메뉴 건너뛰기




Volumn 59, Issue 1, 2000, Pages 95-104

Regulation of metallothionein gene expression by oxidative stress and metal ions

Author keywords

ARE; Cadmium; Metallothionein; Oxidative stress; USF; Zinc

Indexed keywords

CADMIUM; HELIX LOOP HELIX PROTEIN; METAL; METALLOTHIONEIN; TRANSCRIPTION FACTOR; ZINC;

EID: 0033990794     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(99)00301-9     Document Type: Conference Paper
Times cited : (740)

References (91)
  • 1
    • 0025154985 scopus 로고
    • Regulation of metallothionein gene expression
    • Andrews G.K. Regulation of metallothionein gene expression. Prog Food Nutr Sci. 14:1990;193-258.
    • (1990) Prog Food Nutr Sci , vol.14 , pp. 193-258
    • Andrews, G.K.1
  • 2
    • 0026353521 scopus 로고
    • Overview of metallothionein
    • Kagi J.H.R. Overview of metallothionein. Methods Enzymol. 205:1991;613-626.
    • (1991) Methods Enzymol , vol.205 , pp. 613-626
    • Kagi, J.H.R.1
  • 5
    • 0028358324 scopus 로고
    • The transcription factor MTF-I is essential for basal and heavy metal-induced metallothionein gene expression
    • Heuchel R., Radtke F., Georgiev O., Stark G., Aguet M., Schaffner W. The transcription factor MTF-I is essential for basal and heavy metal-induced metallothionein gene expression. EMBO J. 13:1994;2870-2875.
    • (1994) EMBO J , vol.13 , pp. 2870-2875
    • Heuchel, R.1    Radtke, F.2    Georgiev, O.3    Stark, G.4    Aguet, M.5    Schaffner, W.6
  • 6
    • 0030909001 scopus 로고    scopus 로고
    • Reversible activation of the mouse metal response element-binding transcription factor-1 DNA binding involves zinc interactions with the zinc-finger domain
    • Dalton T.D., Bittel D., Andrews G.K. Reversible activation of the mouse metal response element-binding transcription factor-1 DNA binding involves zinc interactions with the zinc-finger domain. Mol Cell Biol. 17:1997;2781-2789.
    • (1997) Mol Cell Biol , vol.17 , pp. 2781-2789
    • Dalton, T.D.1    Bittel, D.2    Andrews, G.K.3
  • 7
    • 0032549517 scopus 로고    scopus 로고
    • The DNA-binding activity of metal response element-binding transcription factor-1 is activated in vivo and in vitro by zinc, but not by other transition metals
    • Bittel D., Dalton T., Samson S., Gedamu L., Andrews G.K. The DNA-binding activity of metal response element-binding transcription factor-1 is activated in vivo and in vitro by zinc, but not by other transition metals. J Biol Chem. 273:1998;7127-7133.
    • (1998) J Biol Chem , vol.273 , pp. 7127-7133
    • Bittel, D.1    Dalton, T.2    Samson, S.3    Gedamu, L.4    Andrews, G.K.5
  • 8
    • 0027182948 scopus 로고
    • Distal regulatory elements from the mouse metallothionein locus stimulate gene expression in transgenic mice
    • Palmiter R.D., Sandgren E.P., Koeller D.M., Brinster R.L. Distal regulatory elements from the mouse metallothionein locus stimulate gene expression in transgenic mice. Mol Cell Biol. 13:1993;5266-5275.
    • (1993) Mol Cell Biol , vol.13 , pp. 5266-5275
    • Palmiter, R.D.1    Sandgren, E.P.2    Koeller, D.M.3    Brinster, R.L.4
  • 10
    • 0029985755 scopus 로고    scopus 로고
    • Transgenic mice that over-express metallothionein-I resist dietary zinc deficiency
    • Dalton T.P., Fu K., Palmiter R.D., Andrews G.K. Transgenic mice that over-express metallothionein-I resist dietary zinc deficiency. J Nutr. 126:1996;825-833.
    • (1996) J Nutr , vol.126 , pp. 825-833
    • Dalton, T.P.1    Fu, K.2    Palmiter, R.D.3    Andrews, G.K.4
  • 11
    • 0032839870 scopus 로고    scopus 로고
    • Expression of the mouse metallothionein-I and -II genes provides a reproductive advantage during maternal dietary zinc deficiency
    • Andrews G.K., Geiser J. Expression of the mouse metallothionein-I and -II genes provides a reproductive advantage during maternal dietary zinc deficiency. J Nutr. 129:1999;1643-1648.
    • (1999) J Nutr , vol.129 , pp. 1643-1648
    • Andrews, G.K.1    Geiser, J.2
  • 12
    • 0029987684 scopus 로고    scopus 로고
    • Metallothionein I and II protect against zinc deficiency and zinc toxicity in mice
    • Kelly E.J., Quaife C.J., Froelick G.J., Palmiter R.D. Metallothionein I and II protect against zinc deficiency and zinc toxicity in mice. J Nutr. 126:1996;1782-1790.
