메뉴 건너뛰기




Volumn 316, Issue 1, 2006, Pages 295-303

Inactivation of CYP2A6 and CYP2A13 during nicotine metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE OXIDASE; COTININE; CYTOCHROME P450 2A13; CYTOCHROME P450 2A6; NICOTINE; NICOTINIC AGENT; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 29244464299     PISSN: 00223565     EISSN: 15210103     Source Type: Journal    
DOI: 10.1124/jpet.105.091306     Document Type: Article
Times cited : (49)

References (39)
  • 1
    • 13444274285 scopus 로고    scopus 로고
    • Metabolism of nicotine and cotinine by human cytochrome P450 2A13
    • Bao Z, He XY, Ding X, Prabhu S, and Hong JY (2005) Metabolism of nicotine and cotinine by human cytochrome P450 2A13. Drug Metab Dispos 33:258-261.
    • (2005) Drug Metab Dispos , vol.33 , pp. 258-261
    • Bao, Z.1    He, X.Y.2    Ding, X.3    Prabhu, S.4    Hong, J.Y.5
  • 2
    • 0024215844 scopus 로고
    • Pharmacological aspects of cigarette smoking and nicotine addiction
    • Benowitz NL (1988) Pharmacological aspects of cigarette smoking and nicotine addiction. N Engl J Med 319:1318-1330.
    • (1988) N Engl J Med , vol.319 , pp. 1318-1330
    • Benowitz, N.L.1
  • 3
    • 0027958225 scopus 로고
    • Nicotine metabolic profile in man: Comparison of cigarette smoking and transdermal nicotine
    • Benowitz NL, Jacob P 3rd, Fong I, and Gupta S (1994) Nicotine metabolic profile in man: comparison of cigarette smoking and transdermal nicotine. J Pharmacol Exp Ther 268:296-303.
    • (1994) J Pharmacol Exp Ther , vol.268 , pp. 296-303
    • Benowitz, N.L.1    Jacob III, P.2    Fong, I.3    Gupta, S.4
  • 4
    • 0018606104 scopus 로고
    • The enzyme "aldehyde oxidase" is an iminium oxidase. Reaction with nicotine delta 1′(5′) iminium ion
    • Brandänge S and Lindblom L (1979) The enzyme "aldehyde oxidase" is an iminium oxidase. Reaction with nicotine delta 1′(5′) iminium ion. Biochem Biophys Res Commun 91:991-996.
    • (1979) Biochem Biophys Res Commun , vol.91 , pp. 991-996
    • Brandänge, S.1    Lindblom, L.2
  • 5
    • 0006003789 scopus 로고    scopus 로고
    • Determination of nicotine and its metabolites in biological fluids: In vivo studies
    • Gorrod JW and Jacob P 3rd, eds Elsevier Science B.V., Amsterdam
    • Davis RA and Curvall M (1999) Determination of nicotine and its metabolites in biological fluids: in vivo studies, in Analytical Determination of Nicotine and Related Compounds and Their Metabolites (Gorrod JW and Jacob P 3rd, eds) pp 583-643, Elsevier Science B.V., Amsterdam.
    • (1999) Analytical Determination of Nicotine and Related Compounds and Their Metabolites , pp. 583-643
    • Davis, R.A.1    Curvall, M.2
  • 6
    • 1642575105 scopus 로고    scopus 로고
    • Nicotine-related alkaloids and metabolites as inhibitors of human cytochrome P-450 2A6
    • Denton TT, Zhang X, and Cashman JR (2004) Nicotine-related alkaloids and metabolites as inhibitors of human cytochrome P-450 2A6. Biochem Pharmacol 67:751-756.
    • (2004) Biochem Pharmacol , vol.67 , pp. 751-756
    • Denton, T.T.1    Zhang, X.2    Cashman, J.R.3
  • 8
    • 0025986938 scopus 로고
    • Trapping of reactive intermediates by incorporation of 14C-sodium cyanide during microsomal oxidation
    • Gorrod JW, Whittlesea CM, and Lam SP (1991) Trapping of reactive intermediates by incorporation of 14C-sodium cyanide during microsomal oxidation. Adv Exp Med Biol 283:657-664.
