메뉴 건너뛰기




Volumn 49, Issue 2, 1995, Pages 127-140

Antioxidant and prooxidant functions of DT-diaphorase in quinone metabolism

Author keywords

antioxidants; chemotherapy; DT diaphorase; free radicals; glutathione; NAD(P)H:(quinone acceptor) oxidoreductase; Superoxide dismutase

Indexed keywords

1,4 BENZOQUINONE; 1,4 NAPHTHOQUINONE DERIVATIVE; ALKYLATING AGENT; ANTHRAQUINONE DERIVATIVE; ANTINEOPLASTIC AGENT; DIAZIRIDINYLBENZOQUINONE DERIVATIVE; GLUCURONOSYLTRANSFERASE; HYDROQUINONE; MITOMYCIN C; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG;

EID: 0028889025     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(94)00333-5     Document Type: Article
Times cited : (262)

References (140)
  • 1
    • 0002117840 scopus 로고
    • DT-diaphorase: A historical review
    • (1987) Chem Scr , vol.27 A , pp. 1-13
    • Ernster1
  • 7
    • 0002783125 scopus 로고
    • On the mechanisms of one- and twoelectron transfer by flavin enzymes
    • (1987) Chem Scr , vol.27 A , pp. 31-36
    • Iyanagi1
  • 10
    • 0025027027 scopus 로고
    • Advances in research on DT-diaphorase—Catalytic properties, regulation of activity and significance in the detoxication of foreign compounds
    • (1990) Kitasato Arch Exp Med , vol.63 , pp. 11-30
    • Horie1
  • 14
  • 16
    • 0027052362 scopus 로고
    • Enhancement of xanthine dehydrogenase mediated mitomycin C metabolism by dicumarol
    • (1992) Cancer Res , vol.52 , pp. 6936-6939
    • Gustafson1    Pritsos2
  • 17
    • 0026699018 scopus 로고
    • Inhibition of mouse glutathione transferases and glutathione peroxidase II by dicumarol and other ligands
    • (1992) Biochem Pharmacol , vol.44 , pp. 921-925
    • Mays1    Benson2
  • 19
    • 0026499189 scopus 로고
    • Identification of a glycine-rich sequence as an NAD(P)H-binding site and tyrosine 128 as a dicumarol-binding site in rat liver NAD(P)H: quinone oxidoreductase by site-directed mutagenesis
    • (1992) J Biol Chem , vol.267 , pp. 22298-22304
    • Ma1    Cui2    Xiao3    Lu4    Yanc5
  • 20
    • 0025907971 scopus 로고
    • Synthesis of the photoaffinity probe 3-(p-azidobenzyl)-4-hydroxycoumarin and identification of the dicumarol binding site in rat liver NAD(P)H: quinone reductase (EC 1.6.99.2)
    • (1991) J Biol Chem , vol.266 , pp. 4789-4797
    • Myszka1    Swenson2
  • 21
    • 0027219704 scopus 로고
    • Inhibition of NAD(P)H: quinone acceptor oxidoreductase by flavones. A structure-activity study
    • (1993) Arch Biochem Biophys , vol.302 , pp. 72-77
    • Chen1    Hwang2    Deng3
  • 23
    • 0025598310 scopus 로고
    • Role of DT-diaphorase in the cytotoxicity of menadione and 4-nitroquinoline-1-oxide in cultured mammalian fibroblastic cells
    • (1990) Cancer Lett , vol.55 , pp. 195-199
    • Tsuda1
  • 24
    • 0026278905 scopus 로고
    • Purified NAD(P)Hquinone oxidoreductase enhances the mutagenicity of dinitropyrenes in vitro
    • (1991) J Biochem Toxicol , vol.6 , pp. 277-282
    • Hajos1    Winston2
  • 26
    • 0020440918 scopus 로고
    • The metabolism of menadione (2-methyl-1,4-naphthoquinone) by isolated hepatocytes. A study of the implications of oxidative stress in intact cells
    • (1982) J Biol Chem , vol.257 , pp. 12419-12425
    • Thor1    Smith2    Hartzell3    Bellomo4    Jewell5    Orrenius6
  • 33
    • 0024253422 scopus 로고
    • Characterization of a glutathione conjugate of the 1,4-benzosemiquinone-free radical formed in rat hepatocytes
    • (1988) J Biol Chem , vol.263 , pp. 17981-17986
    • Rao1    Takahashi2    Mason3
  • 34
    • 0024237151 scopus 로고
    • Sequential oxidation and glutathione addition to 1,4-benzoquinone. Correlation of velocity with increased glutathione substitution
    • (1988) Mol Pharmacol , vol.34 , pp. 829-836
    • Lau1    Hill2    Highet3    Monks4
  • 35
    • 0026787040 scopus 로고
    • DNA strand scission and free radical production in menadione-treated cells. Correlation with cytotoxicity and role of NADPH quinone acceptor oxidoreductase