    • (1996) J Nutr , vol.126 , pp. 1782-1790
    • Kelly, E.J.1    Quaife, C.J.2    Froelick, G.J.3    Palmiter, R.D.4
  • 13
    • 0033515626 scopus 로고    scopus 로고
    • Metallothionein is part of a zinc-scavenging mechanism for cell survival under conditions of extreme zinc deprivation
    • Suhy D.A., Simon K.D., Linzer D.I.H., O'Halloran T.V. Metallothionein is part of a zinc-scavenging mechanism for cell survival under conditions of extreme zinc deprivation. J Biol Chem. 274:1999;9183-9192.
    • (1999) J Biol Chem , vol.274 , pp. 9183-9192
    • Suhy, D.A.1    Simon, K.D.2    Linzer, D.I.H.3    O'Halloran, T.V.4
  • 14
    • 0033514994 scopus 로고    scopus 로고
    • Inhibitory sites in enzymes: Zinc removal and reactivation by thionein
    • Maret W., Jacob C., Vallee B.L., Fischer E.H. Inhibitory sites in enzymes Zinc removal and reactivation by thionein . Proc Natl Acad Sci USA. 96:1999;1936-1940.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1936-1940
    • Maret, W.1    Jacob, C.2    Vallee, B.L.3    Fischer, E.H.4
  • 15
    • 0032555204 scopus 로고    scopus 로고
    • The elusive function of metallothioneins
    • Palmiter R.D. The elusive function of metallothioneins. Proc Natl Acad Sci USA. 95:1998;8428-8430.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8428-8430
    • Palmiter, R.D.1
  • 17
    • 0030667913 scopus 로고    scopus 로고
    • Tran S, Weng WL, Mannix RJ, Watkins SA, Tyurina YY, Tyurin VA, Kagan VE and Lazo JS, Overexpression of metallothionein decreases sensitivity of pulmonary endothelial cells to oxidant injury
    • Pitt B.R., Schwarz M., Woo E.S., Yee E., Wasserloos K. Tran S, Weng WL, Mannix RJ, Watkins SA, Tyurina YY, Tyurin VA, Kagan VE and Lazo JS, Overexpression of metallothionein decreases sensitivity of pulmonary endothelial cells to oxidant injury. Am J Physiol. 273:1997;L856-L865.
    • (1997) Am J Physiol , vol.273
    • Pitt, B.R.1    Schwarz, M.2    Woo, E.S.3    Yee, E.4    Wasserloos, K.5
  • 18
    • 0028944114 scopus 로고
    • Enhanced sensitivity to oxidative stress in cultured embryonic cells from transgenic mice deficient in metallothionein I and II genes
    • Lazo J.S., Kondo Y., Dellapiazza D., Michalska A.E., Choo K.H.A., Pitt B.R. Enhanced sensitivity to oxidative stress in cultured embryonic cells from transgenic mice deficient in metallothionein I and II genes. J Biol Chem. 270:1995;5506-5510.
    • (1995) J Biol Chem , vol.270 , pp. 5506-5510
    • Lazo, J.S.1    Kondo, Y.2    Dellapiazza, D.3    Michalska, A.E.4    Choo, K.H.A.5    Pitt, B.R.6
  • 19
    • 0023071221 scopus 로고
    • Molecular biology of metallothionein gene expression
    • Palmiter R.D. Molecular biology of metallothionein gene expression. EXS. 52:1987;63-80.
    • (1987) EXS , vol.52 , pp. 63-80
    • Palmiter, R.D.1
  • 20
    • 0028593507 scopus 로고
    • Transcriptional induction of the mouse metallothionein-I gene in hydrogen peroxide-treated Hepa cells involves a composite major late transcription factor/antioxidant response element and metal response promoter elements
    • Dalton T.P., Palmiter R.D., Andrews G.K. Transcriptional induction of the mouse metallothionein-I gene in hydrogen peroxide-treated Hepa cells involves a composite major late transcription factor/antioxidant response element and metal response promoter elements. Nucleic Acids Res. 22:1994;5016-5023.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5016-5023
    • Dalton, T.P.1    Palmiter, R.D.2    Andrews, G.K.3
  • 21
    • 0024523351 scopus 로고
    • Inhibition of hydroxyl-radical-generated DNA degradation by metallothionein
    • Abel J., de Ruiter N. Inhibition of hydroxyl-radical-generated DNA degradation by metallothionein. Toxicol Lett. 47:1989;191-196.
    • (1989) Toxicol Lett , vol.47 , pp. 191-196
    • Abel, J.1    De Ruiter, N.2
  • 22
    • 0021944046 scopus 로고
    • Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals
    • Thornalley P.J., Vasak M. Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals. Biochim Biophys Acta. 827:1985;36-44.
    • (1985) Biochim Biophys Acta , vol.827 , pp. 36-44
    • Thornalley, P.J.1    Vasak, M.2
  • 23
    • 0027169905 scopus 로고
    • Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase
    • Tamai K.T., Gralla E.B., Ellerby L.M., Valentine J.S., Thiele D.J. Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase. Proc Natl Acad Sci U S A. 90:1993;8013-8017.
