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Volumn 584, Issue 15, 2010, Pages 3366-3369

The human xenobiotic-metabolizing enzyme arylamine N-acetyltransferase 1 (NAT1) is irreversibly inhibited by inorganic (Hg2+) and organic mercury (CH3Hg+): Mechanism and kinetics

Author keywords

Arylamine N acetyltransferase; Inhibition; Mercury; Xenobiotic metabolism

Indexed keywords

ACYLTRANSFERASE; MERCURY; METHYLMERCURY; N ACETYLTRANSFERASE 1; UNCLASSIFIED DRUG;

EID: 77955281589     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.06.022     Document Type: Article
Times cited : (12)

References (30)
  • 1
    • 0033675835 scopus 로고    scopus 로고
    • Pharmacogenetics of the arylamine N-acetyltransferases: a symposium in honor of Wendell W. Weber
    • Hein D., McQueen C., Grant D., Goodfellow G., Kadlubar F., Weber W. Pharmacogenetics of the arylamine N-acetyltransferases: a symposium in honor of Wendell W. Weber. Drug Metab. Dispos. 2000, 28:1425-1432.
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 1425-1432
    • Hein, D.1    McQueen, C.2    Grant, D.3    Goodfellow, G.4    Kadlubar, F.5    Weber, W.6
  • 3
    • 0033960051 scopus 로고    scopus 로고
    • Molecular genetics and epidemiology of the NAT1 and NAT2 acetylation polymorphisms
    • Hein D.W., et al. Molecular genetics and epidemiology of the NAT1 and NAT2 acetylation polymorphisms. Cancer Epidemiol. Biomarkers Prev. 2000, 9:29-42.
    • (2000) Cancer Epidemiol. Biomarkers Prev. , vol.9 , pp. 29-42
    • Hein, D.W.1
  • 4
    • 0028904406 scopus 로고
    • Acetylation of p-aminobenzoylglutamate, a folic acid catabolite, by recombinant human arylamine N-acetyltransferase and U937 cells
    • Minchin R.F. Acetylation of p-aminobenzoylglutamate, a folic acid catabolite, by recombinant human arylamine N-acetyltransferase and U937 cells. Biochem. J. 1995, 307:1-3.
    • (1995) Biochem. J. , vol.307 , pp. 1-3
    • Minchin, R.F.1
  • 6
    • 12444303338 scopus 로고    scopus 로고
    • Arylamine N-acetyltransferase-1 is highly expressed in breast cancers and conveys enhanced growth and resistance to etoposide in vitro
    • Adam P.J., et al. Arylamine N-acetyltransferase-1 is highly expressed in breast cancers and conveys enhanced growth and resistance to etoposide in vitro. Mol. Cancer Res. 2003, 1:826-835.
    • (2003) Mol. Cancer Res. , vol.1 , pp. 826-835
    • Adam, P.J.1
  • 7
    • 38049061726 scopus 로고    scopus 로고
    • Arylamine N-acetyltransferase 1 expression in breast cancer cell lines: a potential marker in estrogen receptor-positive tumors
    • Wakefield L., Robinson J., Long H., Ibbitt J.C., Cooke S., Hurst H.C., Sim E. Arylamine N-acetyltransferase 1 expression in breast cancer cell lines: a potential marker in estrogen receptor-positive tumors. Genes Chromosomes Cancer 2008, 47:118-126.
    • (2008) Genes Chromosomes Cancer , vol.47 , pp. 118-126
    • Wakefield, L.1    Robinson, J.2    Long, H.3    Ibbitt, J.C.4    Cooke, S.5    Hurst, H.C.6    Sim, E.7
  • 8
    • 77249105346 scopus 로고    scopus 로고
    • Small molecule inhibition of arylamine N-acetyltransferase Type I inhibits proliferation and invasiveness of MDA-MB-231 breast cancer cells
    • Tiang J.M., Butcher N.J., Minchin R.F. Small molecule inhibition of arylamine N-acetyltransferase Type I inhibits proliferation and invasiveness of MDA-MB-231 breast cancer cells. Biochem. Biophys. Res. Commun. 2010, 393:95-100.
    • (2010) Biochem. Biophys. Res. Commun. , vol.393 , pp. 95-100
    • Tiang, J.M.1    Butcher, N.J.2    Minchin, R.F.3
  • 9
    • 77953489818 scopus 로고    scopus 로고
    • Human arylamine N-acetyltransferase 1: a drug-metabolizing enzyme and a drug target?
    • Rodrigues-Lima F., Dairou J., Busi F., Dupret J.M. Human arylamine N-acetyltransferase 1: a drug-metabolizing enzyme and a drug target?. Curr. Drug Targets 2010, 11:759-766.
    • (2010) Curr. Drug Targets , vol.11 , pp. 759-766
