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Volumn 9, Issue 1, 2014, Pages

Accelerated repair and reduced mutagenicity of DNA damage induced by cigarette smoke in human bronchial cells transfected with E.coli formamidopyrimidine DNA glycosylase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); CIGARETTE SMOKE; DNA FORMAMIDOPYRIMIDINE GLYCOSYLASE; ENHANCED GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; PLASMID VECTOR;

EID: 84900444945     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0087984     Document Type: Article
Times cited : (8)

References (40)
  • 2
    • 84871856571 scopus 로고    scopus 로고
    • Personal habits and indoor combustions. Volume 100 E. A review of human carcinogens
    • IARC Working Group on the Evaluation of Carcinogenic Risks to Humans
    • IARC Working Group on the Evaluation of Carcinogenic Risks to Humans (2012) Personal habits and indoor combustions. volume 100 E. A review of human carcinogens. IARC Monogr Eval Carcinog Risks Hum 100: 1-538.
    • (2012) IARC Monogr Eval Carcinog Risks Hum , vol.100 , pp. 1-538
  • 3
    • 9644252940 scopus 로고    scopus 로고
    • Genotoxicity of tobacco smoke and tobacco smoke condensate: A review
    • DeMarini DM (2004) Genotoxicity of tobacco smoke and tobacco smoke condensate: A review. Mutat Res 567: 447-474.
    • (2004) Mutat Res , vol.567 , pp. 447-474
    • DeMarini, D.M.1
  • 4
    • 84884859723 scopus 로고    scopus 로고
    • 7,8-Dihydroxyflavone suppresses oxidative stress-induced base modification in DNA via induction of the repair enzyme 8-oxoguanine DNA glycosylase-1
    • Kim KC, Lee IK, Kang KA, Cha JW, Cho SJ, et al. (2013) 7,8-dihydroxyflavone suppresses oxidative stress-induced base modification in DNA via induction of the repair enzyme 8-oxoguanine DNA glycosylase-1. Biomed Res Int 2013: 863720.
    • (2013) Biomed Res Int , vol.2013 , pp. 863720
    • Kim, K.C.1    Lee, I.K.2    Kang, K.A.3    Cha, J.W.4    Cho, S.J.5
  • 5
    • 6344223490 scopus 로고    scopus 로고
    • Structural basis for the recognition of the FapydG lesion (2,6-diamino-4-hydroxy-5-formamidopyrimidine) by formamidopyrimidine-DNA glycosylase
    • DOI 10.1074/jbc.M405928200
    • Coste F, Ober M, Carell T, Boiteux S, Zelwer C, et al. (2004) Structural basis for the recognition of the FapydG lesion (2,6-diamino-4-hydroxy-5- formamidopyrimidine) by formamidopyrimidine-DNA glycosylase. J Biol Chem 279: 44074-44083. (Pubitemid 39390717)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.42 , pp. 44074-44083
    • Coste, F.1    Ober, M.2    Carell, T.3    Boiteux, S.4    Zelwer, C.5    Castaing, B.6
  • 7
    • 0031777550 scopus 로고    scopus 로고
    • Activity of Escherichia coli DNA-glycosylases on DNA damaged by methylating and ethylating agents and influence of 3-substituted adenine derivatives
    • DOI 10.1016/S0921-8777(98)00005-6, PII S0921877798000056
    • Tudek B, Van Zeeland AA, Kusmierek JT, Laval J (1998) Activity of escherichia coli DNA-glycosylases on DNA damaged by methylating and ethylating agents and influence of 3-substituted adenine derivatives. Mutat Res 407: 169-176. (Pubitemid 28241558)
