메뉴 건너뛰기




Volumn 29, Issue 2, 2010, Pages 175-185

The binding affinity of carcinogenic N-nitrosodimethylamine and N-nitrosomethylaniline to cytochromes P450 2B4, 2E1 and 3A6 does not dictate the rate of their enzymatic N-demethylation

Author keywords

CYP2B4; CYP2E1; CYP3A6; Cytochrome P450; N nitrosamines

Indexed keywords

CARCINOGEN; CYTOCHROME P450; CYTOCHROME P450 2B4; CYTOCHROME P450 2E1; CYTOCHROME P450 3A6; DIMETHYLNITROSAMINE; N METHYL N NITROSOANILINE; UNCLASSIFIED DRUG; CYTOCHROME P-450 CYP2B4 (RABBIT); CYTOCHROME P-450 CYP3A6 (RABBIT); LIPOSOME; N-METHYL-N-NITROSOANILINE; NITROSAMINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; UNSPECIFIC MONOOXYGENASE;

EID: 77954123833     PISSN: 02315882     EISSN: None     Source Type: Journal    
DOI: 10.4149/gpb_2010_02_175     Document Type: Article
Times cited : (19)

References (64)
  • 1
    • 0023224629 scopus 로고
    • Toxic and carcinogenic agents in undiluted mainstream smoke and side stream smoke of different types of cigarettes
    • doi:10.1093/carcin/8.5.729
    • Adams J. D., O'Mara-Adams K. J., Hoffmann D. (1987): Toxic and carcinogenic agents in undiluted mainstream smoke and side stream smoke of different types of cigarettes. Carcinogenesis 8, 729-731; doi:10.1093/carcin/8. 5.729
    • (1987) Carcinogenesis , vol.8 , pp. 729-731
    • Adams, J.D.1    O'Mara-Adams, K.J.2    Hoffmann, D.3
  • 2
    • 41149101153 scopus 로고    scopus 로고
    • Characterization of type II ligands in CYP2C9 and CYP3A4
    • doi:10.1021/jm701121y
    • Ahlström M. M., Zamora I. (2008): Characterization of type II ligands in CYP2C9 and CYP3A4. J. Med. Chem. 51, 1755-1763; doi:10.1021/jm701121y
    • (2008) J. Med. Chem. , vol.51 , pp. 1755-1763
    • Ahlström, M.M.1    Zamora, I.2
  • 4
    • 0023708280 scopus 로고
    • Effect of antibodies against cytochrome P-450 on demethylation and denitrosation of N-nitrosodimethylamine and N-nitrosomethylaniline
    • doi:10.1007/BF02128182
    • Amelizad Z., Appel K. E., Oesch F., Hildebrandt A. G. (1988): Effect of antibodies against cytochrome P-450 on demethylation and denitrosation of N-nitrosodimethylamine and N-nitrosomethylaniline. J. Cancer Res. Clin. Oncol. 114, 380-384; doi:10.1007/BF02128182
    • (1988) J. Cancer Res. Clin. Oncol. , vol.114 , pp. 380-384
    • Amelizad, Z.1    Appel, K.E.2    Oesch, F.3    Hildebrandt, A.G.4
  • 5
    • 0021680014 scopus 로고
    • Relevance of nitrosamines to human cancer
    • doi:10.1093/carcin/5.11.1381
    • Bartsch H., Montesano R. (1984): Relevance of nitrosamines to human cancer. Carcinogenesis 5, 1381-1393; doi:10.1093/carcin/5.11.1381
    • (1984) Carcinogenesis , vol.5 , pp. 1381-1393
    • Bartsch, H.1    Montesano, R.2
  • 6
    • 0037232875 scopus 로고    scopus 로고
    • Heterologous expression of mouse cytochrome P450 2E1 in V79 cells: Construction and characterization of the cell line and comparison with V79 cell line stably expressing rat P450 2E1 and human P450 2E1
    • Bernauer U., Glatt H., Heinrich-Hirsch B., Liu Y., Muckel E., Vieth B., Gundert-Remy U. (2003): Heterologous expression of mouse cytochrome P450 2E1 in V79 cells: construction and characterization of the cell line and comparison with V79 cell line stably expressing rat P450 2E1 and human P450 2E1. Altern. Lab. Anim. 31, 21-30
    • (2003) Altern. Lab. Anim. , vol.31 , pp. 21-30
    • Bernauer, U.1    Glatt, H.2    Heinrich-Hirsch, B.3    Liu, Y.4    Muckel, E.5    Vieth, B.6    Gundert-Remy, U.7
  • 7
    • 0035950397 scopus 로고    scopus 로고
    • α-Naphthoflavone acts as activator and reversible or irreversible inhibitor of rabbit microsomal CYP3A6
    • doi:10.1016/S0009-2797(01)00263-0
    • Borek-Dohalska L., Hodek P., Sulc M., Stiborova M. (2001): α-Naphthoflavone acts as activator and reversible or irreversible inhibitor of rabbit microsomal CYP3A6. Chem. Biol. Interact. 138, 85-106; doi:10.1016/S0009-2797(01)00263-0