    • Rodrigues-Lima, F.1    Dairou, J.2    Busi, F.3    Dupret, J.M.4
  • 10
    • 0038012890 scopus 로고    scopus 로고
    • Skeletal muscles express the xenobiotic-metabolizing enzyme arylamine N-acetyltransferase
    • Rodrigues-Lima F., et al. Skeletal muscles express the xenobiotic-metabolizing enzyme arylamine N-acetyltransferase. J. Histochem. Cytochem. 2003, 51:789-796.
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 789-796
    • Rodrigues-Lima, F.1
  • 11
    • 15744370426 scopus 로고    scopus 로고
    • The xenobiotic-metabolizing enzymes arylamine N-acetyltransferases (NAT) in human lens epithelial cells: inactivation by cellular oxidants and UVB-induced oxidative stress
    • Dairou J., Malecaze F., Dupret J.M., Rodrigues-Lima F. The xenobiotic-metabolizing enzymes arylamine N-acetyltransferases (NAT) in human lens epithelial cells: inactivation by cellular oxidants and UVB-induced oxidative stress. Mol. Pharmacol. 2005, 67:1299-1306.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1299-1306
    • Dairou, J.1    Malecaze, F.2    Dupret, J.M.3    Rodrigues-Lima, F.4
  • 12
    • 26444618665 scopus 로고    scopus 로고
    • Arylamine N-acetyltransferases: what we learn from genes and genomes
    • Boukouvala S., Fakis G. Arylamine N-acetyltransferases: what we learn from genes and genomes. Drug Metab. Rev. 2005, 37:511-564.
    • (2005) Drug Metab. Rev. , vol.37 , pp. 511-564
    • Boukouvala, S.1    Fakis, G.2
  • 14
    • 17444405238 scopus 로고    scopus 로고
    • Molecular and ionic mimicry and the transport of toxic metals
    • Bridges C.C., Zalups R.K. Molecular and ionic mimicry and the transport of toxic metals. Toxicol. Appl. Pharmacol. 2005, 204:274-308.
    • (2005) Toxicol. Appl. Pharmacol. , vol.204 , pp. 274-308
    • Bridges, C.C.1    Zalups, R.K.2
  • 16
    • 36749097280 scopus 로고    scopus 로고
    • Mechanism of inhibition of purified leaping mullet (Liza saliens) NADPH-cytochrome P450 reductase by toxic metals: aluminum and thallium
    • Bozcaarmutlu A., Arinc E. Mechanism of inhibition of purified leaping mullet (Liza saliens) NADPH-cytochrome P450 reductase by toxic metals: aluminum and thallium. J. Biochem. Mol. Toxicol. 2007, 21:340-347.
    • (2007) J. Biochem. Mol. Toxicol. , vol.21 , pp. 340-347
    • Bozcaarmutlu, A.1    Arinc, E.2
  • 17
    • 0032699707 scopus 로고    scopus 로고
    • Inhibition of soluble and microsomal epoxide hydrolase by zinc and other metals
    • Draper A.J., Hammock B.D. Inhibition of soluble and microsomal epoxide hydrolase by zinc and other metals. Toxicol. Sci. 1999, 52:26-32.
    • (1999) Toxicol. Sci. , vol.52 , pp. 26-32
    • Draper, A.J.1    Hammock, B.D.2
  • 18
    • 0035117028 scopus 로고    scopus 로고
    • Comparative study on the in vitro inhibitory effects of heavy metals on rabbit drug-metabolizing enzymes
    • Nakahama T., Inouye Y., Fukuhara M. Comparative study on the in vitro inhibitory effects of heavy metals on rabbit drug-metabolizing enzymes. J. Health Sci. 2001, 47:14-20.
    • (2001) J. Health Sci. , vol.47 , pp. 14-20
    • Nakahama, T.1    Inouye, Y.2    Fukuhara, M.3
  • 19
    • 0014082823 scopus 로고
    • N-Acetylation of drugs: isolation and properties of an N-acetyltransferase from rabbit liver
    • Weber W.W., Cohen S.N. N-Acetylation of drugs: isolation and properties of an N-acetyltransferase from rabbit liver. Mol. Pharmacol. 1967, 3:266-273.
    • (1967) Mol. Pharmacol. , vol.3 , pp. 266-273
    • Weber, W.W.1    Cohen, S.N.2
  • 20
    • 4444234103 scopus 로고    scopus 로고
    • Interpreting mercury in blood and urine of individual patients
    • Nuttall K.L. Interpreting mercury in blood and urine of individual patients. Ann. Clin. Lab. Sci. 2004, 34:235-250.
    • (2004) Ann. Clin. Lab. Sci. , vol.34 , pp. 235-250
    • Nuttall, K.L.1
  • 21
    • 0038782331 scopus 로고    scopus 로고
    • Reversible inhibition of the human xenobiotic-metabolizing enzyme arylamine N-acetyltransferase 1 by S-nitrosothiols