    • (1993) Proc Natl Acad Sci U S a , vol.90 , pp. 8013-8017
    • Tamai, K.T.1    Gralla, E.B.2    Ellerby, L.M.3    Valentine, J.S.4    Thiele, D.J.5
  • 24
    • 0028082427 scopus 로고
    • Oxidative metal release from metallothionein via zinc-thiol/disulfide interchange
    • Maret W. Oxidative metal release from metallothionein via zinc-thiol/disulfide interchange. Proc Natl Acad Sci USA. 91:1994;237-241.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 237-241
    • Maret, W.1
  • 25
    • 0032584186 scopus 로고    scopus 로고
    • Control of zinc transfer between thionein, metallothionein, and zinc proteins
    • Jacob C., Maret W., Vallee B.L. Control of zinc transfer between thionein, metallothionein, and zinc proteins. Proc Natl Acad Sci U S A. 95:1998;3489-3494.
    • (1998) Proc Natl Acad Sci U S a , vol.95 , pp. 3489-3494
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 26
    • 0038929320 scopus 로고
    • A 12-base-pair DNA motif that is repeated several times in metallothionein gene promoters confers metal regulation to a heterologous gene
    • Stuart G.W., Searle P.F., Chen H.Y., Brinster R.L., Palmiter R.D. A 12-base-pair DNA motif that is repeated several times in metallothionein gene promoters confers metal regulation to a heterologous gene. Proc Natl Acad Sci USA. 81:1984;7318-7322.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 7318-7322
    • Stuart, G.W.1    Searle, P.F.2    Chen, H.Y.3    Brinster, R.L.4    Palmiter, R.D.5
  • 27
    • 0022410464 scopus 로고
    • Identification of multiple metal regulatory elements in mouse metallothionein-I promoter by assaying synthetic sequences
    • Stuart G.W., Searle P.F., Palmiter R.D. Identification of multiple metal regulatory elements in mouse metallothionein-I promoter by assaying synthetic sequences. Nature. 317:1985;828-831.
    • (1985) Nature , vol.317 , pp. 828-831
    • Stuart, G.W.1    Searle, P.F.2    Palmiter, R.D.3
  • 28
    • 0033013532 scopus 로고    scopus 로고
    • Characterization of the transcription factor MTF-1 from the Japanese pufferfish (Fugu rubripes) reveals evolutionary conservation of heavy metal stress response
    • Maur A.A.D., Belser T., Elgar G., Georgiev O., Schaffner W. Characterization of the transcription factor MTF-1 from the Japanese pufferfish (Fugu rubripes) reveals evolutionary conservation of heavy metal stress response. Biol Chem. 380:1999;175-185.
    • (1999) Biol Chem , vol.380 , pp. 175-185
    • Maur, A.A.D.1    Belser, T.2    Elgar, G.3    Georgiev, O.4    Schaffner, W.5
  • 31
    • 0029910072 scopus 로고    scopus 로고
    • Oxidative stress activates metal-responsive transcription factor-1 binding activity. Occupancy in vivo of metal response elements in the metallothionein-I gene promoter
    • Dalton T.P., Li Q.W., Bittel D., Liang L.C., Andrews G.K. Oxidative stress activates metal-responsive transcription factor-1 binding activity. Occupancy in vivo of metal response elements in the metallothionein-I gene promoter. J Biol Chem. 271:1996;26233-26241.
    • (1996) J Biol Chem , vol.271 , pp. 26233-26241
    • Dalton, T.P.1    Li, Q.W.2    Bittel, D.3    Liang, L.C.4    Andrews, G.K.5
  • 32
    • 0027185397 scopus 로고
    • Transcriptional regulation of the rat NAD(P)H:quinone reductase gene. Characterization of a DNA-protein interaction at the antioxidant responsive element and induction by 12-O-tetradecanoylphorbol 13-acetate
    • Favreau L.V., Pickett C.B. Transcriptional regulation of the rat NAD(P)H:quinone reductase gene. Characterization of a DNA-protein interaction at the antioxidant responsive element and induction by 12-O-tetradecanoylphorbol 13-acetate. J Biol Chem. 268:1993;19875-19881.
    • (1993) J Biol Chem , vol.268 , pp. 19875-19881
    • Favreau, L.V.1    Pickett, C.B.2
  • 33
    • 0028023597 scopus 로고
    • Antioxidant response element
    • Jaiswal A.K. Antioxidant response element. Biochem Pharmacol. 48:1994;439-444.
    • (1994) Biochem Pharmacol , vol.48 , pp. 439-444
    • Jaiswal, A.K.1
  • 36
    • 0023448190 scopus 로고
    • The major late transcription factor binds to and activates the mouse metallothionein I promoter
    • Carthew R.W., Chodosh L.A., Sharp P.A. The major late transcription factor binds to and activates the mouse metallothionein I promoter. Genes Dev. 1:1987;973-980.
