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Volumn 653, Issue 1-2, 2008, Pages 14-22

Copper, zinc-superoxide dismutase enhances the mutagenicity in Salmonella typhimurium induced by 2-amino-6-methyldipyrido[1,2-a:3′,2′-d]imidazole

Author keywords

Copper, zinc superoxide dismutase; Cytosol; Mutagenicity; N hydroxylation; Salmonella typhimurium

Indexed keywords

AMINO ACID; AROMATIC AMINE; COPPER ZINC SUPEROXIDE DISMUTASE; HETEROCYCLIC AMINE; IMIDAZOLE DERIVATIVE; PROTEIN; 2 AMINO 6 METHYLDIPYRIDO(1,2 A 3',2' D)IMIDAZOLE; 2-AMINO-6-METHYLDIPYRIDO(1,2-A-3',2'-D)IMIDAZOLE; SUPEROXIDE DISMUTASE;

EID: 49649112708     PISSN: 13835718     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrgentox.2008.02.004     Document Type: Article
Times cited : (3)

References (36)
  • 1
    • 56149088024 scopus 로고    scopus 로고
    • Consensus report, The use of short- and medium-term tests for carcinogenesis and data on genetic effects in carcinogenic hazard evaluation, in: J.B. McGregor, J.M. Rice, S. Venitt (Eds.), IARC Scientific Publications No. 146, IARC, Lyon, 1999, pp. 1-18.
    • Consensus report, The use of short- and medium-term tests for carcinogenesis and data on genetic effects in carcinogenic hazard evaluation, in: J.B. McGregor, J.M. Rice, S. Venitt (Eds.), IARC Scientific Publications No. 146, IARC, Lyon, 1999, pp. 1-18.
  • 2
    • 0019800891 scopus 로고
    • Bacterial systems for carcinogenicity testing
    • Mohn G.R. Bacterial systems for carcinogenicity testing. Mutat. Res. 87 (1981) 191-210
    • (1981) Mutat. Res. , vol.87 , pp. 191-210
    • Mohn, G.R.1
  • 3
    • 0032617331 scopus 로고    scopus 로고
    • M. Waters, H. Stack, M. Jackson. Short-term tests for defining mutagenic carcinogens, in: J.B. McGregor, J.M. Rice, S. Venitt (Eds.), IARC Scientific Publications No. 146, IARC, Lyon, 1999, pp. 499-536.
    • M. Waters, H. Stack, M. Jackson. Short-term tests for defining mutagenic carcinogens, in: J.B. McGregor, J.M. Rice, S. Venitt (Eds.), IARC Scientific Publications No. 146, IARC, Lyon, 1999, pp. 499-536.
  • 4
    • 0034693731 scopus 로고    scopus 로고
    • The Ames Salmonella/microsome mutagenicity assay
    • Mortelmans K., and Zeiger E. The Ames Salmonella/microsome mutagenicity assay. Mutat. Res. 455 (2000) 29-60
    • (2000) Mutat. Res. , vol.455 , pp. 29-60
    • Mortelmans, K.1    Zeiger, E.2
  • 5
    • 0022566931 scopus 로고
    • Metabolic activation of mutagenic heterocyclic aromatic amines from protein pyrolysates
    • Kato R. Metabolic activation of mutagenic heterocyclic aromatic amines from protein pyrolysates. Crit. Rev. Toxicol. 16 (1986) 307-348
    • (1986) Crit. Rev. Toxicol. , vol.16 , pp. 307-348
    • Kato, R.1
  • 6
    • 19444383488 scopus 로고    scopus 로고
    • Genotoxicity of heat-processed foods
    • Jagerstad M., and Skog K. Genotoxicity of heat-processed foods. Mutat. Res. 574 (2005) 156-172
    • (2005) Mutat. Res. , vol.574 , pp. 156-172
    • Jagerstad, M.1    Skog, K.2
  • 7
    • 0019846241 scopus 로고
    • Influence of microsomal and cytosolic fractions from rat, mouse, and hamster liver on the mutagenicity of dimethylnitrosamine in the Salmonella plate incorporation assay
    • Prival M.J., and Mitchell V.D. Influence of microsomal and cytosolic fractions from rat, mouse, and hamster liver on the mutagenicity of dimethylnitrosamine in the Salmonella plate incorporation assay. Cancer Res. 41 (1981) 4361-4367
    • (1981) Cancer Res. , vol.41 , pp. 4361-4367
    • Prival, M.J.1    Mitchell, V.D.2
  • 8
    • 0023573141 scopus 로고
    • Bioactivation of N-nitrosopiperidine to mutagens: role of hepatic cytochrome P-450 proteins and contribution of cytosolic fraction
    • Ayrton A.D., Smith J.N., and Ioannides C. Bioactivation of N-nitrosopiperidine to mutagens: role of hepatic cytochrome P-450 proteins and contribution of cytosolic fraction. Carcinogenesis 8 (1987) 1691-1695
