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Volumn 284, Issue 4 53-4, 2003, Pages

Heme activates the heme oxygenase-1 gene in renal epithelial cells by stabilizing Nrf2

Author keywords

Nrf2 transcription factor; Protein stabilization; Stress response element

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 3; BINDING PROTEIN; HEME; HEME OXYGENASE 1; LUCIFERASE; MESSENGER RNA; PROTEIN C JUN; PROTEIN FOS; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR MAFG; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG;

EID: 0037377144     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.00376.2002     Document Type: Article
Times cited : (157)

References (55)
  • 1
    • 0021100151 scopus 로고
    • Hemin-mediated DNA strand scission
    • Aft RL and Mueller GC. Hemin-mediated DNA strand scission. J Biol Chem 258: 12069-12072, 1983.
    • (1983) J Biol Chem , vol.258 , pp. 12069-12072
    • Aft, R.L.1    Mueller, G.C.2
  • 2
    • 0021322523 scopus 로고
    • Hemin-mediated oxidative degradation of proteins
    • Aft RL and Mueller GC. Hemin-mediated oxidative degradation of proteins. J Biol Chem 259: 301-305, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 301-305
    • Aft, R.L.1    Mueller, G.C.2
  • 3
    • 0031883280 scopus 로고    scopus 로고
    • A dominant-negative inhibitor of CREB reveals that it is a general mediator of stimulus-dependent transcription of e-fos
    • Ahn S, Olive M, Aggarwal S, Krylov D, Ginty DD, and Vinson C. A dominant-negative inhibitor of CREB reveals that it is a general mediator of stimulus-dependent transcription of e-fos. Mol Cell Biol 18: 967-977, 1998.
    • (1998) Mol Cell Biol , vol.18 , pp. 967-977
    • Ahn, S.1    Olive, M.2    Aggarwal, S.3    Krylov, D.4    Ginty, D.D.5    Vinson, C.6
  • 4
    • 0002798029 scopus 로고    scopus 로고
    • Functional analysis of the heme oxygenase-1 gene promoter
    • edited by Maines MD, Costa LG, Reed DJ, Sassa S, and Sipes IG. New York: Wiley
    • Alam J. Functional analysis of the heme oxygenase-1 gene promoter. In: Current Protocols in Toxicology, edited by Maines MD, Costa LG, Reed DJ, Sassa S, and Sipes IG. New York: Wiley, 2000, p. 9.7.1-9.7.21.
    • (2000) Current Protocols in Toxicology , pp. 971-9721
    • Alam, J.1
  • 5
    • 0028039868 scopus 로고
    • Isolation and characterization of the mouse heme oxygenase-1 gene. Distal 5′ sequences are required for induction by heme or heavy metals
    • Alam J, Cai J, and Smith A. Isolation and characterization of the mouse heme oxygenase-1 gene. Distal 5′ sequences are required for induction by heme or heavy metals. J Biol Chem 269: 1001-1009, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 1001-1009
    • Alam, J.1    Cai, J.2    Smith, A.3
  • 6
    • 0033543566 scopus 로고    scopus 로고
    • Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene
    • Alam J, Stewart D, Touchard C, Boinapally S, Choi AM, and Cook JL. Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene. J Biol Chem 274: 26071-26078, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 26071-26078
    • Alam, J.1    Stewart, D.2    Touchard, C.3    Boinapally, S.4    Choi, A.M.5    Cook, J.L.6
  • 7
    • 0034623211 scopus 로고    scopus 로고
    • Mechanism of heme oxygenase-1 gene activation by cadmium in MCF-7 mammary epithelial cells. Role of p38 kinase and Nrf2 transcription factor
    • Alam J, Wicks C, Stewart D, Gong P, Touchard C, Otterbein S, Choi AM, Burow ME, and Tou J. Mechanism of heme oxygenase-1 gene activation by cadmium in MCF-7 mammary epithelial cells. Role of p38 kinase and Nrf2 transcription factor. J Biol Chem 275: 27694-27702, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 27694-27702
    • Alam, J.1    Wicks, C.2    Stewart, D.3    Gong, P.4    Touchard, C.5    Otterbein, S.6    Choi, A.M.7    Burow, M.E.8    Tou, J.9
  • 8
    • 0027243681 scopus 로고
    • Erythroid transcription factor NF-E2 is a haematopoietic-specific basic-leucine zipper protein
    • Andrews NC, Erdjument-Bromage H, Davidson MB, Tempst P, and Orkin SH. Erythroid transcription factor NF-E2 is a haematopoietic-specific basic-leucine zipper protein. Nature 362: 722-728, 1993.
