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Volumn 3, Issue 4, 1997, Pages 245-250

Bioactivation of lapachol responsible for DNA scission by NADPH-cytochrome P450 reductase

Author keywords

Active oxygen; Bioactivation; DNA scission; Lapachol; NADPH cytochrome P450 reductase; Quinone reduction

Indexed keywords

LAPACHOL; PHENOBARBITAL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE FERRIHEMOPROTEIN REDUCTASE;

EID: 0030847714     PISSN: 13826689     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1382-6689(97)00019-7     Document Type: Article
Times cited : (36)

References (30)
  • 1
    • 0018194637 scopus 로고
    • A general mechanism for microsomal activation of quinone anticancer agents to free radicals
    • Bachur, N.R., Cordon, S.L., Gee, M.V., 1978. A general mechanism for microsomal activation of quinone anticancer agents to free radicals. Cancer Res. 38, 1745.
    • (1978) Cancer Res. , vol.38 , pp. 1745
    • Bachur, N.R.1    Cordon, S.L.2    Gee, M.V.3
  • 2
    • 0019457695 scopus 로고
    • Reduction of adriamycin to a semiquinone-free radical by NADPH cytochrome P-450 reductase produces DNA cleavage in a reaction mediated by molecular oxygen
    • Berlin, V., Haseltine, W.A., 1981. Reduction of adriamycin to a semiquinone-free radical by NADPH cytochrome P-450 reductase produces DNA cleavage in a reaction mediated by molecular oxygen. J. Biol. Chem. 256, 4747.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4747
    • Berlin, V.1    Haseltine, W.A.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utiliting the principle of protein-dye binding
    • Bradford, M.M., 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utiliting the principle of protein-dye binding. Anal. Biochem. 72, 248.
    • (1976) Anal. Biochem. , vol.72 , pp. 248
    • Bradford, M.M.1
  • 4
    • 0024407187 scopus 로고
    • Biochemistry of oxygen toxicity
    • Cadenas, E., 1989. Biochemistry of oxygen toxicity. Ann. Rev. Biochem. 58, 79.
    • (1989) Ann. Rev. Biochem. , vol.58 , pp. 79
    • Cadenas, E.1
  • 5
    • 0026567982 scopus 로고
    • NAD(P)H (quinone acceptor) oxidoreductase (DT-diaphorase) two-electron reduction of anthraquinone-based antitumour agents and generation of hydroxyl radicals
    • Fisher, G.R., Gutierrez, P.L., Oldcorne, M.A., Patterson, L.H., 1992. NAD(P)H (quinone acceptor) oxidoreductase (DT-diaphorase) two-electron reduction of anthraquinone-based antitumour agents and generation of hydroxyl radicals. Biochem. Pharmacol. 43, 575.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 575
    • Fisher, G.R.1    Gutierrez, P.L.2    Oldcorne, M.A.3    Patterson, L.H.4
  • 7
    • 0027732229 scopus 로고
    • Cytochrome P450 2B1-mediated one-electron reduction of adriamycin: A study with rat liver microsomes and purified enzymes
    • Goeptar, A.R., te Koppele, J.M., Lamme, E.K., Piqué, J.M., Vermeulen, N.P.E., 1993. cytochrome P450 2B1-mediated one-electron reduction of adriamycin: A study with rat liver microsomes and purified enzymes. Mol. Pharmacol. 44, 1267.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 1267
    • Goeptar, A.R.1    Te Koppele, J.M.2    Lamme, E.K.3    Piqué, J.M.4    Vermeulen, N.P.E.5
  • 9
    • 0018582229 scopus 로고
    • Inhibition of the iron-catalyzed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine
    • Gutteride, J.C., Richmond, R., Halliwell, B., 1979. Inhibition of the iron-catalyzed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine. Biochem. J. 184, 469.
    • (1979) Biochem. J. , vol.184 , pp. 469
    • Gutteride, J.C.1    Richmond, R.2    Halliwell, B.3
  • 10
    • 0017920930 scopus 로고
    • Effects of fatty acids on superoxide radical generation in leukocytes
    • Kakinuma, K., Minakami, S., 1978. Effects of fatty acids on superoxide radical generation in leukocytes. Biochim. Biophys. Acta 538, 50.
    • (1978) Biochim. Biophys. Acta , vol.538 , pp. 50
    • Kakinuma, K.1    Minakami, S.2
  • 11
    • 0022573017 scopus 로고