    • (1992) J Biol Chem , vol.267 , pp. 2474-2479
    • Nutter1    Ngo2    Fisher3    Gutierrez4
  • 36
    • 0027419480 scopus 로고
    • Does lung NAD(P)H: quinone reductase (DT-diaphorase) play an antioxidant enzyme role in protection from hyperoxia?
    • (1993) Biochim Biophys Acta , vol.1156 , pp. 275-282
    • Whitney1    Frank2
  • 41
    • 0023944408 scopus 로고
    • Redox cycling and sulfhydryl arylation: Their relative importance in the mechanism of quinone cytotoxicity to isolated hepatocytes
    • (1988) Chem Biol Interact , vol.65 , pp. 157-163
    • Gant1    Rao2    Mason3    Cohen4
  • 44
    • 0021825326 scopus 로고
    • Formation of benzo[a]pyrene-3,6-quinol mono- and diglucuronides in rat liver microsomes
    • (1985) Arch Biochem Biophys , vol.240 , pp. 226-235
    • Lind1
  • 46
  • 48
    • 0027055783 scopus 로고
    • Cell-specific metabolism in mouse bone marrow stroma: Studies of activation and detoxification of benzene metabolites
    • (1992) Mol Pharmacol , vol.42 , pp. 1118-1125
    • Ganousis1    Goon2    Zyglewska3    Wu4    Ross5
  • 50
    • 37049239562 scopus 로고
    • Carcinogenic aromatic hydrocarbons: Special vulnerability of rats
    • (1965) Science , vol.147 , pp. 1153-1154
    • Muggins1    Ford2    Jensen3
  • 52
    • 0024826410 scopus 로고
    • Rat liver NAD(P)H: quinone reductase. Regulation of quinone reductase gene expression by planar aromatic compounds and determination of the exon structure of the quinone reductase structural gene
    • (1989) J Biol Chem , vol.264 , pp. 21793-21797
    • Bayney1    Morton2    Favreau3    Pickett4
  • 53
    • 0025637578 scopus 로고
    • Induction of glutathione transferase and NAD(P)H: quinone reductase by fumaric acid derivatives in rodent cells and tissues
    • (1990) Cancer Res , vol.50 , pp. 7871-7875
    • Spencer1    Wilczak2    Talalay3
  • 54
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stress-inducible genes: Direct activation by oxidation
    • (1990) Science , vol.248 , pp. 189-194
    • Storz1    Tartaglia2    Ames3
  • 56
    • 0024498044 scopus 로고
    • DT-diaphorase-catalysed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates. Effect of substituents on autoxidation rates
    • (1989) Biochem J , vol.257 , pp. 561-571
    • Buffinton1    Öllinger2    Brunmark3    Cadenas4
  • 61
    • 0009516229 scopus 로고
    • Oxidation by Superoxide anion of catechols, ascorbic acid, dihydrophenazine, and reduced flavins to their respective anion radicals. A common mechanism with a sequential proton-hydrogen atom transfer
    • (1985) J Org Chem , vol.50 , pp. 1409-1412
    • Sawyer1    Calderwood2    Johlman3    Wilkins4
  • 62
    • 0018875204 scopus 로고
    • Relationship of the singleelectron reduction potential of quinones to their reduction by flavoproteins
    • (1980) Biochem Pharmacol , vol.29 , pp. 2567-2572
    • Powis1    Appel2
  • 63
    • 0027390265 scopus 로고
    • The one-electron reduction potential of several substrates can be related to their reduction rates by cytochrome P450 reductase
    • (1993) Biochim Biophys Acta , vol.1161 , pp. 73-78
    • Butler1    Hoey2
  • 64
    • 0024535437 scopus 로고
    • Intermediates in the aerobic autoxidation of 6-hydroxydopamine: Relative importance under different reaction conditions
    • (1989) Free Radic Biol Med , vol.6 , pp. 271-284
    • Gee1    Davison2
  • 66
    • 0024854643 scopus 로고
    • 3+-induced neurotoxicity of dopamine: Prevention of quinone-derived oxygen toxicity by DT-diaphorase and Superoxide dismutase
    • (1989) Chem Biol Interact , vol.72 , pp. 309-324
    • Segura-Aguilar1    Lind2
  • 68
    • 0027291424 scopus 로고
    • Induction of antioxidant enzymes and DT-diaphorase in human blood mononuclear cells by light stress
    • (1993) Arch Biochem Biophys , vol.305 , pp. 247-251
    • Alvarez1    Boveris2
  • 74
    • 0021323995 scopus 로고
    • Free radical formation from anthracycline antitumour. Agents and model systemsĪ. Model naphthoquinones and anthraquinones