    • (2001) Chem. Biol. Interact. , vol.138 , pp. 85-106
    • Borek-Dohalska, L.1    Hodek, P.2    Sulc, M.3    Stiborova, M.4
  • 8
    • 0018735516 scopus 로고
    • Statistical analysis of the enzyme kinetic data
    • Cleland W. W. (1983): Statistical analysis of the enzyme kinetic data. Methods Enzymol. 63, 103-138
    • (1983) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 9
    • 0031940804 scopus 로고    scopus 로고
    • Effect of common organic solvents on in vitro cytochrome P450-mediated metabolic activities in human liver microsomes
    • Chauret N., Gauthier A., Nicoll-Griffith D. A. (1998): Effect of common organic solvents on in vitro cytochrome P450-mediated metabolic activities in human liver microsomes. Drug. Metab. Dispos. 26, 1-4
    • (1998) Drug. Metab. Dispos. , vol.26 , pp. 1-4
    • Chauret, N.1    Gauthier, A.2    Nicoll-Griffith, D.A.3
  • 10
    • 41849093366 scopus 로고    scopus 로고
    • Formation of formaldehyde adducts in the reactions of DNA and deoxyribonucleosides with alpha-acetates of 4-(methylnitrosamino)-1-(3-pyridyl)- 1-butanone (NNK), 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL), and N-nitrosodimethylamine (NDMA)
    • doi:10.1021/tx7003823
    • Cheng G., Wang M., Upadhyaya P., Villalta P. W., Hecht S. S. (2008): Formation of formaldehyde adducts in the reactions of DNA and deoxyribonucleosides with alpha-acetates of 4-(methylnitrosamino)-1-(3-pyridyl)- 1-butanone (NNK), 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL), and N-nitrosodimethylamine (NDMA). Chem Res. Toxicol. 21, 746-751; doi:10.1021/tx7003823
    • (2008) Chem Res. Toxicol. , vol.21 , pp. 746-751
    • Cheng, G.1    Wang, M.2    Upadhyaya, P.3    Villalta, P.W.4    Hecht, S.S.5
  • 11
    • 0017326501 scopus 로고
    • NADPH-cytochrome P-450 reductase from rat liver: Purification by affinity chromatography and characterization
    • doi:10.1021/bi00625a014
    • Dignam J. D., Strobel H. W. (1977): NADPH-cytochrome P-450 reductase from rat liver: purification by affinity chromatography and characterization. Biochemistry 16, 1116-1123; doi:10.1021/bi00625a014
    • (1977) Biochemistry , vol.16 , pp. 1116-1123
    • Dignam, J.D.1    Strobel, H.W.2
  • 13
    • 0014188061 scopus 로고
    • Organotropic carcinogenic effects of 65 different N-nitroso-compounds on BD-rats
    • (in German); doi:10.1007/BF00524152
    • Druckrey D., Preussmann R., Ivankovic S., Schmähl D. (1967): Organotropic carcinogenic effects of 65 different N-nitroso-compounds on BD-rats. Z. Krebsforsch 69, 103-201 (in German); doi:10.1007/BF00524152
    • (1967) Z. Krebsforsch , vol.69 , pp. 103-201
    • Druckrey, D.1    Preussmann, R.2    Ivankovic, S.3    Schmähl, D.4
  • 14
    • 0030011821 scopus 로고    scopus 로고
    • The relationship between N-nitrosodimethylamine metabolism and DNA methylation in isolated rat hepatocytes
    • DOI 10.1093/carcin/17.5.1127
    • Encell L., Foiles P. G., Gold B. (1996): The relationship between N-nitrosodimethylamine metabolism and DNA methylation in isolated rat hepatocytes. Carcinogenesis 17, 1127-1134; doi:10.1093/carcin/17.5.1127 (Pubitemid 26158414)
    • (1996) Carcinogenesis , vol.17 , Issue.5 , pp. 1127-1134
    • Encell, L.1    Foiles, P.G.2    Gold, B.3
  • 15
    • 0026035519 scopus 로고
    • Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects
    • doi:10.1021/tx00020a008
    • Guengerich F. P., Kim D. H., Iwasaki M. (1991): Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects. Chem Res. Toxicol. 4, 168-179; doi:10.1021/tx00020a008
    • (1991) Chem Res. Toxicol. , vol.4 , pp. 168-179
    • Guengerich, F.P.1    Kim, D.H.2    Iwasaki, M.3
  • 16
    • 0017057951 scopus 로고
    • Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450
    • Haugen D. A., Coon M. J. (1967): Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450. J. Biol. Chem. 251, 7929-7939