    • (1998) Mutation Research - DNA Repair , vol.407 , Issue.2 , pp. 169-176
    • Tudek, B.1    VanZeeland, A.A.2    Kusmierek, J.T.3    Laval, J.4
  • 8
    • 0024347210 scopus 로고
    • Excision of the imidazole ring-opened form of N-2-aminofluorene-C(8)- guanine adduct in poly(dG-dC) by Escherichia coli formamidopyrimidine-DNA glycosylase
    • Boiteux S, Bichara M, Fuchs RP, Laval J (1989) Excision of the imidazole ring-opened form of N-2-aminofluorene-C(8)-guanine adduct in poly(dG-dC) by escherichia coli formamidopyrimidine-DNA glycosylase. Carcinogenesis 10: 1905-1909. (Pubitemid 19244868)
    • (1989) Carcinogenesis , vol.10 , Issue.10 , pp. 1905-1909
    • Boiteux, S.1    Bichara, M.2    Fuchs, R.P.P.3    Laval, J.4
  • 9
    • 0031407602 scopus 로고    scopus 로고
    • Fpg protein releases a ring-opened N-7 guanine adduct from DNA that has been modified by sulfur mustard
    • DOI 10.1093/carcin/18.5.1035
    • Li Q, Laval J, Ludlum DB (1997) Fpg protein releases a ring-opened N-7 guanine adduct from DNA that has been modified by sulfur mustard. Carcinogenesis 18: 1035-1038. (Pubitemid 28132351)
    • (1997) Carcinogenesis , vol.18 , Issue.5 , pp. 1035-1038
    • Li, Q.1    Laval, J.2    Ludlum, D.B.3
  • 10
    • 33646508777 scopus 로고    scopus 로고
    • Prophylaxis of oxidative DNA damage by formamidopyrimidine-DNA glycosylase
    • Frosina G (2006) Prophylaxis of oxidative DNA damage by formamidopyrimidine-DNA glycosylase. Int J Cancer 119: 1-7.
    • (2006) Int J Cancer , vol.119 , pp. 1-7
    • Frosina, G.1
  • 12
    • 0030614471 scopus 로고    scopus 로고
    • 2-terminal proline acts as a nucleophile in the glycosylase/AP-Lyase reaction catalyzed by Escherichia coli formamidopyrimidine- DNA glycosylase (Fpg) protein
    • DOI 10.1074/jbc.272.8.5335
    • Zharkov DO, Rieger RA, Iden CR, Grollman AP (1997) NH2-terminal proline acts as a nucleophile in the glycosylase/AP-lyase reaction catalyzed by escherichia coli formamidopyrimidine-DNA glycosylase (fpg) protein. J Biol Chem 272: 5335-5341. (Pubitemid 27090098)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.8 , pp. 5335-5341
    • Zharkov, D.O.1    Rieger, R.A.2    Iden, C.R.3    Grollman, A.P.4
  • 13
    • 0034616341 scopus 로고    scopus 로고
    • Role of the N-terminal proline residue in the catalytic activities of the Escherichia coli Fpg protein
    • DOI 10.1074/jbc.275.14.9924
    • Sidorkina OM, Laval J (2000) Role of the N-terminal proline residue in the catalytic activities of the escherichia coli fpg protein. J Biol Chem 275: 9924-9929. (Pubitemid 30202037)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 9924-9929
    • Sidorkina, O.M.1    Laval, J.2
  • 14
    • 75149174615 scopus 로고    scopus 로고
    • Defective repair of 5-hydroxy-29-deoxycytidine in cockayne syndrome cells and its complementation by escherichia coli formamidopyrimidine DNA glycosylase and endonuclease III
    • Foresta M, Ropolo M, Degan P, Pettinati I, Kow YW, et al. (2010) Defective repair of 5-hydroxy-29-deoxycytidine in cockayne syndrome cells and its complementation by escherichia coli formamidopyrimidine DNA glycosylase and endonuclease III. Free Radic Biol Med 48: 681-690.
