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Volumn 60, Issue 4, 2000, Pages 601-605

Protective action of cardiac DT-diaphorase against menadione toxicity in guinea pig isolated atria

Author keywords

Naphthoflavone; Dicoumarol; DT diaphorase; Guinea pig atria; Menadione; Reactive oxygen species

Indexed keywords

BETA NAPHTHOFLAVONE; DICOUMAROL; MENADIONE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); SUPEROXIDE DISMUTASE;

EID: 0034664193     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(00)00350-6     Document Type: Article
Times cited : (19)

References (26)
  • 1
    • 0024351990 scopus 로고
    • Effects of 2-methyl-1,4-naphthoquinone (menadione) on myocardial contractility and cardiac sarcoplasmic reticulum Ca-ATPase
    • Floreani M., Santi Soncin E., Carpenedo F. Effects of 2-methyl-1,4-naphthoquinone (menadione) on myocardial contractility and cardiac sarcoplasmic reticulum Ca-ATPase. Naunyn Schmiedebergs Arch Pharmacol. 339:1989;448-455.
    • (1989) Naunyn Schmiedebergs Arch Pharmacol , vol.339 , pp. 448-455
    • Floreani, M.1    Santi Soncin, E.2    Carpenedo, F.3
  • 2
    • 0025965186 scopus 로고
    • Modifications of cardiac contractility by redox cycling, alkylating and mixed redox cycling/alkylating quinones
    • Floreani M., Carpenedo F. Modifications of cardiac contractility by redox cycling, alkylating and mixed redox cycling/alkylating quinones. J Pharmacol Exp Ther. 256:1991;243-248.
    • (1991) J Pharmacol Exp Ther , vol.256 , pp. 243-248
    • Floreani, M.1    Carpenedo, F.2
  • 3
    • 0026540629 scopus 로고
    • The catecholamine-mediated positive inotropic effect of simple quinones is related to superoxide anion generation
    • Floreani M., Carpenedo F. The catecholamine-mediated positive inotropic effect of simple quinones is related to superoxide anion generation. J Pharmacol Exp Ther. 260:1992;468-473.
    • (1992) J Pharmacol Exp Ther , vol.260 , pp. 468-473
    • Floreani, M.1    Carpenedo, F.2
  • 4
    • 0026654442 scopus 로고
    • One- And two-electron reduction of menadione in guinea-pig and rat cardiac tissue
    • Floreani M., Carpenedo F. One- and two-electron reduction of menadione in guinea-pig and rat cardiac tissue. Gen Pharmacol. 23:1992;757-762.
    • (1992) Gen Pharmacol , vol.23 , pp. 757-762
    • Floreani, M.1    Carpenedo, F.2
  • 5
    • 0018875204 scopus 로고
    • Relationship of the single-electron reduction potential of quinones to their reduction by flavoproteins
    • Powis G., Appel P.L. Relationship of the single-electron reduction potential of quinones to their reduction by flavoproteins. Biochem Pharmacol. 29:1980;2567-2572.
    • (1980) Biochem Pharmacol , vol.29 , pp. 2567-2572
    • Powis, G.1    Appel, P.L.2
  • 6
    • 0014667960 scopus 로고
    • One-electron-transfer reaction in biochemical systems. III. One-electron reduction of quinones by microsomal flavin enzymes
    • Iyanagi T., Yamazaki I. One-electron-transfer reaction in biochemical systems. III. One-electron reduction of quinones by microsomal flavin enzymes. Biochim Biophys Acta. 172:1969;370-381.
    • (1969) Biochim Biophys Acta , vol.172 , pp. 370-381
    • Iyanagi, T.1    Yamazaki, I.2
  • 7
    • 0014842505 scopus 로고
    • One-electron-transfer reaction in biochemical systems. V. Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase)
    • Iyanagi T., Yamazaki I. One-electron-transfer reaction in biochemical systems. V. Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase). Biochim Biophys Acta. 216:1970;282-294.
    • (1970) Biochim Biophys Acta , vol.216 , pp. 282-294