    • (1991) Adv Exp Med Biol , vol.283 , pp. 657-664
    • Gorrod, J.W.1    Whittlesea, C.M.2    Lam, S.P.3
  • 9
    • 4243072969 scopus 로고    scopus 로고
    • Protein cross-linkage induced by formaldehyde derived from semicarbazide-sensitive amine oxidase-mediated deamination of methylamine
    • Gubisne-Haberle D, Hill W, Kazachkov M, Richardson JS, and Yu PH (2004) Protein cross-linkage induced by formaldehyde derived from semicarbazide- sensitive amine oxidase-mediated deamination of methylamine. J Pharmacol Exp Ther 310:1125-1132.
    • (2004) J Pharmacol Exp Ther , vol.310 , pp. 1125-1132
    • Gubisne-Haberle, D.1    Hill, W.2    Kazachkov, M.3    Richardson, J.S.4    Yu, P.H.5
  • 10
    • 0031822496 scopus 로고    scopus 로고
    • Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities
    • Hanna IH, Teiber J, Kokones KL, and Hollenberg PF (1998) Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities. Arch Biochem Biophys 350:324-332.
    • (1998) Arch Biochem Biophys , vol.350 , pp. 324-332
    • Hanna, I.H.1    Teiber, J.2    Kokones, K.L.3    Hollenberg, P.F.4
  • 11
    • 0033012856 scopus 로고    scopus 로고
    • Quantitation of 4-oxo-4-(3-pyridyl)butanoic acid and enantiomers of 4-hydroxy-4-(3-pyridyl)butanoic acid in human urine: A substantial pathway of nicotine metabolism
    • Hecht SS, Hatsukami DK, Bonilla LE, and Hochlater JB (1999) Quantitation of 4-oxo-4-(3-pyridyl)butanoic acid and enantiomers of 4-hydroxy-4-(3-pyridyl) butanoic acid in human urine: a substantial pathway of nicotine metabolism. Chem Res Toxicol 12:172-179.
    • (1999) Chem Res Toxicol , vol.12 , pp. 172-179
    • Hecht, S.S.1    Hatsukami, D.K.2    Bonilla, L.E.3    Hochlater, J.B.4
  • 12
    • 0033749374 scopus 로고    scopus 로고
    • 2′-Hydroxylation of nicotine by cytochrome P450 2A6 and human liver microsomes: Formation of a lung carcinogen precursor
    • Hecht SS, Hochalter JB, Villalta PW, and Murphy SE (2000) 2′-Hydroxylation of nicotine by cytochrome P450 2A6 and human liver microsomes: Formation of a lung carcinogen precursor. Proc Natl Acad Sci USA 97:12493-12497.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12493-12497
    • Hecht, S.S.1    Hochalter, J.B.2    Villalta, P.W.3    Murphy, S.E.4
  • 13
    • 14144253640 scopus 로고    scopus 로고
    • Metabolism and disposition kinetics of nicotine
    • Hukkanen J, Jacob P 3rd, and Benowitz NL (2005) Metabolism and disposition kinetics of nicotine. Pharmacol Rev 57:79-115.
    • (2005) Pharmacol Rev , vol.57 , pp. 79-115
    • Hukkanen, J.1    Jacob III, P.2    Benowitz, N.L.3
  • 14
    • 13944282327 scopus 로고    scopus 로고
    • Cytochrome P450 enzymes as catalysts of metabolism of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK), a tobacco-specific carcinogen
    • Jalas JR, Hecht SS, and Murphy SE (2005) Cytochrome P450 enzymes as catalysts of metabolism of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK), a tobacco-specific carcinogen. Chem Res Toxicol 18:95-110.
