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Volumn 252, Issue 2, 2007, Pages 270-279

DNA adduct formation by the anticancer drug ellipticine in human leukemia HL-60 and CCRF-CEM cells

Author keywords

Cytochromes P450; DNA adduct; Ellipticine; Human leukemia HL 60 and CCRF CEM cells; Peroxidases

Indexed keywords

CYTOCHROME P450; ELLIPTICINE; MYELOPEROXIDASE;

EID: 34248662505     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2006.12.037     Document Type: Article
Times cited : (54)

References (27)
  • 1
    • 0035894174 scopus 로고    scopus 로고
    • The anticancer agent ellipticine on activation by cytochrome P450 forms covalent DNA adducts
    • Stiborová M., Bieler C.A., Wiessler M., and Frei E. The anticancer agent ellipticine on activation by cytochrome P450 forms covalent DNA adducts. Biochem. Pharmacol. 62 (2001) 675-684
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 675-684
    • Stiborová, M.1    Bieler, C.A.2    Wiessler, M.3    Frei, E.4
  • 2
    • 0023617219 scopus 로고
    • Multimodal action of antitumor agents on DNA: the ellipticine series
    • Auclair C. Multimodal action of antitumor agents on DNA: the ellipticine series. Arch. Biochem. Biophys. 259 (1987) 1-14
    • (1987) Arch. Biochem. Biophys. , vol.259 , pp. 1-14
    • Auclair, C.1
  • 3
    • 0027953894 scopus 로고
    • High-field NMR and restrained molecular modeling studies on a DNA heteroduplex containing a modified apurinic abasic site in the form of covalently linked 9-aminoellipticine
    • Singh M.P., Hill G.C., Peoch D., Rayner B., Inabach J.L., and Lown J.W. High-field NMR and restrained molecular modeling studies on a DNA heteroduplex containing a modified apurinic abasic site in the form of covalently linked 9-aminoellipticine. Biochemistry 33 (1994) 1085-10271
    • (1994) Biochemistry , vol.33 , pp. 1085-10271
    • Singh, M.P.1    Hill, G.C.2    Peoch, D.3    Rayner, B.4    Inabach, J.L.5    Lown, J.W.6
  • 4
    • 0026641695 scopus 로고
    • Ellipticine increases the superhelical density of intracellular SV40 DNA by intercalation
    • Chu Y., and Hsu M.T. Ellipticine increases the superhelical density of intracellular SV40 DNA by intercalation. Nucleic Acids Res. 20 (1992) 4033-4038
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4033-4038
    • Chu, Y.1    Hsu, M.T.2
  • 6
    • 0027104314 scopus 로고
    • Stimulation of topoisomerase II-mediated DNA cleavage by ellipticine derivatives: structure-activity relationships
    • Fossé P., René B., Charra M., Paoletti C., and Saucier J.M. Stimulation of topoisomerase II-mediated DNA cleavage by ellipticine derivatives: structure-activity relationships. Mol. Pharmacol. 42 (1992) 590-595
    • (1992) Mol. Pharmacol. , vol.42 , pp. 590-595
    • Fossé, P.1    René, B.2    Charra, M.3    Paoletti, C.4    Saucier, J.M.5
  • 7
    • 0029015354 scopus 로고
    • Topoisomerase II binds to ellipticine in the absence or presence of DNA. Characterization of enzyme-drug interactions by fluorescence spectroscopy
    • Froelich-Ammon S.J., Patchan M.W., Osheroff N., and Thompson R.B. Topoisomerase II binds to ellipticine in the absence or presence of DNA. Characterization of enzyme-drug interactions by fluorescence spectroscopy. J. Biol. Chem. 270 (1995) 14998-15004
    • (1995) J. Biol. Chem. , vol.270 , pp. 14998-15004
    • Froelich-Ammon, S.J.1    Patchan, M.W.2    Osheroff, N.3    Thompson, R.B.4
  • 8
    • 0029114860 scopus 로고
    • Inhibition of p53 protein phosphorylation by 9-hydroxyellipticine: a possible anticancer mechanism. Jpn