    • (1993) Nature , vol.362 , pp. 722-728
    • Andrews, N.C.1    Erdjument-Bromage, H.2    Davidson, M.B.3    Tempst, P.4    Orkin, S.H.5
  • 9
    • 0026318447 scopus 로고
    • Hemin: A possible physiological mediator of low density lipoprotein oxidation and endothelial injury
    • Balla G, Jacob HS, Eaton JW, Belcher JD, and Vercellotti GM. Hemin: a possible physiological mediator of low density lipoprotein oxidation and endothelial injury. Arterioscler Thromb 11: 1700-1711, 1991.
    • (1991) Arterioscler Thromb , vol.11 , pp. 1700-1711
    • Balla, G.1    Jacob, H.S.2    Eaton, J.W.3    Belcher, J.D.4    Vercellotti, G.M.5
  • 10
    • 0025819677 scopus 로고
    • Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species
    • Balla G, Vercellotti GM, Muller-Eberhard U, Eaton J, and Jacob HS. Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species. Lab Invest 64: 648-655, 1991.
    • (1991) Lab Invest , vol.64 , pp. 648-655
    • Balla, G.1    Vercellotti, G.M.2    Muller-Eberhard, U.3    Eaton, J.4    Jacob, H.S.5
  • 11
    • 0027358877 scopus 로고
    • Endothelial-cell heme uptake from heme proteins: Induction of sensitization and desensitization to oxidant damage
    • Balla J, Jacob HS, Balla G, Nath K, Eaton JW, and Vercellotti GM. Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage. Proc Natl Acad Sci USA 90: 9285-9289, 1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9285-9289
    • Balla, J.1    Jacob, H.S.2    Balla, G.3    Nath, K.4    Eaton, J.W.5    Vercellotti, G.M.6
  • 12
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162: 156-159, 1987.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 13
    • 0035963293 scopus 로고    scopus 로고
    • Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H: Quinone oxidoreductasel gene
    • Dhakshinamoorthy S and Jaiswal AK. Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H: quinone oxidoreductasel gene. Oncogene 20: 3906-3917, 2001.
    • (2001) Oncogene , vol.20 , pp. 3906-3917
    • Dhakshinamoorthy, S.1    Jaiswal, A.K.2
  • 14
    • 0033643459 scopus 로고    scopus 로고
    • Antioxidant regulation of genes encoding enzymes that detoxify xenobiotics and carcinogens
    • Dhakshinamoorthy S, Long DJ II, and Jaiswal AK. Antioxidant regulation of genes encoding enzymes that detoxify xenobiotics and carcinogens. Curr Top Cell Regul 36: 201-216, 2000.
    • (2000) Curr Top Cell Regul , vol.36 , pp. 201-216
    • Dhakshinamoorthy, S.1    Long D.J. II2    Jaiswal, A.K.3
  • 15
    • 0035920132 scopus 로고    scopus 로고
    • Cobalt induces heme oxygenase-1 expression by a hypoxia-inducible factor-independent mechanism in Chinese hamster ovary cells: Regulation by Nrf2 and MafG transcription factors
    • Gong P, Hu B, Stewart D, Ellerbe M, Figueroa YG, Blank V, Beckman BS, and Alam J. Cobalt induces heme oxygenase-1 expression by a hypoxia-inducible factor-independent mechanism in Chinese hamster ovary cells: regulation by Nrf2 and MafG transcription factors. J Biol Chem 276: 27018-27025, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 27018-27025
    • Gong, P.1    Hu, B.2    Stewart, D.3    Ellerbe, M.4    Figueroa, Y.G.5    Blank, V.6    Beckman, B.S.7    Alam, J.8
  • 16
    • 0034020776 scopus 로고    scopus 로고
    • Inhibitory effects of heavy metals on transcription factor Sp1
    • Gong P, Ogra Y, and Koizumi S. Inhibitory effects of heavy metals on transcription factor Sp1. Ind Health 38: 224-227, 2000.