    • (2005) Chem Res Toxicol , vol.18 , pp. 95-110
    • Jalas, J.R.1    Hecht, S.S.2    Murphy, S.E.3
  • 15
    • 0032940229 scopus 로고    scopus 로고
    • Mechanism-based inactivation of cytochromes P450 2B1 and P450 2B6 by n-propylxanthate
    • Kent UM, Yanev S, and Hollenberg PF (1999) Mechanism-based inactivation of cytochromes P450 2B1 and P450 2B6 by n-propylxanthate. Chem Res Toxicol 12:317-322.
    • (1999) Chem Res Toxicol , vol.12 , pp. 317-322
    • Kent, U.M.1    Yanev, S.2    Hollenberg, P.F.3
  • 16
    • 0017760669 scopus 로고
    • Inhibition by cyanide of drug oxidations in rat liver microsomes
    • Kitada M, Chiba K, Kamataki T, and Kitagawa H (1977) Inhibition by cyanide of drug oxidations in rat liver microsomes. Jpn J Pharmacol 27:601-608.
    • (1977) Jpn J Pharmacol , vol.27 , pp. 601-608
    • Kitada, M.1    Chiba, K.2    Kamataki, T.3    Kitagawa, H.4
  • 17
    • 0019333104 scopus 로고
    • Kinetics of the hydroperoxide-dependent dealkylation reactions catalyzed by rabbit liver microsomal cytochrome P-450
    • Koop DR and Hollenberg PF (1980) Kinetics of the hydroperoxide-dependent dealkylation reactions catalyzed by rabbit liver microsomal cytochrome P-450. J Biol Chem 255:9685-9692.
    • (1980) J Biol Chem , vol.255 , pp. 9685-9692
    • Koop, D.R.1    Hollenberg, P.F.2
  • 18
    • 0025899971 scopus 로고
    • Application of chemical cytochrome P-450 model systems to studies on drug metabolism. IV. Mechanism of piperidine metabolism pathways via an iminium intermediate
    • Masumoto H, Ohta S, and Hirobe M (1991) Application of chemical cytochrome P-450 model systems to studies on drug metabolism. IV. Mechanism of piperidine metabolism pathways via an iminium intermediate. Drug Metab Dispos 19:768-780.
    • (1991) Drug Metab Dispos , vol.19 , pp. 768-780
    • Masumoto, H.1    Ohta, S.2    Hirobe, M.3
  • 19
    • 0022443226 scopus 로고
    • Characterization of hamster liver nicotine metabolism I. Relative rates of microsomal C and N oxidation
    • McCoy GD, Howard PC, and DeMarco GJ (1986) Characterization of hamster liver nicotine metabolism I. Relative rates of microsomal C and N oxidation. Biochem Pharmacol 35:2767-2773.
    • (1986) Biochem Pharmacol , vol.35 , pp. 2767-2773
    • McCoy, G.D.1    Howard, P.C.2    DeMarco, G.J.3
  • 20
    • 0030885491 scopus 로고    scopus 로고
    • A major role for CYP2A6 in nicotine C-oxidation by human liver microsomes
    • Messina ES, Tyndale RF, and Sellers EM (1997) A major role for CYP2A6 in nicotine C-oxidation by human liver microsomes. J Pharmacol Exp Ther 282:1608-1614.
    • (1997) J Pharmacol Exp Ther , vol.282 , pp. 1608-1614
    • Messina, E.S.1    Tyndale, R.F.2    Sellers, E.M.3
  • 22
    • 0032819109 scopus 로고    scopus 로고
    • Characterization of multiple products of cytochrome P450 2A6 catalyzed cotinine metabolism
    • Murphy SE, Johnson LM, and Pullo DA (1999) Characterization of multiple products of cytochrome P450 2A6 catalyzed cotinine metabolism. Chem Res Toxicol 12:639-645.
    • (1999) Chem Res Toxicol , vol.12 , pp. 639-645
    • Murphy, S.E.1    Johnson, L.M.2    Pullo, D.A.3
  • 23
    • 22944440387 scopus 로고    scopus 로고
    • Nicotine 5′-oxidation and methyl oxidation by P450 2A enzymes
    • Murphy SE, Raulinaitis V, and Brown KM (2005) Nicotine 5′-oxidation and methyl oxidation by P450 2A enzymes. Drug Metab Dispos 13:1166-1173.