    • (1987) Carcinogenesis , vol.8 , pp. 1691-1695
    • Ayrton, A.D.1    Smith, J.N.2    Ioannides, C.3
  • 9
    • 0019782630 scopus 로고
    • Enhancement of N-hydroxy-2-aminofluorene bacterial mutagenicity by the soluble protein fraction from rat liver and partial purification of the enhancement activity
    • Saccone G.T., DasGupta B.R., and Pariza M.W. Enhancement of N-hydroxy-2-aminofluorene bacterial mutagenicity by the soluble protein fraction from rat liver and partial purification of the enhancement activity. Cancer Res. 41 (1981) 4600-4605
    • (1981) Cancer Res. , vol.41 , pp. 4600-4605
    • Saccone, G.T.1    DasGupta, B.R.2    Pariza, M.W.3
  • 10
    • 0019351421 scopus 로고
    • Enhancement of hepatic microsome-mediated bacterial mutagenesis by the rat liver soluble protein fraction
    • Saccone G.T., and Pariza M.W. Enhancement of hepatic microsome-mediated bacterial mutagenesis by the rat liver soluble protein fraction. Mutat. Res. 88 (1981) 135-145
    • (1981) Mutat. Res. , vol.88 , pp. 135-145
    • Saccone, G.T.1    Pariza, M.W.2
  • 11
    • 0020408878 scopus 로고
    • In vitro metabolism of o-aminoazotoluene and mutagenesis of Salmonella by the metabolites
    • Degawa M., Kanazawa C., and Hashimoto Y. In vitro metabolism of o-aminoazotoluene and mutagenesis of Salmonella by the metabolites. Carcinogenesis 3 (1982) 1113-1117
    • (1982) Carcinogenesis , vol.3 , pp. 1113-1117
    • Degawa, M.1    Kanazawa, C.2    Hashimoto, Y.3
  • 12
    • 0018837556 scopus 로고
    • Metabolic activation of mutagenic tryptophan pyrolysis products by rat liver microsomes
    • Ishii K., Yamazoe Y., Kamataki T., and Kato R. Metabolic activation of mutagenic tryptophan pyrolysis products by rat liver microsomes. Cancer Res. 40 (1980) 2596-2600
    • (1980) Cancer Res. , vol.40 , pp. 2596-2600
    • Ishii, K.1    Yamazoe, Y.2    Kamataki, T.3    Kato, R.4
  • 13
    • 0025802760 scopus 로고
    • Carcinogenicities of heterocyclic amines in cooked food
    • Ohgaki H., Takayama S., and Sugimura T. Carcinogenicities of heterocyclic amines in cooked food. Mutat. Res. 259 (1991) 399-410
    • (1991) Mutat. Res. , vol.259 , pp. 399-410
    • Ohgaki, H.1    Takayama, S.2    Sugimura, T.3
  • 14
    • 0023254223 scopus 로고
    • Metabolic activation and covalent binding to nucleic acids of carcinogenic heterocyclic amines from cooked foods and amino acid pyrolysates
    • Kato R., and Yamazoe Y. Metabolic activation and covalent binding to nucleic acids of carcinogenic heterocyclic amines from cooked foods and amino acid pyrolysates. Jpn. J. Cancer Res. 78 (1987) 297-311
    • (1987) Jpn. J. Cancer Res. , vol.78 , pp. 297-311
    • Kato, R.1    Yamazoe, Y.2
  • 15
    • 0032565512 scopus 로고    scopus 로고
    • Chemical and biological factors affecting mutagen potency
    • Colvin M.E., Hatch F.T., and Felton J.S. Chemical and biological factors affecting mutagen potency. Mutat. Res. 400 (1998) 479-492
    • (1998) Mutat. Res. , vol.400 , pp. 479-492
    • Colvin, M.E.1    Hatch, F.T.2    Felton, J.S.3
  • 16
    • 1642321287 scopus 로고    scopus 로고
    • Possibility of the involvement of 9H-pyrido[3,4-b]indole (norharman) in carcinogenesis via inhibition of cytochrome P450-related activities and intercalation to DNA
    • Nii H. Possibility of the involvement of 9H-pyrido[3,4-b]indole (norharman) in carcinogenesis via inhibition of cytochrome P450-related activities and intercalation to DNA. Mutat. Res. 541 (2003) 123-136
    • (2003) Mutat. Res. , vol.541 , pp. 123-136
    • Nii, H.1
  • 17
    • 0017669854 scopus 로고
    • Purification of glutathione S-transferases from human liver by glutathione affinity chromatography
    • Simons P.C., and VanderJagt D.L. Purification of glutathione S-transferases from human liver by glutathione affinity chromatography. Anal. Biochem. 82 (1977) 334-341