    • Iyanagi, T.1    Yamazaki, I.2
  • 8
    • 0020464384 scopus 로고
    • DT-diaphorase as a quinone reductase: A cellular control device against semiquinone and superoxide radical formation
    • Lind C., Hochstein P., Ernster L. DT-diaphorase as a quinone reductase A cellular control device against semiquinone and superoxide radical formation . Arch Biochem Biophys. 216:1982;178-185.
    • (1982) Arch Biochem Biophys , vol.216 , pp. 178-185
    • Lind, C.1    Hochstein, P.2    Ernster, L.3
  • 9
    • 0020440918 scopus 로고
    • The metabolism of menadione (2-methyl-1,4-naphthoquinone) by isolated hepatocytes
    • Thor H., Smith M.T., Hartzell P., Bellomo G., Jewell S.A., Orrenius S. The metabolism of menadione (2-methyl-1,4-naphthoquinone) by isolated hepatocytes. J Biol Chem. 257:1982;12419-12425.
    • (1982) J Biol Chem , vol.257 , pp. 12419-12425
    • Thor, H.1    Smith, M.T.2    Hartzell, P.3    Bellomo, G.4    Jewell, S.A.5    Orrenius, S.6
  • 10
    • 0031665666 scopus 로고    scopus 로고
    • Glutathione S-transferases and prevention of cellular free radical damage
    • Ketterer B. Glutathione S-transferases and prevention of cellular free radical damage. Free Radic Res. 28:1998;647-658.
    • (1998) Free Radic Res , vol.28 , pp. 647-658
    • Ketterer, B.1
  • 11
    • 0024498044 scopus 로고
    • DT-diaphorase-catalysed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates. Effect of substituents on autoxidation rates
    • Buffinton G.D., Ollinger K., Brunmark A., Cadenas E. DT-diaphorase-catalysed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates. Effect of substituents on autoxidation rates. Biochem J. 257:1989;561-571.
    • (1989) Biochem J , vol.257 , pp. 561-571
    • Buffinton, G.D.1    Ollinger, K.2    Brunmark, A.3    Cadenas, E.4
  • 12
    • 0026612119 scopus 로고
    • DT-diaphorase and cancer chemotherapy
    • Riley R.J., Workman P. DT-diaphorase and cancer chemotherapy. Biochem Pharmacol. 43:1992;1657-1669.
    • (1992) Biochem Pharmacol , vol.43 , pp. 1657-1669
    • Riley, R.J.1    Workman, P.2
  • 13
    • 0017597227 scopus 로고
    • Comparison of β-naphthoflavone and 3-methylcholanthrene as inducers of hepatic cytochrome(s) P-448 and aryl hydrocarbon (benzo[a]pyrene) hydroxylase activity
    • Boobis A.R., Nebert D.W., Felton J.S. Comparison of β-naphthoflavone and 3-methylcholanthrene as inducers of hepatic cytochrome(s) P-448 and aryl hydrocarbon (benzo[a]pyrene) hydroxylase activity. Mol Pharmacol. 13:1977;259-268.
    • (1977) Mol Pharmacol , vol.13 , pp. 259-268
    • Boobis, A.R.1    Nebert, D.W.2    Felton, J.S.3
  • 14
    • 0027240209 scopus 로고
    • 1 biotransformation in guinea-pig tissues: Effects of β-naphthoflavone treatment
    • 1 biotransformation in guinea-pig tissues effects of β-naphthoflavone treatment . Arch Toxicol. 67:1993;379-385.
    • (1993) Arch Toxicol , vol.67 , pp. 379-385
    • Liu, L.1    Nakatsu, K.2    Massey, T.E.3
  • 17
    • 0022357068 scopus 로고
    • Ethoxy-, penthoxy- And benzyloxyphenoxazones and homologues: A series of substrates to distinguish between different induced cytochrome P-450
    • Burke M.D., Thompson S., Elcombe C.R., Halpert J., Haaparanta T., Mayer R.T. Ethoxy-, penthoxy- and benzyloxyphenoxazones and homologues A series of substrates to distinguish between different induced cytochrome P-450 . Biochem Pharmacol. 34:1985;3337-3345.
    • (1985) Biochem Pharmacol , vol.34 , pp. 3337-3345
    • Burke, M.D.1    Thompson, S.2    Elcombe, C.R.3    Halpert, J.4    Haaparanta, T.5    Mayer, R.T.6