    • (2005) Drug Metab Dispos , vol.13 , pp. 1166-1173
    • Murphy, S.E.1    Raulinaitis, V.2    Brown, K.M.3
  • 25
    • 0018778253 scopus 로고
    • Metabolic oxidation of nicotine to chemically reactive intermediates
    • Nguyen TL, Gruenke LD, and Castagnoli N (1979) Metabolic oxidation of nicotine to chemically reactive intermediates. J Med Chem 22:259-263.
    • (1979) J Med Chem , vol.22 , pp. 259-263
    • Nguyen, T.L.1    Gruenke, L.D.2    Castagnoli, N.3
  • 26
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T and 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
  • 27
    • 0023123970 scopus 로고
    • Stereochemical studies on the cytochrome P-450 catalyzed oxidation of (S)-nicotine to the (S)-delta-1′,5′-iminium ion
    • Peterson LA, Trevor AJ, and Castagnoli N Jr (1987) Stereochemical studies on the cytochrome P-450 catalyzed oxidation of (S)-nicotine to the (S)-delta-1′,5′-iminium ion. J Med Chem 30:249-254.
    • (1987) J Med Chem , vol.30 , pp. 249-254
    • Peterson, L.A.1    Trevor, A.J.2    Castagnoli Jr., N.3
  • 29
    • 0000555228 scopus 로고    scopus 로고
    • Mechanism-based enzyme inactivators
    • Purich DL ed Academic Press, San Diego
    • Silverman RB (1996) Mechanism-based enzyme inactivators, in Contemporary Enzyme Kinetics and Mechanisms (Purich DL ed) pp 291-334, Academic Press, San Diego.
    • (1996) Contemporary Enzyme Kinetics and Mechanisms , pp. 291-334
    • Silverman, R.B.1
  • 30
    • 0344069675 scopus 로고    scopus 로고
    • Expression of cytochrome P450 2A6 in Escherichia coli: Purification, spectral and catalytic characterization and preparation of polyclonal antibodies
    • Soucek P (1999) Expression of cytochrome P450 2A6 in Escherichia coli: purification, spectral and catalytic characterization and preparation of polyclonal antibodies. Arch Biochem Biophys 370:190-200.
    • (1999) Arch Biochem Biophys , vol.370 , pp. 190-200
    • Soucek, P.1
  • 31
    • 0034665139 scopus 로고    scopus 로고
    • Human cytochrome P 450 CYP2A13: Predominant expression in the respiratory tract and in high efficiency metabolic activation of a tobacco-specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone
    • Su T, Bao Z, Zhang QY, Smith TJ, Hong JY, and Ding X (2000) Human cytochrome P 450 CYP2A13: predominant expression in the respiratory tract and in high efficiency metabolic activation of a tobacco-specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone. Cancer Res 60:5074-5079.
    • (2000) Cancer Res , vol.60 , pp. 5074-5079
    • Su, T.1    Bao, Z.2    Zhang, Q.Y.3    Smith, T.J.4    Hong, J.Y.5    Ding, X.6
  • 32
    • 0034575202 scopus 로고    scopus 로고
    • The biotransformation of nitrogen containing xenobiotics to lactams
    • Vickers S and Polsky SL (2000) The biotransformation of nitrogen containing xenobiotics to lactams. Curr Drug Metab 1:357-389.
    • (2000) Curr Drug Metab , vol.1 , pp. 357-389
    • Vickers, S.1    Polsky, S.L.2
  • 33
    • 1842736562 scopus 로고    scopus 로고
    • The mechanism-based inactivation of P450 2B4 by tert-butyl 1-methyl-2-propynyl ether: Structural determination of the adducts to the P450 heme
    • von Weymarn LB, Blobaum AL, and Hollenberg PF (2004) The mechanism-based inactivation of P450 2B4 by tert-butyl 1-methyl-2-propynyl ether: structural determination of the adducts to the P450 heme. Arch Biochem Biophys 425:95-105.