    • (1987) Genes Dev , vol.1 , pp. 973-980
    • Carthew, R.W.1    Chodosh, L.A.2    Sharp, P.A.3
  • 37
    • 0025061096 scopus 로고
    • TFE3: A helix-loop-helix protein that activates transcription through the immunoglobulin enhancer muE3 motif
    • Beckmann H., Su L.K., Kadesch T. TFE3 a helix-loop-helix protein that activates transcription through the immunoglobulin enhancer muE3 motif . Genes Dev. 4:1990;167-179.
    • (1990) Genes Dev , vol.4 , pp. 167-179
    • Beckmann, H.1    Su, L.K.2    Kadesch, T.3
  • 38
    • 0028050025 scopus 로고
    • 2 on specificity and comparison with binding of Myc family members
    • 2 on specificity and comparison with binding of Myc family members . Nucleic Acids Res. 22:1994;2801-2810.
    • (1994) Nucleic Acids Res , vol.22 , pp. 2801-2810
    • Bendall, A.J.1    Molloy, P.L.2
  • 39
    • 23444453049 scopus 로고
    • Ubiquitous expression of the 43- And 44-kDa forms of transcription factor USF in mammalian cells
    • Sirito M., Lin Q., Maity T., Sawadogo M. Ubiquitous expression of the 43- and 44-kDa forms of transcription factor USF in mammalian cells. Nucleic Acids Res. 22:1994;427-433.
    • (1994) Nucleic Acids Res , vol.22 , pp. 427-433
    • Sirito, M.1    Lin, Q.2    Maity, T.3    Sawadogo, M.4
  • 40
    • 0025084602 scopus 로고
    • The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer
    • Gregor P.D., Sawadogo M., Roeder R.G. The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer. Genes Dev. 4:1990;1730-1740.
    • (1990) Genes Dev , vol.4 , pp. 1730-1740
    • Gregor, P.D.1    Sawadogo, M.2    Roeder, R.G.3
  • 42
    • 0027034611 scopus 로고
    • Members of the USF family of helix-loop-helix proteins bind DNA as homo- as well as heterodimers
    • Sirito M., Walker S., Lin Q., Kozlowski M.T., Klein W.H., Sawadogo M. Members of the USF family of helix-loop-helix proteins bind DNA as homo- as well as heterodimers. Gene Expr. 2:1992;231-240.
    • (1992) Gene Expr , vol.2 , pp. 231-240
    • Sirito, M.1    Walker, S.2    Lin, Q.3    Kozlowski, M.T.4    Klein, W.H.5    Sawadogo, M.6
  • 43
    • 0026680845 scopus 로고
    • Interaction cloning: Identification of a helix-loop-helix zipper protein that interacts with c-Fos
    • Blanar M.A., Rutter W.J. Interaction cloning Identification of a helix-loop-helix zipper protein that interacts with c-Fos . Science. 256:1992;1014-1018.
    • (1992) Science , vol.256 , pp. 1014-1018
    • Blanar, M.A.1    Rutter, W.J.2
  • 44
    • 0028111849 scopus 로고
    • The cellular transcription factor USF cooperates with varicella-zoster virus immediate-early protein 62 to symmetrically activate a bidirectional viral promoter
    • Meier J.L., Luo X., Sawadogo M., Straus S.E. The cellular transcription factor USF cooperates with varicella-zoster virus immediate-early protein 62 to symmetrically activate a bidirectional viral promoter. Mol Cell Biol. 14:1994;6896-6906.
    • (1994) Mol Cell Biol , vol.14 , pp. 6896-6906
    • Meier, J.L.1    Luo, X.2    Sawadogo, M.3    Straus, S.E.4
  • 45
    • 0030996576 scopus 로고    scopus 로고
    • Cross-family interaction between the bHLHZip USF and bZip Fra1 proteins results in down-regulation of AP1 activity
    • Pognonec P., Boulukos K.E., Aperlo C., Fujimoto M., Ariga H., Nomoto A., Kato H. Cross-family interaction between the bHLHZip USF and bZip Fra1 proteins results in down-regulation of AP1 activity. Oncogene. 14:1997;2091-2098.
    • (1997) Oncogene , vol.14 , pp. 2091-2098
    • Pognonec, P.1    Boulukos, K.E.2    Aperlo, C.3    Fujimoto, M.4    Ariga, H.5    Nomoto, A.6    Kato, H.7
  • 46
    • 0031566263 scopus 로고    scopus 로고
    • USF2/FIP associates with the b-Zip transcription factor, c-Maf, via its bHLH domain and inhibits c-Maf DNA binding activity
    • Kurschner C., Morgan J.I. USF2/FIP associates with the b-Zip transcription factor, c-Maf, via its bHLH domain and inhibits c-Maf DNA binding activity. Biochem Biophys Res Commun. 231:1997;333-339.