    • (2010) Free Radic Biol Med , vol.48 , pp. 681-690
    • Foresta, M.1    Ropolo, M.2    Degan, P.3    Pettinati, I.4    Kow, Y.W.5
  • 15
    • 0031985891 scopus 로고    scopus 로고
    • Impairment of proliferating cell nuclear antigen-dependent apurinic/apyrimidinic site repair on linear DNA
    • DOI 10.1074/jbc.273.2.898
    • Biade S, Sobol RW, Wilson SH, Matsumoto Y (1998) Impairment of proliferating cell nuclear antigen-dependent apurinic/apyrimidinic site repair on linear DNA. J Biol Chem 273: 898-902. (Pubitemid 28049182)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.2 , pp. 898-902
    • Biade, S.1    Sobol, R.W.2    Wilson, S.H.3    Matsumoto, Y.4
  • 16
    • 0031419674 scopus 로고    scopus 로고
    • Mutation rate at the hprt locus in human cancer cell lines with specific mismatch repair-gene defects
    • DOI 10.1093/carcin/18.1.1
    • Glaab WE, Tindall KR (1997) Mutation rate at the hprt locus in human cancer cell lines with specific mismatch repair-gene defects. Carcinogenesis 18: 1-8. (Pubitemid 28134609)
    • (1997) Carcinogenesis , vol.18 , Issue.1 , pp. 1-8
    • Glaab, W.E.1    Tindall, K.R.2
  • 17
    • 0030786171 scopus 로고    scopus 로고
    • Modulation of the potency of promutagens and direct acting mutagens in bacteria by inhibitors of the multidrug resistance mechanism
    • De Flora S, Camoirano A, Cartiglia C, Ferguson L (1997) Modulation of the potency of promutagens and direct acting mutagens in bacteria by inhibitors of the multidrug resistance mechanism. Mutagenesis 12: 431-435. (Pubitemid 27503897)
    • (1997) Mutagenesis , vol.12 , Issue.6 , pp. 431-435
    • De Flora, S.1    Camoirano, A.2    Cartiglia, C.3    Ferguson, L.4
  • 18
    • 0032869451 scopus 로고    scopus 로고
    • Formation and persistence of nucleotide alterations in rats exposed whole-body to environmental cigarette smoke
    • DOI 10.1093/carcin/20.8.1499
    • Izzotti A, Bagnasco M, D'Agostini F, Cartiglia C, Lubet RA, et al. (1999) Formation and persistence of nucleotide alterations in rats exposed whole-body to environmental cigarette smoke. Carcinogenesis 20: 1499-1505. (Pubitemid 29385436)
    • (1999) Carcinogenesis , vol.20 , Issue.8 , pp. 1499-1505
    • Izzotti, A.1    Bagnasco, M.2    D'Agostini, F.3    Cartiglia, C.4    Lubet, R.A.5    Kelloff, G.J.6    De Flora, S.7
  • 19
    • 0023919963 scopus 로고
    • A simple technique for quantitation of low levels of DNA damage in individual cells
    • Singh NP, McCoy MT, Tice RR, Schneider EL (1988) A simple technique for quantitation of low levels of DNA damage in individual cells. Exp Cell Res 175: 184-191.
    • (1988) Exp Cell Res , vol.175 , pp. 184-191
    • Singh, N.P.1    McCoy, M.T.2    Tice, R.R.3    Schneider, E.L.4
  • 20
    • 0034681444 scopus 로고    scopus 로고
    • Distinct repair activities of human 7,8-dihydro-8-oxoguanine DNA glycosylase and formamidopyrimidine DNA glycosylase for formamidopyrimidine and 7,8-dihydro-8-oxoguanine
    • DOI 10.1074/jbc.275.7.4956
    • Asagoshi K, Yamada T, Terato H, Ohyama Y, Monden Y, et al. (2000) Distinct repair activities of human 7,8-dihydro-8-oxoguanine DNA glycosylase and formamidopyrimidine DNA glycosylase for formamidopyrimidine and 7,8-dihydro-8-oxoguanine. J Biol Chem 275: 4956-4964. (Pubitemid 30108891)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.7 , pp. 4956-4964
    • Asagoshi, K.1    Yamada, T.2    Terato, H.3    Ohyama, Y.4    Monden, Y.5    Arai, T.6    Nishimura, S.7    Aburatani, H.8    Lindahl, T.9    Ide, H.10
  • 22
    • 79957885201 scopus 로고    scopus 로고
    • Increased resistance to oxidative DNA damage of trabecular meshwork cells by E. Coli FPG gene transfection
    • Foresta M, Frosina G, Sacca SC, Cartiglia C, Longobardi M, et al. (2011) Increased resistance to oxidative DNA damage of trabecular meshwork cells by E. coli FPG gene transfection. Free Radic Res 45: 751-758.
