메뉴 건너뛰기




Volumn 336, Issue 2, 2005, Pages 565-571

Role of a novel dual flavin reductase (NR1) and an associated histidine triad protein (DCS-1) in menadione-induced cytotoxicity

Author keywords

Flavoproteins; Microsomal cytochrome P450 reductase; NADPH dependent flavin reductase

Indexed keywords

FLAVIN REDUCTASE NR1; HISTIDINE; MENADIONE; OXIDOREDUCTASE; PROTEIN; PROTEIN DCS1; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 24644449738     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.129     Document Type: Article
Times cited : (5)

References (31)
  • 1
    • 0013569329 scopus 로고
    • Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains
    • T.D. Porter, and C.B. Kasper Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains Proc. Natl. Acad. Sci. USA 82 1985 973 977
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 973-977
    • Porter, T.D.1    Kasper, C.B.2
  • 2
    • 0642376506 scopus 로고    scopus 로고
    • Expression of mammalian cytochromes P450 in yeast
    • Y. Yabusaki Expression of mammalian cytochromes P450 in yeast Methods Mol. Biol. 107 1998 195 202
    • (1998) Methods Mol. Biol. , vol.107 , pp. 195-202
    • Yabusaki, Y.1
  • 3
    • 0021107944 scopus 로고
    • Possible association of NADPH-cytochrome P-450 reductase and cytochrome P-450 in reconstituted phospholipid vesicles
    • Y. Nisimoto, K. Kinosita Jr., A. Ikegami, N. Kawai, I. Ichihara, and Y. Shibata Possible association of NADPH-cytochrome P-450 reductase and cytochrome P-450 in reconstituted phospholipid vesicles Biochemistry 22 1983 3586 3594
    • (1983) Biochemistry , vol.22 , pp. 3586-3594
    • Nisimoto, Y.1    Kinosita Jr., K.2    Ikegami, A.3    Kawai, N.4    Ichihara, I.5    Shibata, Y.6
  • 4
    • 0015560033 scopus 로고
    • NADPH-cytochrome c reductase and its role in microsomal cytochrome P-450-dependent reactions
    • B.S. Masters, E.B. Nelson, B.A. Schacter, J. Baron, and E.L. Isaacson NADPH-cytochrome c reductase and its role in microsomal cytochrome P-450-dependent reactions Drug Metab. Dispos. 1 1973 121 128
    • (1973) Drug Metab. Dispos. , vol.1 , pp. 121-128
    • Masters, B.S.1    Nelson, E.B.2    Schacter, B.A.3    Baron, J.4    Isaacson, E.L.5
  • 5
    • 0015514943 scopus 로고
    • Hemoprotein catabolism during stimulation of microsomal lipid peroxidation
    • B.A. Schacter, U.A. Meyer, and H.S. Marver Hemoprotein catabolism during stimulation of microsomal lipid peroxidation Biochim. Biophys. Acta 279 1972 221 227
    • (1972) Biochim. Biophys. Acta , vol.279 , pp. 221-227
    • Schacter, B.A.1    Meyer, U.A.2    Marver, H.S.3
  • 6
    • 0018820633 scopus 로고
    • NADPH cytochrome P-450 reductase and its role in the mixed function oxidase reaction
    • H.W. Strobel, J.D. Dignam, and J.R. Gum NADPH cytochrome P-450 reductase and its role in the mixed function oxidase reaction Pharmacol. Ther. 8 1980 525 537
    • (1980) Pharmacol. Ther. , vol.8 , pp. 525-537
    • Strobel, H.W.1    Dignam, J.D.2    Gum, J.R.3
  • 7
    • 0018741206 scopus 로고
    • NADPH cytochrome P-450 reductase activation of quinone anticancer agents to free radicals
    • N.R. Bachur, S.L. Gordon, M.V. Gee, and H. Kon NADPH cytochrome P-450 reductase activation of quinone anticancer agents to free radicals Proc. Natl. Acad. Sci. USA 76 1979 954 957
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 954-957
    • Bachur, N.R.1    Gordon, S.L.2    Gee, M.V.3    Kon, H.4
  • 9
    • 0023113250 scopus 로고
    • Role of hepatic microsomal and purified cytochrome P-450 in one-electron reduction of two quinone imines and concomitant reduction of molecular oxygen
    • R. vande Straat, J. de Vries, and N.P. Vermeulen Role of hepatic microsomal and purified cytochrome P-450 in one-electron reduction of two quinone imines and concomitant reduction of molecular oxygen Biochem. Pharmacol. 36 1987 613 619
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 613-619
    • Vande Straat, R.1    De Vries, J.2    Vermeulen, N.P.3
  • 12
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • D.S. Bredt, P.M. Hwang, C.E. Glatt, C. Lowenstein, R.R. Reed, and S.H. Snyder Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase Nature 351 1991 714 718
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, C.4    Reed, R.R.5    Snyder, S.H.6
  • 14
    • 0028358410 scopus 로고
    • Inhibition of nitric oxide synthase by antineoplastic anthracyclines
    • D. Luo, and S.R. Vincent Inhibition of nitric oxide synthase by antineoplastic anthracyclines Biochem. Pharmacol. 47 1994 2111 2112
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 2111-2112
    • Luo, D.1    Vincent, S.R.2
  • 15
    • 0028984457 scopus 로고
    • Effects of methylene blue and LY83583 on neuronal nitric oxide synthase and NADPH-diaphorase
    • D. Luo, S. Das, and S.R. Vincent Effects of methylene blue and LY83583 on neuronal nitric oxide synthase and NADPH-diaphorase Eur. J. Pharmacol. 290 1995 247 251
    • (1995) Eur. J. Pharmacol. , vol.290 , pp. 247-251