    • (2000) Ind Health , vol.38 , pp. 224-227
    • Gong, P.1    Ogra, Y.2    Koizumi, S.3
  • 17
    • 0036090689 scopus 로고    scopus 로고
    • Activation of the mouse heme oxygenase-1 gene by 15-deoxydelta 12,14-prostaglan din j2 is mediated by the stress response elements and transcription factor nrf2
    • Gong P, Stewart D, Hu B, Li N, Cook J, Nel A, and Alam J. Activation of the mouse heme oxygenase-1 gene by 15-deoxydelta 12,14-prostaglan din j2 is mediated by the stress response elements and transcription factor nrf2. Antioxid Redox Signal 4: 249-257, 2002.
    • (2002) Antioxid Redox Signal , vol.4 , pp. 249-257
    • Gong, P.1    Stewart, D.2    Hu, B.3    Li, N.4    Cook, J.5    Nel, A.6    Alam, J.7
  • 19
    • 0035877643 scopus 로고    scopus 로고
    • Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein, Implication for heme oxygenase-1 gene regulation
    • He CH, Gong P, Hu B, Stewart D, Choi ME, Choi AM, and Alam J. Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein, Implication for heme oxygenase-1 gene regulation. J Biol Chem 276: 20858-20865, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 20858-20865
    • He, C.H.1    Gong, P.2    Hu, B.3    Stewart, D.4    Choi, M.E.5    Choi, A.M.6    Alam, J.7
  • 20
    • 0024551404 scopus 로고
    • Pathobiology of heme interaction with the erythrocyte membrane
    • Hebbel RP and Eaton JW. Pathobiology of heme interaction with the erythrocyte membrane. Semin Hematol 26: 136-149, 1989.
    • (1989) Semin Hematol , vol.26 , pp. 136-149
    • Hebbel, R.P.1    Eaton, J.W.2
  • 22
    • 0033731182 scopus 로고    scopus 로고
    • Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2
    • Huang HC, Nguyen T, and Pickett CB. Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2. Proc Natl Acad Sci USA 97: 12475-12480, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12475-12480
    • Huang, H.C.1    Nguyen, T.2    Pickett, C.B.3
  • 23
    • 0029043995 scopus 로고
    • Cloning and characterization of a novel erythroid cell-derived CNC family transcription factor heterodimerizing with the small Maf family proteins
    • Itoh K, Igarashi K, Hayashi N, Nishizawa M, and Yamamoto M. Cloning and characterization of a novel erythroid cell-derived CNC family transcription factor heterodimerizing with the small Maf family proteins. Mol Cell Biol 15: 4184-4193, 1995.
    • (1995) Mol Cell Biol , vol.15 , pp. 4184-4193
    • Itoh, K.1    Igarashi, K.2    Hayashi, N.3    Nishizawa, M.4    Yamamoto, M.5
  • 24
    • 0032827002 scopus 로고    scopus 로고
    • Regulatory mechanisms of cellular response to oxidative stress
    • Itoh K, Ishii T, Wakabayashi N, and Yamamoto M. Regulatory mechanisms of cellular response to oxidative stress. Free Radic Res 31: 319-324, 1999.
    • (1999) Free Radic Res , vol.31 , pp. 319-324
    • Itoh, K.1    Ishii, T.2    Wakabayashi, N.3    Yamamoto, M.4
  • 25
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K, Wakabayashi N, Katoh Y, Ishii T, Igarashi K, Engel JD, and Yamamoto M. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev 13: 76-86, 1999.
    • (1999) Genes Dev , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 26
    • 0032538797 scopus 로고    scopus 로고
    • Signal transduction in hypoxic cells: Inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1α
    • Kallio PJ, Okamoto K, O'Brien S, Carrero P, Makino Y, Tanaka H, and Poellinger L. Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1α. EMBO J 17: 6573-6586, 1998.