    • Ohashi M., Sugikawa E., and Nakanishi N. Inhibition of p53 protein phosphorylation by 9-hydroxyellipticine: a possible anticancer mechanism. Jpn. J. Cancer Res. 86 (1995) 819-829
    • (1995) J. Cancer Res. , vol.86 , pp. 819-829
    • Ohashi, M.1    Sugikawa, E.2    Nakanishi, N.3
  • 9
    • 0033452649 scopus 로고    scopus 로고
    • Mutant p53 mediated induction of cell cycle arrest and apoptosis at G1 phase by 9-hydroxyellipticine
    • Sugikawa E., Hosoi T., Yazaki N., Gamanuma N., Nakanishi N., and Ohashi M. Mutant p53 mediated induction of cell cycle arrest and apoptosis at G1 phase by 9-hydroxyellipticine. Anticancer Res. 19 (1999) 3099-3108
    • (1999) Anticancer Res. , vol.19 , pp. 3099-3108
    • Sugikawa, E.1    Hosoi, T.2    Yazaki, N.3    Gamanuma, N.4    Nakanishi, N.5    Ohashi, M.6
  • 10
    • 0029157845 scopus 로고
    • Protonophoric activity of ellipticine and isomers across the energy-transducing membrane of mitochondria
    • Schwaller M.A., Allard B., Lescot E., and Moreau F. Protonophoric activity of ellipticine and isomers across the energy-transducing membrane of mitochondria. J. Biol. Chem. 270 (1995) 22709-22713
    • (1995) J. Biol. Chem. , vol.270 , pp. 22709-22713
    • Schwaller, M.A.1    Allard, B.2    Lescot, E.3    Moreau, F.4
  • 11
    • 12244292673 scopus 로고    scopus 로고
    • Rat microsomes activating the anticancer drug ellipticine to species covalently binding to deoxyguanosine in DNA are a suitable model mimicking ellipticine bioactivation in humans
    • Stiborová M., Stiborová-Rupertová M., Bořek-Dohalská L., Wiessler M., and Frei E. Rat microsomes activating the anticancer drug ellipticine to species covalently binding to deoxyguanosine in DNA are a suitable model mimicking ellipticine bioactivation in humans. Chem. Res. Toxicol. 16 (2003) 38-47
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 38-47
    • Stiborová, M.1    Stiborová-Rupertová, M.2    Bořek-Dohalská, L.3    Wiessler, M.4    Frei, E.5
  • 12
    • 33845624680 scopus 로고    scopus 로고
    • Mammalian peroxidases activate anticancer drug ellipticine to intermediates forming deoxyguanosine adducts in DNA identical to those found in vivo and generated from 12-hydroxyellipticine and 13-hydroxyellipticine
    • Stiborová M., Poljaková J., Ryšlavá H., Drači{dotless}́nský M., Eckschlager T., and Frei E. Mammalian peroxidases activate anticancer drug ellipticine to intermediates forming deoxyguanosine adducts in DNA identical to those found in vivo and generated from 12-hydroxyellipticine and 13-hydroxyellipticine. Int. J. Cancer 120 (2007) 243-251
    • (2007) Int. J. Cancer , vol.120 , pp. 243-251
    • Stiborová, M.1    Poljaková, J.2    Ryšlavá, H.3    Dračínský, M.4    Eckschlager, T.5    Frei, E.6
  • 14
    • 1942422695 scopus 로고    scopus 로고
    • DNA adduct formation by the anticancer drug ellipticine and its hydroxy derivatives in human breast adenocarcinoma MCF-7 cells
    • Bořek-Dohalská L., Frei E., and Stiborová M. DNA adduct formation by the anticancer drug ellipticine and its hydroxy derivatives in human breast adenocarcinoma MCF-7 cells. Collect. Czech. Chem. Commun. 69 (2004) 603-615
    • (2004) Collect. Czech. Chem. Commun. , vol.69 , pp. 603-615
    • Bořek-Dohalská, L.1    Frei, E.2    Stiborová, M.3
  • 15
    • 0037099292 scopus 로고    scopus 로고
    • Covalent binding of the anticancer drug ellipticine to DNA in V79 cells transfected with human cytochrome P450 enzymes
    • Frei E., Bieler C.A., Arlt V.M., Wiessler M., and Stiborová M. Covalent binding of the anticancer drug ellipticine to DNA in V79 cells transfected with human cytochrome P450 enzymes. Biochem. Pharmacol. 64 (2002) 289-295