    • (2011) Free Radic Res , vol.45 , pp. 751-758
    • Foresta, M.1    Frosina, G.2    Sacca, S.C.3    Cartiglia, C.4    Longobardi, M.5
  • 23
    • 0034601704 scopus 로고    scopus 로고
    • Stable and unstable transgene integration sites in the human genome: Extinction of the green fluorescent protein transgene in K562 cells
    • Migliaccio AR, Bengra C, Ling J, Pi W, Li C, et al. (2000) Stable and unstable transgene integration sites in the human genome: Extinction of the green fluorescent protein transgene in K562 cells. Gene 256: 197-214.
    • (2000) Gene , vol.256 , pp. 197-214
    • Migliaccio, A.R.1    Bengra, C.2    Ling, J.3    Pi, W.4    Li, C.5
  • 24
    • 0035394724 scopus 로고    scopus 로고
    • Retrovirus-mediated expression of the base excision repair proteins, formamidopyrimidine DNA glycosylase or human oxoguanine DNA glycosylase, protects hematopoietic cells from N,N′,N″- triethylenethiophosphoramide (thioTEPA)-induced toxicity in vitro and in vivo
    • Kobune M, Xu Y, Baum C, Kelley MR, Williams DA (2001) Retrovirus-mediated expression of the base excision repair proteins, formamidopyrimidine DNA glycosylase or human oxoguanine DNA glycosylase, protects hematopoietic cells from N,N′,N″-triethylenethiophosphoramide (thioTEPA)-induced toxicity in vitro and in vivo. Cancer Res 61: 5116-5125. (Pubitemid 32681543)
    • (2001) Cancer Research , vol.61 , Issue.13 , pp. 5116-5125
    • Kobune, M.1    Xu, Y.2    Baum, C.3    Kelley, M.R.4    Williams, D.A.5
  • 25
    • 33745116918 scopus 로고    scopus 로고
    • Expression of the E. coli Fpg protein in CHO cells lowers endogenous oxypurine clustered damage levels and decreases accumulation of endogenous Hprt mutations
    • DOI 10.1080/03235400500301190
    • Paul S, Gros L, Laval J, Sutherland BM (2006) Expression of the E. coli fpg protein in CHO cells lowers endogenous oxypurine clustered damage levels and decreases accumulation of endogenous hprt mutations. Environ Mol Mutagen 47: 311-319. (Pubitemid 43900283)
    • (2006) Environmental and Molecular Mutagenesis , vol.47 , Issue.5 , pp. 311-319
    • Paul, S.1    Gros, L.2    Laval, J.3    Sutherland, B.M.4
  • 26
    • 0029761401 scopus 로고    scopus 로고
    • Increased resistance to N,N',N''-triethylenethiophosphoramide (thiotepa) in cells expressing the Escherichia coli formamidopyrimidine-DNA glycosylase
    • Gill RD, Cussac C, Souhami RL, Laval F (1996) Increased resistance to N,N′,N″ -triethylenethiophosphoramide (thiotepa) in cells expressing the escherichia coli formamidopyrimidine-DNA glycosylase. Cancer Res 56: 3721-3724. (Pubitemid 26272019)
    • (1996) Cancer Research , vol.56 , Issue.16 , pp. 3721-3724
    • Gill, R.D.1    Cussac, C.2    Souhami, R.L.3    Laval, F.4
  • 27
    • 0035122915 scopus 로고    scopus 로고