    • (1997) Biochem Biophys Res Commun , vol.231 , pp. 333-339
    • Kurschner, C.1    Morgan, J.I.2
  • 47
    • 0027325092 scopus 로고
    • The helix-loop-helix containing transcription factor USF binds to and transactivates the promoter of the p53 tumor suppressor gene
    • Reisman D., Rotter V. The helix-loop-helix containing transcription factor USF binds to and transactivates the promoter of the p53 tumor suppressor gene. Nucleic Acids Res. 21:1993;345-350.
    • (1993) Nucleic Acids Res , vol.21 , pp. 345-350
    • Reisman, D.1    Rotter, V.2
  • 48
    • 0030846296 scopus 로고    scopus 로고
    • The basic helix-loop-helix-zipper transcription factor USF1 regulates expression of the surfactant protein-A gene
    • Gao E., Wang Y., Alcorn J.L., Mendelson C.R. The basic helix-loop-helix-zipper transcription factor USF1 regulates expression of the surfactant protein-A gene. J Biol Chem. 272:1997;23398-23406.
    • (1997) J Biol Chem , vol.272 , pp. 23398-23406
    • Gao, E.1    Wang, Y.2    Alcorn, J.L.3    Mendelson, C.R.4
  • 49
    • 0026693875 scopus 로고
    • Definition of the transcriptional activation domain of recombinant 43-kilodalton USF
    • Kirschbaum B.J., Pognonec P., Roeder R.G. Definition of the transcriptional activation domain of recombinant 43-kilodalton USF. Mol Cell Biol. 12:1992;5094-5101.
    • (1992) Mol Cell Biol , vol.12 , pp. 5094-5101
    • Kirschbaum, B.J.1    Pognonec, P.2    Roeder, R.G.3
  • 50
    • 0031024584 scopus 로고    scopus 로고
    • Selective utilization of basic helix-loop-helix-leucine zipper proteins at the immunoglobulin heavy-chain enhancer
    • Carter R.S., Ordentlich P., Kadesch T. Selective utilization of basic helix-loop-helix-leucine zipper proteins at the immunoglobulin heavy-chain enhancer. Mol Cell Biol. 17:1997;18-23.
    • (1997) Mol Cell Biol , vol.17 , pp. 18-23
    • Carter, R.S.1    Ordentlich, P.2    Kadesch, T.3
  • 51
    • 0031005595 scopus 로고    scopus 로고
    • Autoactivation of Xenopus MyoD transcription and its inhibition by USF
    • Lun Y., Sawadogo M., Perry M. Autoactivation of Xenopus MyoD transcription and its inhibition by USF. Cell Growth Differ. 8:1997;275-282.
    • (1997) Cell Growth Differ , vol.8 , pp. 275-282
    • Lun, Y.1    Sawadogo, M.2    Perry, M.3
  • 52
    • 0032533771 scopus 로고    scopus 로고
    • Participation of upstream stimulatory factor (USF) in cadmium-induction of the mouse metallothionein-I gene
    • Li Q.W., Hu N.M., Daggett M.A.F., Chu W.A., Bittel D., Johnson J.A., Andrews G.K. Participation of upstream stimulatory factor (USF) in cadmium-induction of the mouse metallothionein-I gene. Nucleic Acids Res. 26:1998;5182-5189.
    • (1998) Nucleic Acids Res , vol.26 , pp. 5182-5189
    • Li, Q.W.1    Hu, N.M.2    Daggett, M.A.F.3    Chu, W.A.4    Bittel, D.5    Johnson, J.A.6    Andrews, G.K.7
  • 53
    • 0025944389 scopus 로고
    • Increase in metallothionein produced by chemicals that induce oxidative stress
    • Bauman J.W., Liu J., Liu Y.P., Klaassen C.D. Increase in metallothionein produced by chemicals that induce oxidative stress. Toxicol Appl Pharmacol. 110:1991;347-354.
    • (1991) Toxicol Appl Pharmacol , vol.110 , pp. 347-354
    • Bauman, J.W.1    Liu, J.2    Liu, Y.P.3    Klaassen, C.D.4
  • 54
    • 0027081945 scopus 로고
    • Examination of potential mechanism(s) of metallothionein induction by diethyl maleate
    • Bauman J.W., Liu Y.P., Andrews G.K., Klaassen C.D. Examination of potential mechanism(s) of metallothionein induction by diethyl maleate. Toxicol Appl Pharmacol. 117:1992;226-232.
    • (1992) Toxicol Appl Pharmacol , vol.117 , pp. 226-232
    • Bauman, J.W.1    Liu, Y.P.2    Andrews, G.K.3    Klaassen, C.D.4
  • 57
    • 0025989424 scopus 로고
    • Induction of hepatic metallothionein by nonmetallic compounds associated with acute-phase response in inflammation
    • Min K.-S., Terano Y., Onosaka S., Tanaka K. Induction of hepatic metallothionein by nonmetallic compounds associated with acute-phase response in inflammation. Toxicol Appl Pharmacol. 111:1991;152-162.