    • Luo, D.1    Das, S.2    Vincent, S.R.3
  • 16
    • 0034691656 scopus 로고    scopus 로고
    • One-electron reduction of quinones by the neuronal nitric-oxide synthase reductase domain
    • H. Matsuda, S. Kimura, and T. Iyanagi One-electron reduction of quinones by the neuronal nitric-oxide synthase reductase domain Biochim. Biophys. Acta 1459 2000 106 116
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 106-116
    • Matsuda, H.1    Kimura, S.2    Iyanagi, T.3
  • 18
    • 0345505668 scopus 로고    scopus 로고
    • Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1
    • R.D. Finn, J. Basran, O. Roitel, C.R. Wolf, A.W. Munro, M.J. Paine, and N.S. Scrutton Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1 Eur. J. Biochem. 270 2003 1164 1175
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1164-1175
    • Finn, R.D.1    Basran, J.2    Roitel, O.3    Wolf, C.R.4    Munro, A.W.5    Paine, M.J.6    Scrutton, N.S.7
  • 19
    • 0141643119 scopus 로고    scopus 로고
    • Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and Hint-related 7meGMP-directed hydrolase, DCS-1
    • D.A. Kwasnicka, A. Krakowiak, C. Thacker, C. Brenner, and S.R. Vincent Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and Hint-related 7meGMP-directed hydrolase, DCS-1 J. Biol. Chem. 278 2003 39051 39058
    • (2003) J. Biol. Chem. , vol.278 , pp. 39051-39058
    • Kwasnicka, D.A.1    Krakowiak, A.2    Thacker, C.3    Brenner, C.4    Vincent, S.R.5
  • 21
    • 0026040838 scopus 로고
    • Molecular mechanisms of quinone cytotoxicity
    • P.J. O'Brien Molecular mechanisms of quinone cytotoxicity Chem. Biol. Interact. 80 1991 1 41
    • (1991) Chem. Biol. Interact. , vol.80 , pp. 1-41
    • O'Brien, P.J.1
  • 22
    • 0032866401 scopus 로고    scopus 로고
    • The use of heterologously expressed drug metabolizing enzymes-state of the art and prospects for the future
    • C.L. Crespi, and V.P. Miller The use of heterologously expressed drug metabolizing enzymes-state of the art and prospects for the future Pharmacol. Ther. 84 1999 121 131
    • (1999) Pharmacol. Ther. , vol.84 , pp. 121-131
    • Crespi, C.L.1    Miller, V.P.2
  • 23
    • 0030454188 scopus 로고    scopus 로고
    • Stable expression and coexpression of human cytochrome P450 oxidoreductase and cytochrome P450 1A2 in V79 Chinese hamster cells: Sensitivity to quinones and biotransformation of 7-alkoxyresorufins and triazines
    • W.A. Schmalix, D. Lang, A. Schneider, R. Bocker, H. Greim, and J. Doehmer Stable expression and coexpression of human cytochrome P450 oxidoreductase and cytochrome P450 1A2 in V79 Chinese hamster cells: sensitivity to quinones and biotransformation of 7-alkoxyresorufins and triazines Drug Metab. Dispos. 24 1996 1314 1319
    • (1996) Drug Metab. Dispos. , vol.24 , pp. 1314-1319
    • Schmalix, W.A.1    Lang, D.2    Schneider, A.3    Bocker, R.4    Greim, H.5    Doehmer, J.6
  • 24
    • 0020490599 scopus 로고
    • Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region
    • S.D. Black, and M.J. Coon Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region J. Biol. Chem. 257 1982 5929 5938
    • (1982) J. Biol. Chem. , vol.257 , pp. 5929-5938
    • Black, S.D.1    Coon, M.J.2
  • 25
    • 0032883882 scopus 로고    scopus 로고
    • The histidine triad superfamily of nucleotide-binding proteins
    • C. Brenner, P. Bieganowski, H.C. Pace, and K. Huebner The histidine triad superfamily of nucleotide-binding proteins J. Cell Physiol. 181 1999 179 187
    • (1999) J. Cell Physiol. , vol.181 , pp. 179-187
    • Brenner, C.1    Bieganowski, P.2    Pace, H.C.3    Huebner, K.4
  • 26
    • 0037162392 scopus 로고    scopus 로고
    • Hint, Fhit, and GalT: Function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases
    • C. Brenner Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases Biochemistry 41 2002 9003 9014
    • (2002) Biochemistry , vol.41 , pp. 9003-9014
    • Brenner, C.1
  • 27
    • 0037009517 scopus 로고    scopus 로고
    • The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases
    • H. Liu, N.D. Rodgers, X. Jiao, and M. Kiledjian The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases EMBO J. 21 2002 4699 4708
    • (2002) EMBO J. , vol.21 , pp. 4699-4708
    • Liu, H.1    Rodgers, N.D.2    Jiao, X.3    Kiledjian, M.4
  • 30
    • 0039613985 scopus 로고    scopus 로고
    • Suppression of microphthalmia transcriptional activity by its association with protein kinase C-interacting protein1 in mast cells
    • E. Razin, Z.C. Zhang, H. Nechushtan, S. Frenkel, Y.N. Lee, R. Arudchandran, and J. Rivera Suppression of microphthalmia transcriptional activity by its association with protein kinase C-interacting protein1 in mast cells J. Biol. Chem. 274 1999 34272 34276
    • (1999) J. Biol. Chem. , vol.274 , pp. 34272-34276
    • Razin, E.1    Zhang, Z.C.2    Nechushtan, H.3    Frenkel, S.4    Lee, Y.N.5    Arudchandran, R.6    Rivera, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.