    • Protection of mammalian cells against chemotherapeutic agents thiotepa, 1,3-N,N′-bis(2-chloroethyl)-N-nitrosourea, and mafosfamide using the DNA base excision repair genes Fpg and alpha-hOgg1: Implications for protective gene therapy applications
    • Xu Y, Hansen WK, Rosenquist TA, Williams DA, Limp-Foster M, et al. (2001) Protection of mammalian cells against chemotherapeutic agents thiotepa, 1,3-N,N′-bis(2-chloroethyl)-N-nitrosourea, and mafosfamide using the DNA base excision repair genes fpg and alpha-hOgg1: Implications for protective gene therapy applications. J Pharmacol Exp Ther 296: 825-831. (Pubitemid 32187354)
    • (2001) Journal of Pharmacology and Experimental Therapeutics , vol.296 , Issue.3 , pp. 825-831
    • Xu, Y.1    Hansen, W.K.2    Rosenquist, T.A.3    Williams, D.A.4    Limp-Foster, M.5    Kelley, M.R.6
  • 28
    • 34447324079 scopus 로고    scopus 로고
    • Nuclear localization of enhanced green fluorescent protein homomultimers
    • DOI 10.1016/j.ab.2007.05.025, PII S0003269707003399
    • Seibel NM, Eljouni J, Nalaskowski MM, Hampe W (2007) Nuclear localization of enhanced green fluorescent protein homomultimers. Anal Biochem 368: 95-99. (Pubitemid 47058434)
    • (2007) Analytical Biochemistry , vol.368 , Issue.1 , pp. 95-99
    • Seibel, N.M.1    Eljouni, J.2    Nalaskowski, M.M.3    Hampe, W.4
  • 30
    • 0021760535 scopus 로고
    • Two rotameric forms of open ring 7-methylguanine are present in alkylated polynucleotides
    • Boiteux S, Belleney J, Roques BP, Laval J (1984) Two rotameric forms of open ring 7-methylguanine are present in alkylated polynucleotides. Nucleic Acids Res 12: 5429-5439.
    • (1984) Nucleic Acids Res , vol.12 , pp. 5429-5439
    • Boiteux, S.1    Belleney, J.2    Roques, B.P.3    Laval, J.4
  • 32
    • 0027146414 scopus 로고
    • 4-ethenocytosine, and 4-amino-5-(imidazol- 2-yl)imidazole
    • DOI 10.1021/bi00210a031
    • Basu AK, Wood ML, Niedernhofer LJ, Ramos LA, Essigmann JM (1993) Mutagenic and genotoxic effects of three vinyl chloride-induced DNA lesions: 1,N6-ethenoadenine, 3,N4-ethenocytosine, and 4-amino-5-(imidazol-2-yl)imidazole. Biochemistry 32: 12793-12801. (Pubitemid 24005879)
    • (1993) Biochemistry , vol.32 , Issue.47 , pp. 12793-12801
    • Basu, A.K.1    Wood, M.L.2    Niedernhofer, L.J.3    Ramos, L.A.4    Essigmann, J.M.5
  • 33
    • 0035877833 scopus 로고    scopus 로고
    • The pyrimidine ring-opened derivative of 1,N6-ethenoadenine is excised from DNA by the escherichia coli fpg and nth proteins
    • Speina E, Ciesla JM, Wojcik J, Bajek M, Kusmierek JT, et al. (2001) The pyrimidine ring-opened derivative of 1,N6-ethenoadenine is excised from DNA by the escherichia coli fpg and nth proteins. J Biol Chem 276: 21821-21827.