    • (1991) Toxicol Appl Pharmacol , vol.111 , pp. 152-162
    • Min, K.-S.1    Terano, Y.2    Onosaka, S.3    Tanaka, K.4
  • 58
    • 33751155885 scopus 로고
    • Role of quinone-mediated generation of hydroxyl radicals in the induction of glutathione S-transferase gene expression
    • Pinkus R., Weiner L.M., Daniel V. Role of quinone-mediated generation of hydroxyl radicals in the induction of glutathione S-transferase gene expression. Biochemistry. 34:1995;81-88.
    • (1995) Biochemistry , vol.34 , pp. 81-88
    • Pinkus, R.1    Weiner, L.M.2    Daniel, V.3
  • 59
    • 0029027838 scopus 로고
    • Electrophile and antioxidant regulation of enzymes that detoxify carcinogens
    • Prestera T., Talalay P. Electrophile and antioxidant regulation of enzymes that detoxify carcinogens. Proc Natl Acad Sci USA. 92:1995;8965-8969.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8965-8969
    • Prestera, T.1    Talalay, P.2
  • 60
    • 0029000906 scopus 로고
    • Antitumor promotion by phenolic antioxidants: Inhibition of AP-1 activity through induction of Fra expression
    • Yoshioka K., Deng T., Cavigelli M., Karin M. Antitumor promotion by phenolic antioxidants Inhibition of AP-1 activity through induction of Fra expression . Proc Natl Acad Sci USA. 92:1995;4972-4976.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4972-4976
    • Yoshioka, K.1    Deng, T.2    Cavigelli, M.3    Karin, M.4
  • 61
    • 0027278951 scopus 로고
    • Oxygen radical formation during prostaglandin H synthase-mediated biotransformation of butylated hydroxyanisole
    • Schilderman P.A., van Maanen J.M., Smeets E.J., ten Hoor F., Kleinjans J.C. Oxygen radical formation during prostaglandin H synthase-mediated biotransformation of butylated hydroxyanisole. Carcinogenesis. 14:1993;347-353.
    • (1993) Carcinogenesis , vol.14 , pp. 347-353
    • Schilderman, P.A.1    Van Maanen, J.M.2    Smeets, E.J.3    Ten Hoor, F.4    Kleinjans, J.C.5
  • 62
    • 0026657120 scopus 로고
    • Formation of the semiquinone anion radical from tert-butylquinone and from tert-butylhydroquinone in rat liver microsomes
    • Bergmann B., Dohrmann J.K., Kahl R. Formation of the semiquinone anion radical from tert-butylquinone and from tert-butylhydroquinone in rat liver microsomes. Toxicology. 74:1992;127-133.
    • (1992) Toxicology , vol.74 , pp. 127-133
    • Bergmann, B.1    Dohrmann, J.K.2    Kahl, R.3
  • 63
    • 0025105624 scopus 로고
    • Oxidant stress leads to transcriptional activation of the human heme oxygenase gene in cultured skin fibroblasts
    • Keyse S.M., Applegate L.A., Tromvoukis Y., Tyrrell R.M. Oxidant stress leads to transcriptional activation of the human heme oxygenase gene in cultured skin fibroblasts. Mol Cell Biol. 10:1990;4967-4969.
    • (1990) Mol Cell Biol , vol.10 , pp. 4967-4969
    • Keyse, S.M.1    Applegate, L.A.2    Tromvoukis, Y.3    Tyrrell, R.M.4
  • 64
    • 0023281199 scopus 로고
    • Both near ultraviolet radiation and the oxidizing agent hydrogen peroxide induce a 32-kDa stress protein in normal human skin fibroblasts
    • Keyse S.M., Tyrrell R.M. Both near ultraviolet radiation and the oxidizing agent hydrogen peroxide induce a 32-kDa stress protein in normal human skin fibroblasts. J Biol Chem. 262:1987;14821-14825.
    • (1987) J Biol Chem , vol.262 , pp. 14821-14825
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 65
    • 0024497521 scopus 로고
    • Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite
    • Keyse S.M., Tyrrell R.M. Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc Natl Acad Sci USA. 86:1989;99-103.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 66
    • 0026033907 scopus 로고
    • Induction of heme oxygenase: A general response to oxidant stress in cultured mammalian cells
    • Applegate L.A., Luscher P., Tyrrell R.M. Induction of heme oxygenase A general response to oxidant stress in cultured mammalian cells . Cancer Res. 51:1991;974-978.
    • (1991) Cancer Res , vol.51 , pp. 974-978
    • Applegate, L.A.1    Luscher, P.2    Tyrrell, R.M.3
  • 67
    • 0025271438 scopus 로고
    • Induction of the heme oxygenase gene in human skin fibroblasts by hydrogen peroxide and UVA (365 nm) radiation: Evidence for the involvement of the hydroxyl radical
    • Keyse S.M., Tyrrell R.M. Induction of the heme oxygenase gene in human skin fibroblasts by hydrogen peroxide and UVA (365 nm) radiation Evidence for the involvement of the hydroxyl radical . Carcinogenesis. 11:1990;787-791.