    • Overview of enzyme systems involved in bioreduction of drugs and in redox cycling
    • Kappus, H., 1986. Overview of enzyme systems involved in bioreduction of drugs and in redox cycling. Biochem. Pharmacol. 35, 1.
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 1
    • Kappus, H.1
  • 12
    • 0020385188 scopus 로고
    • Generation of hydroxyl radical by anticancer quinone drugs, carbazilquinone, mitomycin C, aclacinomycin A and adriamycin, in the presence of NADPH-cytochrome P-450 reductase
    • Komiyama, T., Kikuchi, T., Sugiura, Y., 1982. Generation of hydroxyl radical by anticancer quinone drugs, carbazilquinone, mitomycin C, aclacinomycin A and adriamycin, in the presence of NADPH-cytochrome P-450 reductase. Biochem. Pharmacol. 31, 3651.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 3651
    • Komiyama, T.1    Kikuchi, T.2    Sugiura, Y.3
  • 13
    • 0025756894 scopus 로고
    • Hydroxyl radical mediated demethylenation of (methylenedioxy)phenyl compounds
    • Kumagai, Y., Lin, L.Y., Schmitz, D.A., Cho, A.K., 1991. Hydroxyl radical mediated demethylenation of (methylenedioxy)phenyl compounds. Chem. Res. Toxicol. 4, 330.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 330
    • Kumagai, Y.1    Lin, L.Y.2    Schmitz, D.A.3    Cho, A.K.4
  • 14
    • 0028122583 scopus 로고
    • An efficient method for purification of cuprozinc superoxide dismutase from bovine erythrocytes
    • Kumagai, Y., Shinyashiki, M., Sun, G.F., Shimojo, N., Sagai, M., 1994a. An efficient method for purification of cuprozinc superoxide dismutase from bovine erythrocytes. Experimentia 50, 373.
    • (1994) Experimentia , vol.50 , pp. 373
    • Kumagai, Y.1    Shinyashiki, M.2    Sun, G.F.3    Shimojo, N.4    Sagai, M.5
  • 15
    • 0028069445 scopus 로고
    • Participation of cytochrome P450-2B and -2D isozymes in the demethylenation of methylenedioxy-methamphetamine enantiomers by rats
    • Kumagai, Y., Lin, L.Y., Hiratsuka, A., Narimatsu, S., Suzuki, T., Yamada, H., Oguri, K., Yoshimura, H., Cho, A.K., 1994b. Participation of cytochrome P450-2B and -2D isozymes in the demethylenation of methylenedioxy-methamphetamine enantiomers by rats. Mol. Pharmacol. 45, 359.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 359
    • Kumagai, Y.1    Lin, L.Y.2    Hiratsuka, A.3    Narimatsu, S.4    Suzuki, T.5    Yamada, H.6    Oguri, K.7    Yoshimura, H.8    Cho, A.K.9
  • 16
    • 0031034402 scopus 로고    scopus 로고
    • Generation of reactive oxygen species during interaction of diesel exhaust particles components with NADPH-cytochrome P450 reductase and involvement of the bioactivation in the DNA damage
    • Kumagai, Y., Arimoto, T., Shinyashiki, M., Shimojo, N., Nakai, Y., Yoshikawa, T., Sagai, M., 1997. Generation of reactive oxygen species during interaction of diesel exhaust particles components with NADPH-cytochrome P450 reductase and involvement of the bioactivation in the DNA damage, Free Rad. Biol. Med. 22, 479.
    • (1997) Free Rad. Biol. Med. , vol.22 , pp. 479
    • Kumagai, Y.1    Arimoto, T.2    Shinyashiki, M.3    Shimojo, N.4    Nakai, Y.5    Yoshikawa, T.6    Sagai, M.7
  • 17
    • 0016754801 scopus 로고
    • Comparison of in vitro drug metabolism by lung, liver, and kidney of several common laboratory species
    • Litterst, C.L., Mimnaugh, E.G., Reagan, R.L., Gram, T.E., 1975. Comparison of in vitro drug metabolism by lung, liver, and kidney of several common laboratory species. Drug Metab. Dispos. 3, 259.
    • (1975) Drug Metab. Dispos. , vol.3 , pp. 259
    • Litterst, C.L.1    Mimnaugh, E.G.2    Reagan, R.L.3    Gram, T.E.4
  • 19
    • 0026040838 scopus 로고
    • Molecular mechanism of quinone cytotoxicity
    • O'Brien, P.J., 1991. Molecular mechanism of quinone cytotoxicity. Chem.-Biol. Interact. 80, 1.
    • (1991) Chem.-Biol. Interact. , vol.80 , pp. 1
    • O'Brien, P.J.1
  • 20
    • 0021345793 scopus 로고
    • Reductive activation of mitomycin C and mitomycin C metabolites catalyzed by NADPH-cytochrome P-450 reductase and xanthine oxidase