    • (1984) Biochem Pharmacol , vol.33 , pp. 379-385
    • Dodd1    Mukherjee2
  • 75
  • 76
    • 0026767519 scopus 로고
    • Reductive metabolism of diaziquone (AZQ) in the S9 fraction of MCF-7 cells. II. Enhancement of the alkylating activity of AZQ by NAD(P)H: quinone-acceptor oxidoreductase (DT-diaphorase)
    • (1992) Biochem Pharmacol , vol.44 , pp. 1625-1635
    • Fisher1    Donis2    Gutierrez3
  • 77
    • 0026348793 scopus 로고
    • Free radical formation and DNA strand breakage during metabolism of diaziquone by NAD(P)H quinone-acceptor oxidoreductase (DT-diaphorase) and NAD(P)Hcytochrome c reductase
    • (1991) Free Radic Biol Med , vol.11 , pp. 597-607
    • Fisher1    Gutierrez2
  • 78
    • 0025799550 scopus 로고
    • The reductive metabolism of diaziquone (AZQ) in the S9 fraction of MCF-7 cells: Free radical formation and NAD(P)H: quinoneacceptor oxidoreductase (DT-diaphorase) activity
    • (1991) Free Radic Biol Med , vol.10 , pp. 359-370
    • Fisher1    Gutierrez2
  • 79
    • 0026795829 scopus 로고
    • Thiol oxidation coupled to DT-diaphorase-catalysed reduction of diaziquone. Reductive and oxidative pathways of diaziquone semiquinone modulated by glutathione and superoxide dismutase.
    • (1992) Biochem J , vol.286 , pp. 481-490
    • Ordoñez1    Cadenas2
  • 80
    • 0025318270 scopus 로고
    • Differential cytotoxicity of diaziquone toward Chinese hamster ovary cells under hypoxic and aerobic conditions
    • (1990) Cancer Res , vol.50 , pp. 1516-1520
    • O'Brien1    Kaul2    Rauth3
  • 81
    • 0024418918 scopus 로고
    • Diaziquone-induced cytotoxicity in isolated rat hepatocytes
    • (1989) Cancer Res , vol.49 , pp. 5550-5554
    • Silva1    O'Brien2
  • 82
    • 0026689273 scopus 로고
    • Modulation of trenimon-induced cytotoxicity by DT-diaphorase in isolated rat hepatocytes under aerobic versus hypoxic conditions
    • (1992) Cancer Res , vol.52 , pp. 3015-3021
    • Silva1    Ramakrishna Rao2    O'Brien3
  • 84
    • 0016804540 scopus 로고
    • Studies on the reaction mechanism of DT-diaphorase. Intermediary plateau and trough regions in the initial velocity vs substrate concentration curves
    • (1975) Arch Biochem Biophys , vol.169 , pp. 568-576
    • Hollander1    Bartfai2    Gatt3
  • 85
    • 0019578706 scopus 로고
    • Cytochrome c reduction by semiquinone radicals can be indirectly inhibited by Superoxide dismutase
    • (1981) Arch Biochem Biophys , vol.209 , pp. 159-167
    • Winterbourn1
  • 86
  • 87
    • 0028304021 scopus 로고
    • One- and two-electron activation of 2-methyl-1,4-naphthoquinone bioreductive alkylating agents. Kinetic studies, free radical production, thiol oxidation, and DNA strand break formation
    • (1994) Biochem J , vol.301 , pp. 21-30
    • Giulivi1    Cadenas2
  • 90
    • 0023641132 scopus 로고
    • Mechanisms of toxicity of 2- and 5-hydroxy-1,4-naphthoquinone; Absence of a role for redox cycling in the toxicity of 2-hydroxy-1,4-naphthoquinone to isolated hepatocytes
    • (1987) J Appl Toxicol , vol.7 , pp. 123-129
    • d'Arcy Doherty1    Rodgers2    Cohen3
  • 91
    • 0027441799 scopus 로고
    • In vitro cytotoxicities of 1,4-naphthoquinone and hydroxylated 1,4-naphthoquinones to replicating cells
    • (1993) J Appl Toxicol , vol.13 , pp. 353-358
    • Babich1    Stern2
  • 92
  • 94
    • 0026567982 scopus 로고
    • NAD(P) (quinone acceptor) oxidoreductase (DT-diaphorase-mediated two-electron reduction of anthraquinone-based antitumour agents and generation of hydroxyl radicals
    • (1992) Biochem Pharmacol , vol.43 , pp. 575-585
    • Fisher1    Gutierrez2    Oldcorne3    Patterson4
  • 97
    • 0021104497 scopus 로고
    • Hepatic low-level chemiluminescence during redox cycling of menadione and the menadione-glutathione conjugate: Relation to glutathione and NAD(P)H:quinone reductase (DT-diaphorase) activity
    • (1982) Archives of Biochemistry and Biophysics , vol.224 , pp. 568-578