    • (1990) Carcinogenesis , vol.11 , pp. 787-791
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 68
    • 0019483405 scopus 로고
    • Transcriptional regulation of the mouse metallothionein-I gene by heavy metals
    • Durnam D.M., Palmiter R.D. Transcriptional regulation of the mouse metallothionein-I gene by heavy metals. J Biol Chem. 256:1981;5712-5716.
    • (1981) J Biol Chem , vol.256 , pp. 5712-5716
    • Durnam, D.M.1    Palmiter, R.D.2
  • 69
    • 0025948113 scopus 로고
    • The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
    • Rushmore T.H., Morton M.R., Pickett C.B. The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J Biol Chem. 266:1991;11632-11639.
    • (1991) J Biol Chem , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 70
    • 0024550092 scopus 로고
    • Fine mapping of a mouse metallothionein gene metal response element
    • Culotta V.C., Hamer D.H. Fine mapping of a mouse metallothionein gene metal response element. Mol Cell Biol. 9:1989;1376-1380.
    • (1989) Mol Cell Biol , vol.9 , pp. 1376-1380
    • Culotta, V.C.1    Hamer, D.H.2
  • 71
    • 0024997241 scopus 로고
    • Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants
    • Rushmore T.H., Pickett C.B. Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants. J Biol Chem. 265:1990;14648-14653.
    • (1990) J Biol Chem , vol.265 , pp. 14648-14653
    • Rushmore, T.H.1    Pickett, C.B.2
  • 73
    • 0023986832 scopus 로고
    • Constitutive and metal-inducible protein: DNA interactions at the mouse metallothionein I promoter examined by in vivo and in vitro footprinting
    • Mueller P.R., Salser S.J., Wold B. Constitutive and metal-inducible protein DNA interactions at the mouse metallothionein I promoter examined by in vivo and in vitro footprinting . Genes Dev. 2:1988;412-427.
    • (1988) Genes Dev , vol.2 , pp. 412-427
    • Mueller, P.R.1    Salser, S.J.2    Wold, B.3
  • 74
    • 0028802636 scopus 로고
    • The rat quinone reductase antioxidant response element. Identification of the nucleotide sequence required for basal and inducible activity and detection of antioxidant response element-binding proteins in hepatoma and non-hepatoma cell lines
    • Favreau L.V., Pickett C.B. The rat quinone reductase antioxidant response element. Identification of the nucleotide sequence required for basal and inducible activity and detection of antioxidant response element-binding proteins in hepatoma and non-hepatoma cell lines. J Biol Chem. 270:1995;24468-24474.
    • (1995) J Biol Chem , vol.270 , pp. 24468-24474
    • Favreau, L.V.1    Pickett, C.B.2
  • 75
    • 0028364075 scopus 로고
    • Transcriptional regulation of a rat liver glutathione S-transferase Ya subunit gene. Analysis of the antioxidant response element and its activation by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate
    • Nguyen T., Rushmore T.H., Pickett C.B. Transcriptional regulation of a rat liver glutathione S-transferase Ya subunit gene. Analysis of the antioxidant response element and its activation by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate. J Biol Chem. 269:1994;13656-13662.
    • (1994) J Biol Chem , vol.269 , pp. 13656-13662
    • Nguyen, T.1    Rushmore, T.H.2    Pickett, C.B.3
  • 77
    • 0028798434 scopus 로고
    • Oxidative mechanisms in the toxicity of metal ions
    • Stohs S.J., Bagchi D. Oxidative mechanisms in the toxicity of metal ions. Free Radic Biol Med. 18:1995;321-336.
    • (1995) Free Radic Biol Med , vol.18 , pp. 321-336
    • Stohs, S.J.1    Bagchi, D.2
  • 78
    • 0027319872 scopus 로고
    • 2+ -induced c-myc mRNA accumulation in NRK-49F cells is blocked by the protein kinase inhibitor H7 but not by HA1004, indicating that protein kinase C is a mediator of the response
    • 2+ -induced c-myc mRNA accumulation in NRK-49F cells is blocked by the protein kinase inhibitor H7 but not by HA1004, indicating that protein kinase C is a mediator of the response. Toxicology. 81:1993;155-164.
    • (1993) Toxicology , vol.81 , pp. 155-164
    • Tang, N.1    Enger, M.D.2
  • 80
    • 0025876960 scopus 로고
    • In vivo effects of cadmium on calmodulin and calmodulin regulated enzymes in rat brain
    • Vig P.J.S., Nath R. In vivo effects of cadmium on calmodulin and calmodulin regulated enzymes in rat brain. Biochem Int. 23:1991;927-934.
    • (1991) Biochem Int , vol.23 , pp. 927-934
    • Vig, P.J.S.1    Nath, R.2
  • 81
    • 0024519393 scopus 로고
    • Cadmium evokes inositol polyphosphate formation and calcium mobilization. Evidence for a cell surface receptor that cadmium stimulates and zinc antagonizes
    • Smith J.B., Dwyer S.D., Smith L. Cadmium evokes inositol polyphosphate formation and calcium mobilization. Evidence for a cell surface receptor that cadmium stimulates and zinc antagonizes. J Biol Chem. 264:1989;7115-7118.