    • Pan, S.-S., Andrews, P.A., Glover, C.J., 1984. Reductive activation of mitomycin C and mitomycin C metabolites catalyzed by NADPH-cytochrome P-450 reductase and xanthine oxidase. J. Biol. Chem. 259, 959.
    • (1984) J. Biol. Chem. , vol.259 , pp. 959
    • Pan, S.-S.1    Andrews, P.A.2    Glover, C.J.3
  • 21
    • 0021688186 scopus 로고
    • Lapachol inhibition of vitmin K epoxide reductase and vitamin K quinone reductase
    • Preusch, P.C., Suttie, J.W., 1984. Lapachol inhibition of vitmin K epoxide reductase and vitamin K quinone reductase. Arch. Biochem. Biophys. 234, 405.
    • (1984) Arch. Biochem. Biophys. , vol.234 , pp. 405
    • Preusch, P.C.1    Suttie, J.W.2
  • 22
    • 0022504974 scopus 로고
    • Lapachol inhibition of DT-diaphorase (NAD(P)H: Quinone dehydrogenase)
    • Preusch, P.C., 1986. Lapachol inhibition of DT-diaphorase (NAD(P)H: quinone dehydrogenase). Biochem. Biophys. Res. Commun. 137, 781.
    • (1986) Biochem. Biophys. Res. Commun. , vol.137 , pp. 781
    • Preusch, P.C.1
  • 23
    • 0024600028 scopus 로고
    • Sulfaquinoxaline inhibition of vitamin K epoxide and quinone reductase
    • Preusch, P.C., Hazelett, S.E., Lemasters, K.K., 1989. Sulfaquinoxaline inhibition of vitamin K epoxide and quinone reductase. Arch. Biochem. Biophys. 269, 18.
    • (1989) Arch. Biochem. Biophys. , vol.269 , pp. 18
    • Preusch, P.C.1    Hazelett, S.E.2    Lemasters, K.K.3
  • 24
    • 0022622807 scopus 로고
    • Generation of reactive oxygen radicals through bioactivation of mitomycin antibiotics
    • Pritsos, C.A., Sartorelli, A.C., 1986. Generation of reactive oxygen radicals through bioactivation of mitomycin antibiotics. Cancer Res. 46, 3528.
    • (1986) Cancer Res. , vol.46 , pp. 3528
    • Pritsos, C.A.1    Sartorelli, A.C.2
  • 25
    • 84863987739 scopus 로고
    • Recongnition and evaluation of lapachol as an antitumor agent
    • Rao, K.V., McBride, T.J., Oleson, J.J., 1968. Recongnition and evaluation of lapachol as an antitumor agent. Cancer Res. 28, 1952.
    • (1968) Cancer Res. , vol.28 , pp. 1952
    • Rao, K.V.1    McBride, T.J.2    Oleson, J.J.3
  • 26
    • 0026612119 scopus 로고
    • DT-Diaphorase and cancer chemotherapy
    • Riley, R., Workman, P., 1992. DT-Diaphorase and cancer chemotherapy. Biochem. Pharmacol. 43, 1657.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 1657
    • Riley, R.1    Workman, P.2
  • 27
    • 0028299381 scopus 로고
    • The mechanism of stimulation of NADPH oxidation during the mechanism-based inactivation of cytochrome P-450 2B1 by N-methylcabazole: Redox cycling and DNA scission
    • Shen, T., Hollenberg, P.F., 1994. The mechanism of stimulation of NADPH oxidation during the mechanism-based inactivation of cytochrome P-450 2B1 by N-methylcabazole: redox cycling and DNA scission. Chem. Res. Toxicol. 7, 231.
    • (1994) Chem. Res. Toxicol. , vol.7 , pp. 231
    • Shen, T.1    Hollenberg, P.F.2
  • 28
  • 29
    • 0023113250 scopus 로고
    • Role of hepatic microsomal and purified cytochrome P450 in the one-electron reduction of the quinoneimines and concomitant reduction of molecular oxygen
    • van de Straat, R., deVries, J., Vermeulen, N.P.E., 1987. Role of hepatic microsomal and purified cytochrome P450 in the one-electron reduction of the quinoneimines and concomitant reduction of molecular oxygen. Biochem. Pharmacol. 36, 613.
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 613
    • Van De Straat, R.1    DeVries, J.2    Vermeulen, N.P.E.3
  • 30
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P450) reductase purified by biospecific affinity chromatography
    • Yasukochi, Y., Masters, B.S.S., 1976. Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P450) reductase purified by biospecific affinity chromatography. J. Biol. Chem. 251, 5337.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5337
    • Yasukochi, Y.1    Masters, B.S.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.