    • (2004) Arch Biochem Biophys , vol.425 , pp. 95-105
    • Von Weymarn, L.B.1    Blobaum, A.L.2    Hollenberg, P.F.3
  • 34
    • 0033401703 scopus 로고    scopus 로고
    • N-Nitrosobenzylmethylamine α-hydroxylation and coumarin 7-hydroxylation by rat esophageal microsomes and cytochrome P450 2A3 and 2A6 enzymes
    • von Weymarn LB, Felicia ND, Ding X, and Murphy SE (1999) N-Nitrosobenzylmethylamine α-hydroxylation and coumarin 7-hydroxylation by rat esophageal microsomes and cytochrome P450 2A3 and 2A6 enzymes. Chem Res Toxicol 12:1254-1261.
    • (1999) Chem Res Toxicol , vol.12 , pp. 1254-1261
    • Von Weymarn, L.B.1    Felicia, N.D.2    Ding, X.3    Murphy, S.E.4
  • 36
    • 0025346271 scopus 로고
    • The role of cytochromes P-450 and flavin-containing monooxygenase in the metabolism of (S)-nicotine by rabbit lung
    • Williams DE, Shigenaga MK, and Castagnoli N (1990) The role of cytochromes P-450 and flavin-containing monooxygenase in the metabolism of (S)-nicotine by rabbit lung. Drug Metab Dispos 18:418-428.
    • (1990) Drug Metab Dispos , vol.18 , pp. 418-428
    • Williams, D.E.1    Shigenaga, M.K.2    Castagnoli, N.3
  • 37
    • 12144265866 scopus 로고    scopus 로고
    • Cytochrome P450 2A-catalyzed metabolic activation of structurally similar carcinogenic nitrosamines: N′-nitrosonornicotine enantiomers, N-nitrosopiperidine and N-nitrosopyrrolidine
    • Wong HL, Murphy SE, and Hecht SS (2005a) Cytochrome P450 2A-catalyzed metabolic activation of structurally similar carcinogenic nitrosamines: N′-nitrosonornicotine enantiomers, N-nitrosopiperidine and N-nitrosopyrrolidine. Chem Res Toxicol 18:61-69.
    • (2005) Chem Res Toxicol , vol.18 , pp. 61-69
    • Wong, H.L.1    Murphy, S.E.2    Hecht, S.S.3
  • 38
    • 21144437181 scopus 로고    scopus 로고
    • Metabolic activation of the tobacco carcinogen 4-(methylnitrosamino)-(3- pyridyl)-1-butanone by cytochrome P450 2A13 in human fetal nasal microsomes
    • Wong HL, Zhang X, Zhang QY, Gu J, Ding X, Hecht SS, and Murphy SE (2005b) Metabolic activation of the tobacco carcinogen 4-(methylnitrosamino)-(3- pyridyl)-1-butanone by cytochrome P450 2A13 in human fetal nasal microsomes. Chem Res Toxicol 18:913-918.
    • (2005) Chem Res Toxicol , vol.18 , pp. 913-918
    • Wong, H.L.1    Zhang, X.2    Zhang, Q.Y.3    Gu, J.4    Ding, X.5    Hecht, S.S.6    Murphy, S.E.7
  • 39
    • 0032931833 scopus 로고    scopus 로고
    • Roles of CYP2A6 and CYP2B6 in nicotine C-oxidation by human liver microsomes
    • Yamazaki H, Inoue K, Hashimoto M, and Shimada T (1999) Roles of CYP2A6 and CYP2B6 in nicotine C-oxidation by human liver microsomes. Arch Toxicol 73:65-70.
    • (1999) Arch Toxicol , vol.73 , pp. 65-70
    • Yamazaki, H.1    Inoue, K.2    Hashimoto, M.3    Shimada, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.