    • (2001) J Biol Chem , vol.276 , pp. 21821-21827
    • Speina, E.1    Ciesla, J.M.2    Wojcik, J.3    Bajek, M.4    Kusmierek, J.T.5
  • 34
    • 0028916180 scopus 로고
    • Inhibition by N-acetylcysteine of carcinogen-DNA adducts in the tracheal epithelium of rats exposed to cigarette smoke
    • Izzotti A, Balansky R, Scatolini L, Rovida A, De Flora S (1995) Inhibition by N-acetylcysteine of carcinogen-DNA adducts in the tracheal epithelium of rats exposed to cigarette smoke. Carcinogenesis 16: 669-672.
    • (1995) Carcinogenesis , vol.16 , pp. 669-672
    • Izzotti, A.1    Balansky, R.2    Scatolini, L.3    Rovida, A.4    De Flora, S.5
  • 35
    • 71549164074 scopus 로고    scopus 로고
    • MKP1 repression is required for the chemosensitizing effects of NF-kappaB and PI3K inhibitors to cisplatin in non-small cell lung cancer
    • Cortes-Sempere M, Chattopadhyay S, Rovira A, Rodriguez-Fanjul V, Belda-Iniesta C, et al. (2009) MKP1 repression is required for the chemosensitizing effects of NF-kappaB and PI3K inhibitors to cisplatin in non-small cell lung cancer. Cancer Lett 286: 206-216.
    • (2009) Cancer Lett , vol.286 , pp. 206-216
    • Cortes-Sempere, M.1    Chattopadhyay, S.2    Rovira, A.3    Rodriguez-Fanjul, V.4    Belda-Iniesta, C.5
  • 36
    • 67349142331 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-akt signaling in pulmonary carcinoid cells
    • Pitt SC, Chen H, Kunnimalaiyaan M (2009) Phosphatidylinositol 3-kinase-akt signaling in pulmonary carcinoid cells. J Am Coll Surg 209: 82-88.
    • (2009) J Am Coll Surg , vol.209 , pp. 82-88
    • Pitt, S.C.1    Chen, H.2    Kunnimalaiyaan, M.3
  • 37
    • 84882855823 scopus 로고    scopus 로고
    • Lung cancer stem cells: Progress and prospects
    • Lundin A, Driscoll B (2013) Lung cancer stem cells: Progress and prospects. Cancer Lett 338: 89-93.
    • (2013) Cancer Lett , vol.338 , pp. 89-93
    • Lundin, A.1    Driscoll, B.2
  • 38
    • 0028801762 scopus 로고
    • Overexpression of N-methylpurine-DNA glycosylase in chinese hamster ovary cells renders them more sensitive to the production of chromosomal aberrations by methylating agents - A case of imbalanced DNA repair
    • Coquerelle T, Dosch J, Kaina B (1995) Overexpression of N-methylpurine-DNA glycosylase in chinese hamster ovary cells renders them more sensitive to the production of chromosomal aberrations by methylating agents-a case of imbalanced DNA repair. Mutat Res 336: 9-17.
    • (1995) Mutat Res , vol.336 , pp. 9-17
    • Coquerelle, T.1    Dosch, J.2    Kaina, B.3
  • 39
    • 0345620782 scopus 로고    scopus 로고
    • Overexpression of DNA polymerase beta: A genomic instability enhancer process
    • Canitrot Y, Frechet M, Servant L, Cazaux C, Hoffmann JS (1999) Overexpression of DNA polymerase beta: A genomic instability enhancer process. FASEB J 13: 1107-1111. (Pubitemid 29249737)
    • (1999) FASEB Journal , vol.13 , Issue.9 , pp. 1107-1111
    • Canitrot, Y.1    Frechet, M.2    Servant, L.3    Cazaux, C.4    Hoffmann, J.-S.5
  • 40
    • 0028556986 scopus 로고
    • Expression of the E. coli fpg gene in mammalian cells reduces the mutagenicity of gamma-rays
    • Laval F (1994) Expression of the E. coli fpg gene in mammalian cells reduces the mutagenicity of gamma-rays. Nucleic Acids Res 22: 4943-4946.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4943-4946
    • Laval, F.1


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