    • (1998) EMBO J , vol.17 , pp. 6573-6586
    • Kallio, P.J.1    Okamoto, K.2    O'Brien, S.3    Carrero, P.4    Makino, Y.5    Tanaka, H.6    Poellinger, L.7
  • 28
    • 0027954409 scopus 로고
    • Maf nuclear oncoprotein recognizes sequences related to an AP-1 site and forms heterodimers with both Fos and Jun
    • Kataoka K, Noda M, and Nishizawa M. Maf nuclear oncoprotein recognizes sequences related to an AP-1 site and forms heterodimers with both Fos and Jun. Mol Cell Biol 14: 700-712, 1994.
    • (1994) Mol Cell Biol , vol.14 , pp. 700-712
    • Kataoka, K.1    Noda, M.2    Nishizawa, M.3
  • 29
    • 0035947654 scopus 로고    scopus 로고
    • Hemin-induced activation of the thioredoxin gene by Nrf2. A differential regulation of the antioxidant responsive element by a switch of its binding factors
    • Kim YC, Masutani H, Yamaguchi Y, Itoh K, Yamamoto M, and Yodoi J. Hemin-induced activation of the thioredoxin gene by Nrf2. A differential regulation of the antioxidant responsive element by a switch of its binding factors. J Biol Chem 276: 18399-18406, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 18399-18406
    • Kim, Y.C.1    Masutani, H.2    Yamaguchi, Y.3    Itoh, K.4    Yamamoto, M.5    Yodoi, J.6
  • 31
    • 0029055185 scopus 로고
    • Dependence of globin gene expression in mouse erythroleukemia cells on the NF-E2 heterodimer
    • Kotkow KJ and Orkin SH. Dependence of globin gene expression in mouse erythroleukemia cells on the NF-E2 heterodimer. Mol Cell Biol 15: 4640-4647, 1995.
    • (1995) Mol Cell Biol , vol.15 , pp. 4640-4647
    • Kotkow, K.J.1    Orkin, S.H.2
  • 32
    • 0035573719 scopus 로고    scopus 로고
    • The heme oxygenase system and cellular defense mechanisms. Do HO-1 and HO-2 have different functions?
    • Maines MD and Panahian N. The heme oxygenase system and cellular defense mechanisms. Do HO-1 and HO-2 have different functions? Adv Exp Med Biol 502: 249-272, 2001.
    • (2001) Adv Exp Med Biol , vol.502 , pp. 249-272
    • Maines, M.D.1    Panahian, N.2
  • 33
    • 0030974478 scopus 로고    scopus 로고
    • hMAF, a small human transcription factor that heterodimerizes specifically with Nrf1 and Nrf2
    • Marini MG, Chan K, Casula L, Kan YW, Cao A, and Moi P. hMAF, a small human transcription factor that heterodimerizes specifically with Nrf1 and Nrf2. J Biol Chem 272: 16490-16497, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 16490-16497
    • Marini, M.G.1    Chan, K.2    Casula, L.3    Kan, Y.W.4    Cao, A.5    Moi, P.6
  • 36
    • 0027498438 scopus 로고
    • Bioactivity of heme and its containment
    • Muller-Eberhard U and Fraig M. Bioactivity of heme and its containment. Am J Hematol 42: 59-62, 1993.
    • (1993) Am J Hematol , vol.42 , pp. 59-62
    • Muller-Eberhard, U.1    Fraig, M.2
  • 37
    • 0032967906 scopus 로고    scopus 로고
    • Differential metal response and regulation of human heavy metal-inducible genes
    • Murata M, Gong P, Suzuki K, and Koizumi S. Differential metal response and regulation of human heavy metal-inducible genes. J Cell Physiol 180: 105-113, 1999.
    • (1999) J Cell Physiol , vol.180 , pp. 105-113
    • Murata, M.1    Gong, P.2    Suzuki, K.3    Koizumi, S.4
  • 39
    • 0028900182 scopus 로고
    • Heme protein-mediated renal injury: A protective role for 21-amino-steroids in vitro and in vivo
    • Nath KA, Balla J, Croatt AJ, and Vercellotti GM. Heme protein-mediated renal injury: a protective role for 21-amino-steroids in vitro and in vivo. Kidney Int 47: 592-602, 1995.