    • Wefers1    Sies2
  • 98
    • 0025980713 scopus 로고
    • The toxicity of menadione (2-methyl-l,4-naphthoquinone) and two thioether conjugates studied with isolated renal epithelial cells
    • (1991) Arch Biochem Biophys , vol.285 , pp. 187-196
    • Brown1    Dulik2    Jones3
  • 100
    • 0023761518 scopus 로고
    • 2-Bromo(diglutathion-S-yl) hydroquinone nephrotoxicity. Physiological, biochemical and electrochemical determinants
    • (1988) Mol Pharmacol , vol.34 , pp. 492-500
    • Monks1    Highet2    Lau3
  • 102
    • 0027093458 scopus 로고
    • The effects of 2,3,5(triglutathion-S-yl) hydroquinone on renal mitochondrial respiratory function in vivo and in vitro: Possible role in cytotoxicity
    • (1992) Toxicol Appl Pharmacol , vol.117 , pp. 165-171
    • Hill1    Monks2    Lau3
  • 105
    • 0024349246 scopus 로고
    • Interconversion of NAD(H) to NADP(H). A cellular response to quinone-induced oxidative stress in isolated hepatocytes
    • (1989) Biochem Pharmacol , vol.38 , pp. 2631-2637
    • Stubberfield1    Cohen2
  • 108
    • 0025776518 scopus 로고
    • Glutathionyl- and hydroxyl radical formation coupled to the redox transitions of 1,4-naphthoquinone bioreductive alkylating agents during glutathione twoelectron reductive addition
    • (1991) Arch Biochem Biophys , vol.288 , pp. 386-396
    • Goin1    Gibson2    McCay3    Cadenas4
  • 119
    • 0028097816 scopus 로고
    • Unusually marked hypoxic sensitization to indoloquinone EO9 and mitomycin C in a human colon-tumour cell line that lacks DT-diaphorase activity
    • (1994) Int J Cancer , vol.56 , pp. 134-139
    • Plumb1    Workman2
  • 121
    • 0025688249 scopus 로고
    • Metabolism of mitomycin C by DT-diaphorase: Role in mitomycin C-induced DNA damage and cytotoxicity in human colon carcinoma cells
    • (1990) Cancer Res , vol.50 , pp. 7483-7489
    • Siegel1    Gibson2    Preusch3    Ross4
  • 122
    • 0027051111 scopus 로고
    • Role of NAD(P)H: (quinone acceptor) oxidoreductase (DT-diaphorase) in activation of mitomycin C under hypoxia
    • (1992) Mol Pharmacol , vol.41 , pp. 677-682
    • Begleiter1    Robotham2    Leith3
  • 123
    • 0027219365 scopus 로고
    • Role of NAD(P)H: (quinone acceptor) oxidoreductase (DT-diaphorase) in activation of mitomycin C under acidic conditions
    • (1993) Mol Pharmacol , vol.44 , pp. 210-215
    • Begleiter1    Leith2
  • 124
    • 0022622807 scopus 로고
    • Generation of reactive oxygen radicals though bioactivation of mitomycin antibiotics
    • (1986) Cancer Res , vol.46 , pp. 3528-3532
    • Pritsos1    Sartorelli2
  • 127
    • 0001213485 scopus 로고
    • Role of hydrogen peroxide and hydroxyl radical formation in the killing of Ehrlich tumor cells by anticancer quinones
    • 3rd Edn
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4514-4518
    • Doroshow1
  • 128
  • 131
  • 132
    • 0027427924 scopus 로고
    • Kinetics and mechanism of mitomycin C bioactivation by xanthine dehydrogenase under aerobic and hypoxic conditions
    • (1993) Cancer Res , vol.53 , pp. 5470-5474
    • Gustafson1    Pritsos2
  • 134
    • 0027048768 scopus 로고
    • Relationship between DT-diaphorase-mediated metabolism of a series of aziridinylbenzoquinones and DNA damage and cytotoxicity
    • (1992) Mol Pharmacol , vol.42 , pp. 531-536
    • Gibson1    Hartley2    Butler3    Siegel4    Ross5
  • 138
    • 0027321621 scopus 로고
    • A comparison of free radical formation by quinone antitumour agents in MCF-7 cells and the role of NAD(P)H:(quinone acceptor) oxidoreductase (DT-diaphorase)
    • (1993) Chem Biol Interact , vol.88 , pp. 137-153
    • Fisher1    Patterson2    Gutierrez3
  • 139
    • 0025893246 scopus 로고
    • The role of NAD(P)H: quinone reductase (EC 1.6.99.2, DT-diaphorase) in the reductive bioactivation of the novel indoloquinone antitumour agent EO9
    • (1991) Cancer Commun , vol.3 , pp. 199-206
    • Wallon1    Smith2    Workman3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.