    • (1967) J. Biol. Chem. , vol.251 , pp. 7929-7939
    • Haugen, D.A.1    Coon, M.J.2
  • 17
    • 41849128336 scopus 로고    scopus 로고
    • N-nitrosoamines
    • (Eds. W. B. Rom and S. B. Markowitz), Wolters Kluwer/Lipponcott Williams & Wilkins, Philadelphia
    • Hecht S. S. (2007): N-nitrosoamines. In: Environmental and Occupational Medicine. (Eds. W. B. Rom and S. B. Markowitz), pp. 1226-1239, Wolters Kluwer/Lipponcott Williams & Wilkins, Philadelphia
    • (2007) Environmental and Occupational Medicine , pp. 1226-1239
    • Hecht, S.S.1
  • 18
    • 38949170926 scopus 로고    scopus 로고
    • Progress and challenges in selected areas of tobacco carcinogenesis
    • doi:10.1021/tx7002068
    • Hecht S. S. (2008): Progress and challenges in selected areas of tobacco carcinogenesis. Chem Res. Toxicol. 21, 160-171; doi:10.1021/tx7002068
    • (2008) Chem Res. Toxicol. , vol.21 , pp. 160-171
    • Hecht, S.S.1
  • 19
    • 0023798421 scopus 로고
    • Metabolism of diamantane by rat liver microsomal cytochromes P-450
    • Hodek P., Janscak P., Anzenbacher P., Burkhard J., Janků J., Vodicka L. (1988): Metabolism of diamantane by rat liver microsomal cytochromes P-450. Xenobiotica 18, 1109-1118; doi:10.3109/00498258809042233 (Pubitemid 18267199)
    • (1988) Xenobiotica , vol.18 , Issue.10 , pp. 1109-1118
    • Hodek, P.1    Janscak, P.2    Anzenbacher, P.3    Burkhard, J.4    Janku, J.5    Vodicka, L.6
  • 20
    • 0028829754 scopus 로고
    • Probing the cytochrome P-450 2B1 active site with diamantoid compounds
    • Hodek P., Burkhard J., Janků J. (1995): Probing the cytochrome P-450 2B1 active site with diamantoid compounds. Gen. Physiol. Biophys. 14, 225-239
    • (1995) Gen. Physiol. Biophys. , vol.14 , pp. 225-239
    • Hodek, P.1    Burkhard, J.2    Janků, J.3
  • 21
    • 17144383651 scopus 로고    scopus 로고
    • Structural requirements for inhibitors of cytochromes P450 2B: Assessment of the enzyme interaction with diamondoids
    • doi:10.1080/14756360400024324
    • Hodek P., Borek-Dohalska L., Sopko B., Sulc M., Smrcek S., Hudecek J., Janků J., Stiborová M. (2005): Structural requirements for inhibitors of cytochromes P450 2B: assessment of the enzyme interaction with diamondoids. J. Enzyme Inhib. Med. Chem. 20, 25-33; doi:10.1080/ 14756360400024324
    • (2005) J. Enzyme Inhib. Med. Chem. , vol.20 , pp. 25-33
    • Hodek, P.1    Borek-Dohalska, L.2    Sopko, B.3    Sulc, M.4    Smrcek, S.5    Hudecek, J.6    Janků, J.7    Stiborová, M.8
  • 22
    • 0029041637 scopus 로고
    • Induction mechanisms of cytochrome P450 2E1 in liver: Interplay between ethanol treatment and starvation
    • doi:10.1016/0006-2952(95)00128-M
    • Hu Y., Ingelman-Sundberg M., Lindros K. O. (1995): Induction mechanisms of cytochrome P450 2E1 in liver: interplay between ethanol treatment and starvation. Biochem. Pharmacol. 50, 155-161; doi:10.1016/0006-2952(95)00128-M
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 155-161
    • Hu, Y.1    Ingelman-Sundberg, M.2    Lindros, K.O.3
  • 23
    • 33947491564 scopus 로고    scopus 로고
    • Formaldehyde, 2-butoxyethanol and 1-terc-butoxypropan-2-ol
    • IARC (International Agency for Research on Cancer) IARC, Lyon, France
    • IARC (International Agency for Research on Cancer) (2006): Formaldehyde, 2-butoxyethanol and 1-terc-butoxypropan-2-ol. In: IARC Monographs on the Evaluation of Carcinogenic Risk to Humans. Vol. 88, pp. 39-325, IARC, Lyon, France
    • (2006) IARC Monographs on the Evaluation of Carcinogenic Risk to Humans , vol.88 , pp. 39-325
  • 24
    • 0030910832 scopus 로고    scopus 로고
    • Intramolecular isotope effects for benzylic hydroxylation of isomeric xylenes and 4,4′-dimethylbiphenyl by cytochrome P450: Relationship between distance of methyl groups and masking of the intrinsic isotope effect
    • doi:10.1021/bi962810m