    • Dairou J., Atmane N., Dupret J.M., Rodrigues-Lima F. Reversible inhibition of the human xenobiotic-metabolizing enzyme arylamine N-acetyltransferase 1 by S-nitrosothiols. Biochem. Biophys. Res. Commun. 2003, 307:1059-1065.
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 1059-1065
    • Dairou, J.1    Atmane, N.2    Dupret, J.M.3    Rodrigues-Lima, F.4
  • 22
    • 0037023704 scopus 로고    scopus 로고
    • The C-terminus of arylamine N-acetyl transferase from Salmonella typhimurium controls enzymic activity
    • Mushtaq A., Payton M., Sim E. The C-terminus of arylamine N-acetyl transferase from Salmonella typhimurium controls enzymic activity. J. Biol. Chem. 2002, 277:12175-12181.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12175-12181
    • Mushtaq, A.1    Payton, M.2    Sim, E.3
  • 23
    • 0025967717 scopus 로고
    • Monomorphic and polymorphic human arylamine N-acetyltransferases: a comparison of liver isozymes and expressed products of two cloned genes
    • Grant D.M., Blum M., Beer M., Meyer U.A. Monomorphic and polymorphic human arylamine N-acetyltransferases: a comparison of liver isozymes and expressed products of two cloned genes. Mol. Pharmacol. 1991, 39:184-191.
    • (1991) Mol. Pharmacol. , vol.39 , pp. 184-191
    • Grant, D.M.1    Blum, M.2    Beer, M.3    Meyer, U.A.4
  • 25
    • 44249120547 scopus 로고    scopus 로고
    • Identification of the xenobiotic-metabolizing enzyme arylamine N-acetyltransferase 1 (NAT1) as a new target of cisplatin in breast cancer cells: molecular and cellular mechanisms of inhibition
    • Ragunathan N., Dairou J., Pluvinage B., Martins M., Petit E., Janel N., Dupret J.M., Rodrigues-Lima F. Identification of the xenobiotic-metabolizing enzyme arylamine N-acetyltransferase 1 (NAT1) as a new target of cisplatin in breast cancer cells: molecular and cellular mechanisms of inhibition. Mol. Pharmacol. 2008, 73:1761-1768.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1761-1768
    • Ragunathan, N.1    Dairou, J.2    Pluvinage, B.3    Martins, M.4    Petit, E.5    Janel, N.6    Dupret, J.M.7    Rodrigues-Lima, F.8
  • 27
    • 34247156315 scopus 로고    scopus 로고
    • Induction of reactive oxygen species and apoptosis in BEAS-2B cells by mercuric chloride
    • Park E.J., Park K. Induction of reactive oxygen species and apoptosis in BEAS-2B cells by mercuric chloride. Toxicol. In Vitro 2007, 21:789-794.
    • (2007) Toxicol. In Vitro , vol.21 , pp. 789-794
    • Park, E.J.1    Park, K.2
  • 28
    • 21244461430 scopus 로고    scopus 로고
    • Metabolism and bioactivation of toxicants in the lung. The in vitro cellular approach
    • Castell J.V., Donato M.T., Gomez-Lechon M.J. Metabolism and bioactivation of toxicants in the lung. The in vitro cellular approach. Exp. Toxicol. Pathol. 2005, 57(Suppl. 1):189-204.
    • (2005) Exp. Toxicol. Pathol. , vol.57 , Issue.SUPPL. 1 , pp. 189-204
    • Castell, J.V.1    Donato, M.T.2    Gomez-Lechon, M.J.3
  • 29
    • 0022366691 scopus 로고
    • Influence of mercury (II), cadmium (II), methylmercury, and phenylmercury on the kinetic properties of rat liver glutathione peroxidase
    • Bem E.M., Mailer K., Elson C.M. Influence of mercury (II), cadmium (II), methylmercury, and phenylmercury on the kinetic properties of rat liver glutathione peroxidase. Can. J. Biochem. Cell Biol. 1985, 63:1212-1216.
    • (1985) Can. J. Biochem. Cell Biol. , vol.63 , pp. 1212-1216
    • Bem, E.M.1    Mailer, K.2    Elson, C.M.3
  • 30
    • 0034190372 scopus 로고    scopus 로고
    • Regulation of redox glutathione levels and gene transcription in lung inflammation: therapeutic approaches
    • Rahman I., MacNee W. Regulation of redox glutathione levels and gene transcription in lung inflammation: therapeutic approaches. Free Radic. Biol. Med. 2000, 28:1405-1420.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1405-1420
    • Rahman, I.1    MacNee, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.