  • 18
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., Jakoby W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J Biol Chem. 249:1974;7130-7139.
    • (1974) J Biol Chem , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 19
    • 0030913865 scopus 로고    scopus 로고
    • A comparison between different methods for the determination of reduced and oxidized glutathione in mammalian tissues
    • Floreani M., Petrone M., Debetto P., Palatini P. A comparison between different methods for the determination of reduced and oxidized glutathione in mammalian tissues. Free Radic Res. 26:1997;449-455.
    • (1997) Free Radic Res , vol.26 , pp. 449-455
    • Floreani, M.1    Petrone, M.2    Debetto, P.3    Palatini, P.4
  • 21
    • 0026699018 scopus 로고
    • Inhibition of mouse glutathione transferases and glutathione peroxidase II by dicumarol and other ligands
    • Mays J.B., Benson A.M. Inhibition of mouse glutathione transferases and glutathione peroxidase II by dicumarol and other ligands. Biochem Pharmacol. 44:1992;921-925.
    • (1992) Biochem Pharmacol , vol.44 , pp. 921-925
    • Mays, J.B.1    Benson, A.M.2
  • 22
    • 0026356151 scopus 로고
    • Induction of cytochrome P450IA1 and P450IA2 and measurement of catalytic activities
    • Rodrigues A.D., Prough R.A. Induction of cytochrome P450IA1 and P450IA2 and measurement of catalytic activities. Methods Enzymol. 206:1991;423-431.
    • (1991) Methods Enzymol , vol.206 , pp. 423-431
    • Rodrigues, A.D.1    Prough, R.A.2
  • 23
    • 0029623125 scopus 로고
    • Response of [Ah] battery genes to compounds that protect against menadione toxicity
    • Vasiliou V., Shertzer H.G., Liu R.M., Sainsbury M., Nebert D.W. Response of [Ah] battery genes to compounds that protect against menadione toxicity. Biochem Pharmacol. 50:1995;1885-1891.
    • (1995) Biochem Pharmacol , vol.50 , pp. 1885-1891
    • Vasiliou, V.1    Shertzer, H.G.2    Liu, R.M.3    Sainsbury, M.4    Nebert, D.W.5
  • 24
    • 0031474716 scopus 로고    scopus 로고
    • Ah receptor, a novel ligand-activated transcription factor
    • Sogawa K., Fujii-Kuriyama Y. Ah receptor, a novel ligand-activated transcription factor. J Biochem. 122:1997;1075-1079.
    • (1997) J Biochem , vol.122 , pp. 1075-1079
    • Sogawa, K.1    Fujii-Kuriyama, Y.2
  • 25
    • 0027395864 scopus 로고
    • Effects of acute arsenite administration on the pulmonary chemical metabolizing enzymes, cytochrome P-450 monooxygenase, NAD(P)H:quinone acceptor oxidoreductase and glutathione S-transferase in guinea pig: Comparison with effects in liver and kidney
    • Falkner K.C., McCallum G.P., Cherian M.G., Bend J.R. Effects of acute arsenite administration on the pulmonary chemical metabolizing enzymes, cytochrome P-450 monooxygenase, NAD(P)H:quinone acceptor oxidoreductase and glutathione S-transferase in guinea pig Comparison with effects in liver and kidney . Chem Biol Interact. 86:1993;51-68.
    • (1993) Chem Biol Interact , vol.86 , pp. 51-68
    • Falkner, K.C.1    McCallum, G.P.2    Cherian, M.G.3    Bend, J.R.4
  • 26
    • 0029012812 scopus 로고
    • Age- And peroxidative stress-related modifications of the cerebral enzymatic activities linked to mitochondria and the glutathione system
    • Benzi G., Moretti A. Age- and peroxidative stress-related modifications of the cerebral enzymatic activities linked to mitochondria and the glutathione system. Free Radic Biol Med. 19:1995;77-101.
    • (1995) Free Radic Biol Med , vol.19 , pp. 77-101
    • Benzi, G.1    Moretti, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.