    • Iyer K. R., Jones J. P., Darbyshire J. F., Trager W. F. (1997): Intramolecular isotope effects for benzylic hydroxylation of isomeric xylenes and 4,4′-dimethylbiphenyl by cytochrome P450: relationship between distance of methyl groups and masking of the intrinsic isotope effect. Biochemistry 36, 7136-7143; doi:10.1021/bi962810m
    • (1997) Biochemistry , vol.36 , pp. 7136-7143
    • Iyer, K.R.1    Jones, J.P.2    Darbyshire, J.F.3    Trager, W.F.4
  • 25
    • 0024269576 scopus 로고
    • Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c
    • Johnson E. F., Schwab G. E., Vickery L. E. (1988): Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c. J. Biol. Chem. 263, 17672-17677
    • (1988) J. Biol. Chem. , vol.263 , pp. 17672-17677
    • Johnson, E.F.1    Schwab, G.E.2    Vickery, L.E.3
  • 26
    • 0024451771 scopus 로고
    • Theory for the observed isotope effects from enzymatic systems that form multiple products via branched reaction pathways: Cytochrome P-450
    • doi:10.1021/bi00449a009
    • Korzekwa K. R., Trager W. F., Gillette J. R. (1989): Theory for the observed isotope effects from enzymatic systems that form multiple products via branched reaction pathways: cytochrome P-450. Biochemistry 28, 9012-9018; doi:10.1021/bi00449a009
    • (1989) Biochemistry , vol.28 , pp. 9012-9018
    • Korzekwa, K.R.1    Trager, W.F.2    Gillette, J.R.3
  • 27
    • 0034694174 scopus 로고    scopus 로고
    • Development of a Salmonella tester strain sensitive to promutagenic N-nitrosamines: Expression of recombinant CYP2A6 and human NADPH-cytochrome P450 reductase in S. typhimurium YG7108
    • Kushida H., Fujita K., Suzuki A., Yamada M., Nohmi T., Kamataki T. (2000): Development of a Salmonella tester strain sensitive to promutagenic N-nitrosamines: expression of recombinant CYP2A6 and human NADPH-cytochrome P450 reductase in S. typhimurium YG7108. Mutat. Res. 471, 135-143
    • (2000) Mutat. Res. , vol.471 , pp. 135-143
    • Kushida, H.1    Fujita, K.2    Suzuki, A.3    Yamada, M.4    Nohmi, T.5    Kamataki, T.6
  • 28
    • 0026046620 scopus 로고
    • Purification and properties of a shortened form of cytochrome P-450 2E1: Deletion of the NH2-terminal membrane-insertion signal peptide does not alter the catalytic activities
    • doi:10.1073/pnas.88.20.9141
    • Larson J. R., Coon M. J., Porter T. D. (1991): Purification and properties of a shortened form of cytochrome P-450 2E1: deletion of the NH2-terminal membrane-insertion signal peptide does not alter the catalytic activities. Proc. Natl. Acad. Sci. U.S.A. 88, 9141-9145; doi:10.1073/pnas.88.20. 9141
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9141-9145
    • Larson, J.R.1    Coon, M.J.2    Porter, T.D.3
  • 29
    • 0023477406 scopus 로고
    • Structure activity relations in carcinogenesis by N-nitroso compounds
    • doi:10.1007/BF00144269
    • Lijinsky W. (1987): Structure activity relations in carcinogenesis by N-nitroso compounds. Cancer Metastasis Rev. 6, 301-356; doi:10.1007/BF00144269
    • (1987) Cancer Metastasis Rev. , vol.6 , pp. 301-356
    • Lijinsky, W.1
  • 30
    • 49049098816 scopus 로고    scopus 로고
    • Mutagenicity of N-nitrosodiethanolamine in a V79-derived cell line expressing two human biotransformation enzymes
    • doi:10.1016/j.mrfmmm.2008.06.003
    • Liu Y., Glatt H. (2008): Mutagenicity of N-nitrosodiethanolamine in a V79-derived cell line expressing two human biotransformation enzymes. Mutat. Res. 643, 64-69; doi:10.1016/j.mrfmmm.2008.06.003
    • (2008) Mutat. Res. , vol.643 , pp. 64-69
    • Liu, Y.1    Glatt, H.2
  • 31
    • 34047158165 scopus 로고    scopus 로고
    • Visible spectra of type II cytochrome P450-drug complexes: Evidence that "incomplete" heme coordination is common
    • doi:10.1124/dmd.106.012609
    • Locuson C. W., Hutzler J. M., Tracy T. S. (2007): Visible spectra of type II cytochrome P450-drug complexes: Evidence that "incomplete" heme coordination is common. Drug. Metab. Dispos. 35, 614-622; doi:10.1124/dmd.106. 012609