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 289-295
    • Frei, E.1    Bieler, C.A.2    Arlt, V.M.3    Wiessler, M.4    Stiborová, M.5
  • 20
    • 0037108678 scopus 로고    scopus 로고
    • Sudan I is a potential carcinogen for humans: evidence for its metabolic activation and detoxication by human recombinant cytochrome P450 1A1 and liver microsomes
    • Stiborová M., Marti{dotless}́nek V., Rýdlová H., Hodek P., and Frei E. Sudan I is a potential carcinogen for humans: evidence for its metabolic activation and detoxication by human recombinant cytochrome P450 1A1 and liver microsomes. Cancer Res. 62 (2002) 5678-5684
    • (2002) Cancer Res. , vol.62 , pp. 5678-5684
    • Stiborová, M.1    Martínek, V.2    Rýdlová, H.3    Hodek, P.4    Frei, E.5
  • 21
    • 0018787040 scopus 로고
    • NADPH-cytochrome c (P450) reductase: spectrophotometric and stopped flow kinetic studies on the formation of reduced flavoprotein intermediates
    • Yasukochi Y., Peterson J.A., and Masters B. NADPH-cytochrome c (P450) reductase: spectrophotometric and stopped flow kinetic studies on the formation of reduced flavoprotein intermediates. J. Biol. Chem. 254 (1979) 7097-7104
    • (1979) J. Biol. Chem. , vol.254 , pp. 7097-7104
    • Yasukochi, Y.1    Peterson, J.A.2    Masters, B.3
  • 22
    • 17644405812 scopus 로고    scopus 로고
    • Expression of cytochrome P450 1A1 and its contribution to oxidation of a potential human carcinogen 1-phenylazo-2-naphthol (Sudan I) in human livers
    • Stiborová M., Marti{dotless}́nek V., Rýdlová H., Koblas T., and Hodek P. Expression of cytochrome P450 1A1 and its contribution to oxidation of a potential human carcinogen 1-phenylazo-2-naphthol (Sudan I) in human livers. Cancer Lett. 220 (2005) 145-154
    • (2005) Cancer Lett. , vol.220 , pp. 145-154
    • Stiborová, M.1    Martínek, V.2    Rýdlová, H.3    Koblas, T.4    Hodek, P.5
  • 23
    • 0030803825 scopus 로고    scopus 로고
    • Comparative analysis of different permeabilization methods for the flow cytometry measurement of cytoplasmic myeloperoxidase and lysozyme in normal and leukemic cells
    • Lanza F., Latorraca A., Moretti S., Castagnari B., Ferrari L., and Castoldi G. Comparative analysis of different permeabilization methods for the flow cytometry measurement of cytoplasmic myeloperoxidase and lysozyme in normal and leukemic cells. Cytometry 30 (1997) 34-144
    • (1997) Cytometry , vol.30 , pp. 34-144
    • Lanza, F.1    Latorraca, A.2    Moretti, S.3    Castagnari, B.4    Ferrari, L.5    Castoldi, G.6
  • 25
    • 0026715860 scopus 로고
    • Molecular analysis of mutations induced by the intercalating agent ellipticine at the hisD3052 allele of Salmonella typhimurium TA98
    • DeMarini D.M., Abu-Shakra A., Gupta R., Hendee L.J., and Levine J.G. Molecular analysis of mutations induced by the intercalating agent ellipticine at the hisD3052 allele of Salmonella typhimurium TA98. Environ. Mol. Mutagenesis 20 (1992) 12-18
    • (1992) Environ. Mol. Mutagenesis , vol.20 , pp. 12-18
    • DeMarini, D.M.1    Abu-Shakra, A.2    Gupta, R.3    Hendee, L.J.4    Levine, J.G.5
  • 26
    • 0030958469 scopus 로고    scopus 로고
    • Multienzyme-mediated stable and transient multidrug resistance and collateral sensitivity induced by xenobiotics
    • Rekha G.K., and Sladek N.E. Multienzyme-mediated stable and transient multidrug resistance and collateral sensitivity induced by xenobiotics. Cancer Chemother. Pharmacol. 40 (1997) 215-224
    • (1997) Cancer Chemother. Pharmacol. , vol.40 , pp. 215-224
    • Rekha, G.K.1    Sladek, N.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.