    • (1977) Anal. Biochem. , vol.82 , pp. 334-341
    • Simons, P.C.1    VanderJagt, D.L.2
  • 18
    • 0027500351 scopus 로고
    • Binding of human xanthine oxidase to sulphated glycosaminoglycans on the endotherial-cell surface
    • Adachi T., Fukushima T., Usami Y., and Hirano K. Binding of human xanthine oxidase to sulphated glycosaminoglycans on the endotherial-cell surface. Biochem. J. 289 (1993) 523-527
    • (1993) Biochem. J. , vol.289 , pp. 523-527
    • Adachi, T.1    Fukushima, T.2    Usami, Y.3    Hirano, K.4
  • 19
    • 0020420450 scopus 로고
    • Modification of DNA with potent mutacarcinogenic 2-amino-6-methyldipyrido[1,2-a:3′,2′-d]imidazole isolated from a glutamic acid pyrolysate: structure of the modified nucleic acid base and initial chemical event caused by the mutagen
    • Hashimoto Y., Shudo K., and Okamoto T. Modification of DNA with potent mutacarcinogenic 2-amino-6-methyldipyrido[1,2-a:3′,2′-d]imidazole isolated from a glutamic acid pyrolysate: structure of the modified nucleic acid base and initial chemical event caused by the mutagen. J. Am. Chem. Soc. 104 (1982) 7636-7640
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 7636-7640
    • Hashimoto, Y.1    Shudo, K.2    Okamoto, T.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0014691242 scopus 로고
    • Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein)
    • McCord J.M., and Fridovich I. Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244 (1969) 6049-6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 24
    • 0020533372 scopus 로고
    • Revised methods for the Salmonella mutagenicity test
    • Maron D.M., and Ames M.N. Revised methods for the Salmonella mutagenicity test. Mutat. Res. 113 (1983) 172-215
    • (1983) Mutat. Res. , vol.113 , pp. 172-215
    • Maron, D.M.1    Ames, M.N.2
  • 25
    • 0019868837 scopus 로고
    • Metabolic activation of glutamic acid pyrolysis product, 2-amino-6-methyldipyrido[1,2-a:3′,2′-d]imidazole and 2-amino-dipyrido[1,2-a:3′,2′-d]imidazole, by purified cytochrome P-450
    • Ishii K., Yamazoe Y., Kamataki T., and Kato R. Metabolic activation of glutamic acid pyrolysis product, 2-amino-6-methyldipyrido[1,2-a:3′,2′-d]imidazole and 2-amino-dipyrido[1,2-a:3′,2′-d]imidazole, by purified cytochrome P-450. Chem. -Biol. Interact. 38 (1981) 1-13
    • (1981) Chem. -Biol. Interact. , vol.38 , pp. 1-13
    • Ishii, K.1    Yamazoe, Y.2    Kamataki, T.3    Kato, R.4
  • 26
    • 4243336240 scopus 로고    scopus 로고
    • Superoxide dismutase-applications and relevance to human diseases
    • Noor R., Mittal S., and Iqbal J. Superoxide dismutase-applications and relevance to human diseases. Med. Sci. Monit. 8 (2002) 210-215
    • (2002) Med. Sci. Monit. , vol.8 , pp. 210-215
    • Noor, R.1    Mittal, S.2    Iqbal, J.3
  • 27
    • 0031910337 scopus 로고    scopus 로고
    • NAD(P)H:quinone oxidoreductase 1 reduces the mutagenicity of DNA caused by NADPH:P450 reductase-activated metabolites of benzo(a)pyrene quinones
    • Joseph P., and Jaiswal A.K. NAD(P)H:quinone oxidoreductase 1 reduces the mutagenicity of DNA caused by NADPH:P450 reductase-activated metabolites of benzo(a)pyrene quinones. Br. J. Cancer 77 (1998) 709-719
    • (1998) Br. J. Cancer , vol.77 , pp. 709-719
    • Joseph, P.1    Jaiswal, A.K.2
  • 28
    • 0030596091 scopus 로고    scopus 로고
    • Mutagenicity of dihydroxybenzenes and dihydroxynaphthalenes for Ames Salmonella tester strains
    • Hakura A., Tsutsui Y., Mochida H., Sugihara Y., Mikami T., and Sagami F. Mutagenicity of dihydroxybenzenes and dihydroxynaphthalenes for Ames Salmonella tester strains. Mutat. Res. 371 (1996) 293-299
    • (1996) Mutat. Res. , vol.371 , pp. 293-299
    • Hakura, A.1    Tsutsui, Y.2    Mochida, H.3    Sugihara, Y.4    Mikami, T.5    Sagami, F.6