    • (2007) Drug. Metab. Dispos. , vol.35 , pp. 614-622
    • Locuson, C.W.1    Hutzler, J.M.2    Tracy, T.S.3
  • 32
    • 33846383667 scopus 로고    scopus 로고
    • Differential behavior of the sub-sites of cytochrome P450 active site in binding of substrates, and products (implications for coupling/uncoupling)
    • Narasimhulu S. (2007): Differential behavior of the sub-sites of cytochrome P450 active site in binding of substrates, and products (implications for coupling/uncoupling). Biochim. Biophys. Acta 1770, 360-375
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 360-375
    • Narasimhulu, S.1
  • 33
    • 77049138167 scopus 로고
    • The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
    • Nash T. (1953): The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochem. J. 55, 416-421
    • (1953) Biochem. J. , vol.55 , pp. 416-421
    • Nash, T.1
  • 34
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T., Sato R. (1964): The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 239, 2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 35
    • 2942620151 scopus 로고    scopus 로고
    • A novel "clip-and-link" activity of repeat in toxin (RTX) proteins from gram-negative pathogens. Covalent protein cross-linking by an Asp-Lys isopeptide bond upon calcium-dependent processing at an Asp-Pro bond
    • doi:10.1074/jbc.M314013200
    • Osička R., Procházková K., Šulc M., Linhartová I., Havlíček V., Šebo P. (2004): A novel "clip-and-link" activity of repeat in toxin (RTX) proteins from gram-negative pathogens. Covalent protein cross-linking by an Asp-Lys isopeptide bond upon calcium-dependent processing at an Asp-Pro bond. J. Biol. Chem. 279, 24944-24956; doi:10.1074/jbc.M314013200
    • (2004) J. Biol. Chem. , vol.279 , pp. 24944-24956
    • Osička, R.1    Procházková, K.2    Šulc, M.3    Linhartová, I.4    Havlíček, V.5    Šebo, P.6
  • 36
    • 33646874799 scopus 로고    scopus 로고
    • Surface plasmon resonance analysis of antifungal azoles binding to CYP3A4 with kinetic resolution of multiple binding orientations
    • doi:10.1021/bi0600042
    • Pearson J. T., Hill J. J., Swank J., Isoherranen N., Kunze K. L., Atkins W.M. (2006): Surface plasmon resonance analysis of antifungal azoles binding to CYP3A4 with kinetic resolution of multiple binding orientations. Biochemistry 45, 6341-6353; doi:10.1021/bi0600042
    • (2006) Biochemistry , vol.45 , pp. 6341-6353
    • Pearson, J.T.1    Hill, J.J.2    Swank, J.3    Isoherranen, N.4    Kunze, K.L.5    Atkins, W.M.6
  • 39
    • 0023257802 scopus 로고
    • The enigma of the organ-specificity of carcinogenic nitrosamines
    • doi:10.1016/0165-6147(87)90164-7
    • Preussmann R., Weissler, M. (1987): The enigma of the organ-specificity of carcinogenic nitrosamines. Trends Pharm. Sci. 8,185-189; doi:10.1016/0165- 6147(87)90164-7
    • (1987) Trends Pharm. Sci. , vol.8 , pp. 185-189
    • Preussmann, R.1    Weissler, M.2
  • 40
    • 54249135294 scopus 로고    scopus 로고
    • Mutagenic potential of nitrenium ions of nitrobenzanthrones: Correlation between theory and experiment
    • doi:10.1002/em.20411
    • Reynisson J., Stiborová M., Martínek V., Gamboa da Costa G., Phillips D. H., Arlt V. M. (2008): Mutagenic potential of nitrenium ions of nitrobenzanthrones: correlation between theory and experiment. Environ. Mol. Mutagen. 49, 659-667; doi:10.1002/em.20411
    • (2008) Environ. Mol. Mutagen. , vol.49 , pp. 659-667
    • Reynisson, J.1    Stiborová, M.2    Martínek, V.3    Gamboa Da Costa, G.4    Phillips, D.H.5    Arlt, V.M.6
  • 41
    • 0014059179 scopus 로고
    • Spectral studies of drug interaction with hepatic microsomal cytochrome
    • Schenkman J. B., Remmer H., Estabrook R. W. (1967): Spectral studies of drug interaction with hepatic microsomal cytochrome. Mol. Pharmacol. 3, 113-123
    • (1967) Mol. Pharmacol. , vol.3 , pp. 113-123