    • (1989) J Biol Chem , vol.264 , pp. 7115-7118
    • Smith, J.B.1    Dwyer, S.D.2    Smith, L.3
  • 82
    • 0020471220 scopus 로고
    • Enhancement of rat and human phagocyte superoxide anion radical production by cadmium in vitro
    • Amoruso M.A., Witz G., Goldstein B.D. Enhancement of rat and human phagocyte superoxide anion radical production by cadmium in vitro. Toxicol Lett. 10:1982;133-138.
    • (1982) Toxicol Lett , vol.10 , pp. 133-138
    • Amoruso, M.A.1    Witz, G.2    Goldstein, B.D.3
  • 83
    • 0026549103 scopus 로고
    • Transforming growth factor β1-responsive element: Closely associated binding sites for USF and CCAAT-binding transcription factor-nuclear factor I in the type 1 plasminogen activator inhibitor gene
    • Riccio A., Pedone P.V., Lund L.R., Olesen T., Olsen H.S., Andreasen P.A. Transforming growth factor β1-responsive element Closely associated binding sites for USF and CCAAT-binding transcription factor-nuclear factor I in the type 1 plasminogen activator inhibitor gene . Mol Cell Biol. 12:1992;1846-1855.
    • (1992) Mol Cell Biol , vol.12 , pp. 1846-1855
    • Riccio, A.1    Pedone, P.V.2    Lund, L.R.3    Olesen, T.4    Olsen, H.S.5    Andreasen, P.A.6
  • 84
    • 0030890418 scopus 로고    scopus 로고
    • A three-protein-DNA complex on a B cell-specific domain of the immunoglobulin mu heavy chain gene enhancer
    • Rao E., Dang W., Tian G., Sen R. A three-protein-DNA complex on a B cell-specific domain of the immunoglobulin mu heavy chain gene enhancer. J Biol Chem. 272:1997;6722-6732.
    • (1997) J Biol Chem , vol.272 , pp. 6722-6732
    • Rao, E.1    Dang, W.2    Tian, G.3    Sen, R.4
  • 85
    • 0030038632 scopus 로고    scopus 로고
    • Participation of altered upstream stimulatory factor in the induction of rat heme oxygenase-1 by cadmium
    • Maeshima H., Sato M., Ishikawa K., Katagata Y., Yoshida T. Participation of altered upstream stimulatory factor in the induction of rat heme oxygenase-1 by cadmium. Nucleic Acids Res. 24:1996;2959-2965.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2959-2965
    • Maeshima, H.1    Sato, M.2    Ishikawa, K.3    Katagata, Y.4    Yoshida, T.5
  • 86
    • 0028125990 scopus 로고
    • Regulation of metallothionein genes by heavy metals appears to be mediated by a zinc-sensitive inhibitor that interacts with a constitutively active transcription factor, MTF-1
    • Palmiter R.D. Regulation of metallothionein genes by heavy metals appears to be mediated by a zinc-sensitive inhibitor that interacts with a constitutively active transcription factor, MTF-1. Proc Natl Acad Sci USA. 91:1994;1219-1223.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1219-1223
    • Palmiter, R.D.1
  • 87
    • 0032508398 scopus 로고    scopus 로고
    • Structural and functional heterogeneity among the zinc fingers of human MRE-binding transcription factor-1
    • Chen X.H., Agarwal A., Giedroc D.P. Structural and functional heterogeneity among the zinc fingers of human MRE-binding transcription factor-1. Biochemistry. 37:1998;11152-11161.
    • (1998) Biochemistry , vol.37 , pp. 11152-11161
    • Chen, X.H.1    Agarwal, A.2    Giedroc, D.P.3
  • 88
    • 0025828493 scopus 로고
    • Transcriptional control by nuclear receptors
    • Beato M. Transcriptional control by nuclear receptors. FASEB J. 5:1991;2044-2051.
    • (1991) FASEB J , vol.5 , pp. 2044-2051
    • Beato, M.1
  • 89
    • 0026743186 scopus 로고
    • Expression of a yeast metallothionein gene family is activated by a single metalloregulatory transcription factor
    • Zhou P., Szczypka M.S., Sosinowski T., Thiele D.J. Expression of a yeast metallothionein gene family is activated by a single metalloregulatory transcription factor. Mol Cell Biol. 12:1992;3766-3775.
    • (1992) Mol Cell Biol , vol.12 , pp. 3766-3775
    • Zhou, P.1    Szczypka, M.S.2    Sosinowski, T.3    Thiele, D.J.4
  • 90
    • 0005791294 scopus 로고
    • Cooperative activation of a eukaryotic transcription factor: Interaction between Cu(I) and yeast ACE1 protein
    • Fürst P., Hamer D. Cooperative activation of a eukaryotic transcription factor Interaction between Cu(I) and yeast ACE1 protein . Proc Natl Acad Sci USA. 86:1989;5267-5271.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5267-5271
    • Fürst, P.1    Hamer, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.