    • Tukey, R.H.1    Strassburg, C.P.2
  • 95
    • 0026316817 scopus 로고
    • Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro
    • Ulmanen, I., and Lundstrom, K. (1991). Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro. Eur. J. Biochem. 202, 1013-1020.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1013-1020
    • Ulmanen, I.1    Lundstrom, K.2
  • 96
    • 74549165963 scopus 로고    scopus 로고
    • Lack of functional and expression homology between human and mouse aldo-keto reductase 1C enzymes: implications for modelling human cancers
    • Velica, P., Davies, N. J., Rocha, P. P., Schrewe, H., Ride, J. P., and Bunce, C. M. (2009). Lack of functional and expression homology between human and mouse aldo-keto reductase 1C enzymes: implications for modelling human cancers. Mol. Cancer 8, 121.
    • (2009) Mol. Cancer , vol.8 , pp. 121
    • Velica, P.1    Davies, N.J.2    Rocha, P.P.3    Schrewe, H.4    Ride, J.P.5    Bunce, C.M.6
  • 97
    • 0036165473 scopus 로고    scopus 로고
    • Sulfotransferase (SULT) 1A1 polymorphism as a predisposition factor for lung cancer: a case-control analysis
    • Wang, Y., Spitz, M. R., Tsou, A. M., Zhang, K., Makan, N., and Wu, X. (2002). Sulfotransferase (SULT) 1A1 polymorphism as a predisposition factor for lung cancer: a case-control analysis. Lung Cancer 35, 137-142.
    • (2002) Lung Cancer , vol.35 , pp. 137-142
    • Wang, Y.1    Spitz, M.R.2    Tsou, A.M.3    Zhang, K.4    Makan, N.5    Wu, X.6
  • 98
    • 0019495032 scopus 로고
    • Purification and propertiesof anNADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase
    • Wermuth, B. (1981). Purification and propertiesof anNADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. 256, 1206-1213.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1206-1213
    • Wermuth, B.1
  • 99
    • 33749055937 scopus 로고    scopus 로고
    • Smoking and cancer-related gene expression in bronchial epithelium and non-small-cell lung cancers
    • Woenckhaus, M., Klein-Hitpass, L., Grepmeier, U., Merk, J., Pfeifer, M., Wild, P., et al. (2006). Smoking and cancer-related gene expression in bronchial epithelium and non-small-cell lung cancers. J. Pathol. 210, 192-204.
    • (2006) J. Pathol. , vol.210 , pp. 192-204
    • Woenckhaus, M.1    Klein-Hitpass, L.2    Grepmeier, U.3    Merk, J.4    Pfeifer, M.5    Wild, P.6
  • 100
    • 20444412643 scopus 로고    scopus 로고
    • Metabolic activation of polycyclic and heterocyclic aromatic hydrocarbons and DNA damage: a review
    • Xue, W., and Warshawsky, D. (2005). Metabolic activation of polycyclic and heterocyclic aromatic hydrocarbons and DNA damage: a review. Toxicol. Appl. Pharmacol. 206, 73-93.
    • (2005) Toxicol. Appl. Pharmacol. , vol.206 , pp. 73-93
    • Xue, W.1    Warshawsky, D.2
  • 101
    • 0035998283 scopus 로고    scopus 로고
    • Reactive oxygen species generated by PAH o-quinones cause change-in-function mutations in p53
    • Yu, D., Berlin, J. A., Penning, T. M., and Field, J. (2002). Reactive oxygen species generated by PAH o-quinones cause change-in-function mutations in p53. Chem. Res. Toxicol. 15, 832-842.
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 832-842
    • Yu, D.1    Berlin, J.A.2    Penning, T.M.3    Field, J.4
  • 102
    • 84865500021 scopus 로고    scopus 로고
    • Detoxication of benzo[a]pyrene-7, 8-dione by sul-fotransferases (SULTs) in human lung cells
    • Zhang, L., Huang, M., Blair, I. A., and Penning, T. M. (2012). Detoxication of benzo[a]pyrene-7, 8-dione by sul-fotransferases (SULTs) in human lung cells. J. Biol. Chem. 287, 29909-29920.
    • (2012) J. Biol. Chem. , vol.287 , pp. 29909-29920
    • Zhang, L.1    Huang, M.2    Blair, I.A.3    Penning, T.M.4
  • 103
    • 79960436551 scopus 로고    scopus 로고
    • Detoxication of structurally diverse polycyclic aromatic hydrocarbon (PAH) o-quinones by human recombi-nant catechol-O-methyltransferase (COMT) via O-methylation of PAH catechols
    • Zhang, L., Jin, Y., Chen, M., Huang, M., Harvey, R. G., Blair, I. A., et al. (2011). Detoxication of structurally diverse polycyclic aromatic hydrocarbon (PAH) o-quinones by human recombi-nant catechol-O-methyltransferase (COMT) via O-methylation of PAH catechols. J. Biol. Chem. 286, 25644-25654.
    • (2011) J. Biol. Chem. , vol.286 , pp. 25644-25654
    • Zhang, L.1    Jin, Y.2    Chen, M.3    Huang, M.4    Harvey, R.G.5    Blair, I.A.6
  • 104
    • 59049088289 scopus 로고    scopus 로고
    • Impact of smoking cessation on global gene expression in the bronchial epithelium of chronic smokers
    • Zhang, L., Lee, J. J., Tang, H., Fan, Y. H., Xiao, L., Ren, H., et al. (2008). Impact of smoking cessation on global gene expression in the bronchial epithelium of chronic smokers. Cancer Prev. Res. (Phila.) 1, 112-118.
    • (2008) Cancer Prev. Res. (Phila.) , vol.1 , pp. 112-118
    • Zhang, L.1    Lee, J.J.2    Tang, H.3    Fan, Y.H.4    Xiao, L.5    Ren, H.6
  • 105
    • 0035913673 scopus 로고    scopus 로고
    • Tobacco carcinogen-detoxifying enzyme UGT1A7 and its association with orolaryngeal cancer risk
    • Zheng, Z., Park, J. Y., Guillemette, C., Schantz, S. P., and Lazarus, P. (2001). Tobacco carcinogen-detoxifying enzyme UGT1A7 and its association with orolaryngeal cancer risk. J. Natl. Cancer Inst. 93, 1411-1418.
    • (2001) J. Natl. Cancer Inst. , vol.93 , pp. 1411-1418
    • Zheng, Z.1    Park, J.Y.2    Guillemette, C.3    Schantz, S.P.4    Lazarus, P.5
  • 106
    • 46949109025 scopus 로고    scopus 로고
    • A comprehensive analysis of phase I and phase II metabolism gene polymorphisms and risk of non-small cell lung cancer in smokers
    • Zienolddiny, S., Campa, D., Lind, H., Ryberg, D., Skaug, V., Stangeland, L. B., et al. (2008). A comprehensive analysis of phase I and phase II metabolism gene polymorphisms and risk of non-small cell lung cancer in smokers. Carcinogenesis 29, 1164-1169.
    • (2008) Carcinogenesis , vol.29 , pp. 1164-1169
    • Zienolddiny, S.1    Campa, D.2    Lind, H.3    Ryberg, D.4    Skaug, V.5    Stangeland, L.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.