    • Schenkman, J.B.1    Remmer, H.2    Estabrook, R.W.3
  • 42
    • 0025120321 scopus 로고
    • Metabolic activation and biological effects of nitrosamines in the mammalian lung
    • doi:10.1016/0163-7258(90)90037-3
    • Schuller H. M., Falzon M., McMahon J. B. (1990): Metabolic activation and biological effects of nitrosamines in the mammalian lung. Pharmacol. Ther. 46, 95-103; doi:10.1016/0163-7258(90)90037-3
    • (1990) Pharmacol. Ther. , vol.46 , pp. 95-103
    • Schuller, H.M.1    Falzon, M.2    McMahon, J.B.3
  • 43
    • 0025937342 scopus 로고
    • Recent studies in Canada on the occurrence and formation of N-nitroso compounds in foods and food contact materials
    • Sen N. P. (1991): Recent studies in Canada on the occurrence and formation of N-nitroso compounds in foods and food contact materials. IARC Sci. Publ. 105, 232-234
    • (1991) IARC Sci. Publ. , vol.105 , pp. 232-234
    • Sen, N.P.1
  • 44
    • 0020503960 scopus 로고
    • Pharmacokinetic model for N-nitrosodimethylamine based on Michaelis-Menten constants determined with the isolated perfused rat liver
    • Skipper P. L., Tomera J. F., Wishnok J. S., Brunengraber H., Tannenbaum S. R. (1983): Pharmacokinetic model for N-nitrosodimethylamine based on Michaelis-Menten constants determined with the isolated perfused rat liver. Cancer Res. 43, 4786-4790
    • (1983) Cancer Res. , vol.43 , pp. 4786-4790
    • Skipper, P.L.1    Tomera, J.F.2    Wishnok, J.S.3    Brunengraber, H.4    Tannenbaum, S.R.5
  • 45
    • 0003174184 scopus 로고
    • Analysis of proteins
    • (Ed. F. Ausubel), John Wiley & Sons Inc., New York
    • Smith J. A. (1995): Analysis of proteins. In: Short Protocols in Molecular Biology. (Ed. F. Ausubel), pp 10.5-10.11 John Wiley & Sons Inc., New York
    • (1995) Short Protocols in Molecular Biology
    • Smith, J.A.1
  • 46
    • 0031867196 scopus 로고    scopus 로고
    • Characterization of xenobiotic-metabolizing enzymes and nitrosamine metabolism in the human esophagus
    • DOI 10.1093/carcin/19.4.667
    • Smith T. J., Liao A., Wang L. D., Yang G.Y., Starcic S., Philbert M. A., Yang C. S. (1998): Characterization of xenobiotic-metabolizing enzymes and nitrosamine metabolism in the human esophagus. Carcinogenesis 19, 667-672; doi:10.1093/carcin/19.4.667 (Pubitemid 28376812)
    • (1998) Carcinogenesis , vol.19 , Issue.4 , pp. 667-672
    • Smith, T.J.1    Liao, A.2    Wang, L.-D.3    Yang, G.-Y.4    Starcic, S.5    Philbert, M.A.6    Yang, C.S.7
  • 47
    • 0025050762 scopus 로고
    • Solvolysis of model compounds for a-hydroxylation of N-nitroso- nornicotine and 4-(methylnitrosamino)-1-(3-pyridiyl)-1-butanone. Evidence for a cyclic oxonium ion intermediate in the alkylation of nucleotides
    • doi:10.1021/tx00016a013
    • Spratt T. E., Peterson L. A., Confer W. L., Hecht S. S. (1990): Solvolysis of model compounds for a-hydroxylation of N-nitroso-nornicotine and 4-(methylnitrosamino)-1-(3-pyridiyl)-1-butanone. Evidence for a cyclic oxonium ion intermediate in the alkylation of nucleotides. Chem Res. Toxicol. 3, 350-356; doi:10.1021/tx00016a013
    • (1990) Chem Res. Toxicol. , vol.3 , pp. 350-356
    • Spratt, T.E.1    Peterson, L.A.2    Confer, W.L.3    Hecht, S.S.4
  • 48
    • 0026534746 scopus 로고
    • Peroxidase oxidizes N-nitrosomethylaniline to ultimate carcinogens(s) binding to DNA and transfer RNA in vitro
    • doi:10.1016/0304-3835(92)90089-E
    • Stiborová M., Frei E., Schmeiser H. H., Wiessler M., Anzenbacher P. (1992): Peroxidase oxidizes N-nitrosomethylaniline to ultimate carcinogens(s) binding to DNA and transfer RNA in vitro. Cancer Lett. 63, 53-59; doi:10.1016/0304-3835(92)90089-E
    • (1992) Cancer Lett. , vol.63 , pp. 53-59
    • Stiborová, M.1    Frei, E.2    Schmeiser, H.H.3    Wiessler, M.4    Anzenbacher, P.5
  • 49
    • 0030155090 scopus 로고    scopus 로고