  • 29
    • 0029073961 scopus 로고
    • Effects of antioxidants on fiber mutagenesis
    • Hei T.K., He Z.Y., and Suzuki K. Effects of antioxidants on fiber mutagenesis. Carcinogenesis 16 (1995) 1573-1578
    • (1995) Carcinogenesis , vol.16 , pp. 1573-1578
    • Hei, T.K.1    He, Z.Y.2    Suzuki, K.3
  • 30
    • 0027203076 scopus 로고
    • Antimutagenic action of superoxide dismutase on sodium azide- and nitrosoguanidine-induced mutagenesis in Salmonella typhimurium TA1535
    • Vorob'eva L.I., Cherdyntseva T.A., Aver'ianov A.A., and Abilev S.K. Antimutagenic action of superoxide dismutase on sodium azide- and nitrosoguanidine-induced mutagenesis in Salmonella typhimurium TA1535. Genetika 29 (1993) 760-767
    • (1993) Genetika , vol.29 , pp. 760-767
    • Vorob'eva, L.I.1    Cherdyntseva, T.A.2    Aver'ianov, A.A.3    Abilev, S.K.4
  • 31
    • 0027191832 scopus 로고
    • Mutagenesis in Escherichia coli K-12 mutants defective in superoxide dismutase or catalase
    • Prieto-Alamo M.J., Abril N., and Pueyo C. Mutagenesis in Escherichia coli K-12 mutants defective in superoxide dismutase or catalase. Carcinogenesis 14 (1993) 237-244
    • (1993) Carcinogenesis , vol.14 , pp. 237-244
    • Prieto-Alamo, M.J.1    Abril, N.2    Pueyo, C.3
  • 32
    • 0026541681 scopus 로고
    • N-methyl-N′-nitro-N-nitrosoguanidine-induced light emission in Chinese hamster cell cultures: correlation with enhancement of chromosomal aberrations
    • Kimura M., Roschger P., Kobayashi M., Kimura S., and Inaba H. N-methyl-N′-nitro-N-nitrosoguanidine-induced light emission in Chinese hamster cell cultures: correlation with enhancement of chromosomal aberrations. Mutat. Res. 281 (1992) 215-220
    • (1992) Mutat. Res. , vol.281 , pp. 215-220
    • Kimura, M.1    Roschger, P.2    Kobayashi, M.3    Kimura, S.4    Inaba, H.5
  • 33
    • 0023692347 scopus 로고
    • Superoxide dismutase-mediated reversible conversion of 3-hydroxyamino-1-methyl-5H-pyrido[4,3-b]indole, the N-hydroxy derivative of Trp-P-2, into its nitroso derivative
    • Hiramoto K., Negishi K., Namba T., Katsu T., and Hayatsu H. Superoxide dismutase-mediated reversible conversion of 3-hydroxyamino-1-methyl-5H-pyrido[4,3-b]indole, the N-hydroxy derivative of Trp-P-2, into its nitroso derivative. Carcinogenesis 9 (1988) 2003-2008
    • (1988) Carcinogenesis , vol.9 , pp. 2003-2008
    • Hiramoto, K.1    Negishi, K.2    Namba, T.3    Katsu, T.4    Hayatsu, H.5
  • 35
    • 0021103046 scopus 로고
    • Mechanism of activation of proximate mutagens in Ames' tester strains: the acetyl-CoA dependent enzyme in Salmonella typhimurium TA98 deficient in TA98/1,8-DNP6 catalyzes DNA-binding as the cause of mutagenicity
    • Saito K., Yamazoe Y., Kamataki T., and Kato R. Mechanism of activation of proximate mutagens in Ames' tester strains: the acetyl-CoA dependent enzyme in Salmonella typhimurium TA98 deficient in TA98/1,8-DNP6 catalyzes DNA-binding as the cause of mutagenicity. Biochem. Biophys. Res. Commun. 116 (1983) 141-147
    • (1983) Biochem. Biophys. Res. Commun. , vol.116 , pp. 141-147
    • Saito, K.1    Yamazoe, Y.2    Kamataki, T.3    Kato, R.4
  • 36
    • 0028126786 scopus 로고
    • N-hydroxyarylamine O-acetyltransferase of Salmonella typhimurium: proposal for a common catalytic mechanism of arylamine acetyltransferase enzymes
    • Watanabe M., Igarashi T., Kaminuma T., Sofuni T., and Nohmi T. N-hydroxyarylamine O-acetyltransferase of Salmonella typhimurium: proposal for a common catalytic mechanism of arylamine acetyltransferase enzymes. Environ. Health Perspect. 102 Suppl. 6 (1994) 83-89
    • (1994) Environ. Health Perspect. , vol.102 , Issue.SUPPL. 6 , pp. 83-89
    • Watanabe, M.1    Igarashi, T.2    Kaminuma, T.3    Sofuni, T.4    Nohmi, T.5


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