    • Cytochromes P450 2B1 and P450 2B2 demethylate N-nitrosodimethylamine and N-nitrosomethylaniline in vitro
    • Stiborová M., Hansíková H., Frei E. (1996a): Cytochromes P450 2B1 and P450 2B2 demethylate N-nitrosodimethylamine and N-nitrosomethylaniline in vitro. Gen Physiol. Biophys. 15, 211-223
    • (1996) Gen Physiol. Biophys. , vol.15 , pp. 211-223
    • Stiborová, M.1    Hansíková, H.2    Frei, E.3
  • 50
    • 0030596188 scopus 로고    scopus 로고
    • Metabolism of carcinogenic N-nitroso-N-methylaniline by purified cytochromes p450 2B1 and p450 2B2
    • DOI 10.1016/S0304-3835(97)89405-0, PII S0304383596044473
    • Stiborová M., Hansíková H., Frei E. (1996b): Metabolism of carcinogenic N-nitroso-N-methylaniline by purified cytochromes P450 2B1 and P450 2B2. Cancer Lett. 110, 11-17; doi:10.1016/S0304-3835(97)89405- 0 (Pubitemid 27042916)
    • (1996) Cancer Letters , vol.110 , Issue.1-2 , pp. 11-17
    • Stiborova, M.1    Hansikova, H.2    Frei, E.3
  • 51
    • 0031218909 scopus 로고    scopus 로고
    • An investigation of the metabolism of N-nitrosodimemylamine and N-nitrosomethylaniline by horseradish peroxidase in vitro
    • Stiborová M., Hansíková H., Schmeiser H. H., Frei E. (1997): An investigation of the metabolism of N-nitrosodimemylamine and N-nitrosomethylaniline by horseradish peroxidase in vitro. Gen Physiol. Biophys. 16, 285-297
    • (1997) Gen Physiol. Biophys. , vol.16 , pp. 285-297
    • Stiborová, M.1    Hansíková, H.2    Schmeiser, H.H.3    Frei, E.4
  • 52
    • 0033606129 scopus 로고    scopus 로고
    • 32P- postlabeling technique
    • DOI 10.1016/S0304-3835(98)00369-3, PII S0304383598003693
    • Stiborová M., Schmeiser H. H., Wiessler M., Frei E. (1999): Direct evidence for the formation of deoxyribonucleotide adducts from carcinogenic N-nitroso-N-methylaniline revealed by the 32P-postlabeling technique. Cancer Lett. 138, 61-66; doi:10.1016/S0304-3835(98)00369-3 (Pubitemid 29189185)
    • (1999) Cancer Letters , vol.138 , Issue.1-2 , pp. 61-66
    • Stiborova, M.1    Schmeiser, H.H.2    Wiessler, M.3    Frei, E.4
  • 53
    • 8644288137 scopus 로고    scopus 로고
    • The anticancer drug ellipticine forms covalent DNA adducts, mediated by human cytochromes P450, through metabolism to 13-hydroxyellipticine and ellipticine N2-oxide
    • doi:10.1158/0008-5472.CAN-04-2202
    • Stiborová M., Sejbal J., Borek-Dohalská L., Aimová D., Poljaková J., Forsterová K., Rupertová M., Wiesner J., Hudeček J., Wiessler M., Frei E. (2004): The anticancer drug ellipticine forms covalent DNA adducts, mediated by human cytochromes P450, through metabolism to 13-hydroxyellipticine and ellipticine N2-oxide. Cancer Res. 64, 8374-8380; doi:10.1158/0008-5472.CAN-04-2202
    • (2004) Cancer Res. , vol.64 , pp. 8374-8380
    • Stiborová, M.1    Sejbal, J.2    Borek-Dohalská, L.3    Aimová, D.4    Poljaková, J.5    Forsterová, K.6    Rupertová, M.7    Wiesner, J.8    Hudeček, J.9    Wiessler, M.10    Frei, E.11
  • 54
    • 14844344427 scopus 로고    scopus 로고
    • Rabbit liver microsomal system: Study of interaction with two model N-nitrosamines and their metabolism
    • Šulc M., Kubíčkova B., Máslová V., Hodek P. (2004): Rabbit liver microsomal system: Study of interaction with two model N-nitrosamines and their metabolism. Gen. Physiol. Biophys. 23. 423-433
    • (2004) Gen. Physiol. Biophys. , vol.23 , pp. 423-433
    • Šulc, M.1    Kubíčkova, B.2    Máslová, V.3    Hodek, P.4
  • 55
    • 0022342407 scopus 로고
    • Demethylation and denitrosation of nitrosamines by cytochrome P-450 isozymes
    • doi:10.1016/0003-9861(85)90476-X
    • Tu Y. Y., Yang C. S. (1985): Demethylation and denitrosation of nitrosamines by cytochrome P-450 isozymes. Arch. Biochem. Biophys. 242, 32-40; doi:10.1016/0003-9861(85)90476-X
    • (1985) Arch. Biochem. Biophys. , vol.242 , pp. 32-40
    • Tu, Y.Y.1    Yang, C.S.2
  • 56
    • 28144456644 scopus 로고    scopus 로고
    • U.S. Department of Health and Human Services U.S. Government Printing Office, Washington DC
    • U.S. Department of Health and Human Services (2004): 11th Report on Carcinogens. U.S. Government Printing Office, Washington DC
    • (2004) 11th Report on Carcinogens
  • 57
    • 0017801794 scopus 로고
    • Purified liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states
    • Vermilion J. L., Coon M. J. (1978): Purified liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states. J. Biol. Chem. 253, 2694-2704
    • (1978) J. Biol. Chem. , vol.253 , pp. 2694-2704
    • Vermilion, J.L.1    Coon, M.J.2
  • 58
    • 0024289285 scopus 로고
    • Investigation of the bicinchoninic acid protein assay: Identification of the groups resposible for color formation
    • doi:10.1016/0003-2697(88)90383-1
    • Wiechelman K. J., Braun R. D., Fitzpatrick J. D. (1988): Investigation of the bicinchoninic acid protein assay: identification of the groups resposible for color formation. Anal. Biochem. 175, 231-237; doi:10.1016/0003-2697(88) 90383-1
    • (1988) Anal. Biochem. , vol.175 , pp. 231-237
    • Wiechelman, K.J.1    Braun, R.D.2    Fitzpatrick, J.D.3
  • 59
    • 73649173283 scopus 로고
    • Microsomal triphosphopyridine nucleotide-cytochrome c redurtase of liver
    • Williams C. H. Jr., Kamin H. (1962): Microsomal triphosphopyridine nucleotide-cytochrome c redurtase of liver. J. Biol. Chem. 237, 587-595
    • (1962) J. Biol. Chem. , vol.237 , pp. 587-595
    • Williams Jr., C.H.1    Kamin, H.2
  • 60
    • 0021958785 scopus 로고
    • Metabolism of nitrosamines by purified rabbit liver cytochrome P-450 isozymes
    • Yang C. S., Tu Y. Y., Koop D. R., Coon M. J. (1985): Metabolism of nitrosamines by purified rabbit liver cytochrome P-450 isozymes. Cancer Res. 45, 1140-1145
    • (1985) Cancer Res. , vol.45 , pp. 1140-1145
    • Yang, C.S.1    Tu, Y.Y.2    Koop, D.R.3    Coon, M.J.4
  • 61
    • 0025167020 scopus 로고
    • Cytochrome P450IIE1: Roles in nitrosamine metabolism and mechanisms of regulation
    • doi:10.3109/03602539009041082
    • Yang C. S. Yoo J. S., Ishizaki H., Hong J. Y. (1990): Cytochrome P450IIE1: roles in nitrosamine metabolism and mechanisms of regulation. Drug Metab. Rev. 22, 147-159; doi:10.3109/03602539009041082
    • (1990) Drug Metab. Rev. , vol.22 , pp. 147-159
    • Yang, C.S.1    Yoo, J.S.2    Ishizaki, H.3    Hong, J.Y.4
  • 62
    • 0028324459 scopus 로고
    • Cytochrome P-450 enzymes as targets for chemoprevention against chemical carcinogenesis and toxicity: Opportunities and limitations
    • Yang C. S., Smith T. J., Hong J. Y. (1994): Cytochrome P-450 enzymes as targets for chemoprevention against chemical carcinogenesis and toxicity: opportunities and limitations. Cancer Res. 54 (Suppl. 7), 1982-1986
    • (1994) Cancer Res. , vol.54 , Issue.SUPPL. 7 , pp. 1982-1986
    • Yang, C.S.1    Smith, T.J.2    Hong, J.Y.3
  • 63
    • 0023263168 scopus 로고
    • Nature of N-nitrosodimethylamine demethylase and its inhibitors
    • Yoo J. S., Cheung R. J., Patten C. J., Wade D., Yang C. S. (1987): Nature of N-nitrosodimethylamine demethylase and its inhibitors. Cancer Res. 47, 3378-3383
    • (1987) Cancer Res. , vol.47 , pp. 3378-3383
    • Yoo, J.S.1    Cheung, R.J.2    Patten, C.J.3    Wade, D.4    Yang, C.S.5
  • 64
    • 0025635625 scopus 로고
    • Roles of cytochrome P450IIE1 in the dealkylation and denitrosation of N-nitrosodimethylamine and N-nitrosodiethylamine in rat liver microsomes
    • doi:10.1093/carcin/11.12.2239
    • Yoo J. S., Ishizaki H., Yang C. S. (1990): Roles of cytochrome P450IIE1 in the dealkylation and denitrosation of N-nitrosodimethylamine and N-nitrosodiethylamine in rat liver microsomes. Carcinogenesis 11, 2239-2243; doi:10.1093/carcin/11.12.2239
    • (1990) Carcinogenesis , vol.11 , pp. 2239-2243
    • Yoo, J.S.1    Ishizaki, H.2    Yang, C.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.