    • (1995) Kidney Int , vol.47 , pp. 592-602
    • Nath, K.A.1    Balla, J.2    Croatt, A.J.3    Vercellotti, G.M.4
  • 41
    • 0033847184 scopus 로고    scopus 로고
    • The indispensability of heme oxygenase-1 in protecting against acute heme protein-induced toxicity in vivo
    • Nath KA, Haggard JJ, Croatt AJ, Grande JP, Poss KD, and Alam J. The indispensability of heme oxygenase-1 in protecting against acute heme protein-induced toxicity in vivo. Am J Pathol 156: 1527-1535, 2000.
    • (2000) Am J Pathol , vol.156 , pp. 1527-1535
    • Nath, K.A.1    Haggard, J.J.2    Croatt, A.J.3    Grande, J.P.4    Poss, K.D.5    Alam, J.6
  • 44
    • 0030802419 scopus 로고    scopus 로고
    • A dominant negative to activation protein-1 (AP1) that abolishes DNA binding and inhibits oncogenesis
    • Olive M, Krylov D, Echlin DR, Gardner K, Taparowsky E, and Vinson C. A dominant negative to activation protein-1 (AP1) that abolishes DNA binding and inhibits oncogenesis. J Biol Chem 272: 18586-18594, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 18586-18594
    • Olive, M.1    Krylov, D.2    Echlin, D.R.3    Gardner, K.4    Taparowsky, E.5    Vinson, C.6
  • 45
    • 0033579570 scopus 로고    scopus 로고
    • Degradation of the basic helix-loop-helix/Per-ARNT-Sim homology domain dioxin receptor via the ubiquitin/proteasome pathway
    • Roberts BJ and Whitelaw ML. Degradation of the basic helix-loop-helix/Per-ARNT-Sim homology domain dioxin receptor via the ubiquitin/proteasome pathway. J Biol Chem 274: 36351-36356, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 36351-36356
    • Roberts, B.J.1    Whitelaw, M.L.2
  • 47
    • 0027493650 scopus 로고
    • A single phosphotyrosine residue of Stat91 required for gene activation by interferon-γ
    • Shuai K, Stark GR, Kerr IM, and Darnell JE Jr. A single phosphotyrosine residue of Stat91 required for gene activation by interferon-γ. Science 261: 1744-1746, 1993.
    • (1993) Science , vol.261 , pp. 1744-1746
    • Shuai, K.1    Stark, G.R.2    Kerr, I.M.3    Darnell J.E., Jr.4
  • 48
    • 0025368527 scopus 로고
    • Induction of haem oxygenase as a defence against oxidative stress
    • Stocker R. Induction of haem oxygenase as a defence against oxidative stress. Free Radic Res Commun 9: 101-112, 1990.
    • (1990) Free Radic Res Commun , vol.9 , pp. 101-112
    • Stocker, R.1
  • 49
    • 0025150585 scopus 로고
    • Antioxidant activities of bile pigments: Biliverdin and bilirubin
    • Stocker R, McDonagh AF, Glazer AN, and Ames BN. Antioxidant activities of bile pigments: biliverdin and bilirubin. Methods Enzymol 186: 301-309, 1990.
    • (1990) Methods Enzymol , vol.186 , pp. 301-309
    • Stocker, R.1    McDonagh, A.F.2    Glazer, A.N.3    Ames, B.N.4
  • 52
    • 0032542213 scopus 로고    scopus 로고
    • Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes
    • Venugopal R and Jaiswal AK. Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes. Oncogene 17: 3145-3156, 1998.
    • (1998) Oncogene , vol.17 , pp. 3145-3156
    • Venugopal, R.1    Jaiswal, A.K.2
  • 53
    • 0028941025 scopus 로고
    • Acquired resistance to acute oxidative stress. Possible role of heme oxygenase and ferritin
    • Vogt BA, Alam J, Croatt AJ, Vercellotti GM, and Nath KA. Acquired resistance to acute oxidative stress. Possible role of heme oxygenase and ferritin. Lab Invest 72: 474-483, 1995.
    • (1995) Lab Invest , vol.72 , pp. 474-483
    • Vogt, B.A.1    Alam, J.2    Croatt, A.J.3    Vercellotti, G.M.4    Nath, K.A.5
  • 55
    • 0037183998 scopus 로고    scopus 로고
    • The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
    • Zipper LM and Mulcahy RT. The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm. J Biol Chem 277: 36544-36552, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 36544-36552
    • Zipper, L.M.1    Mulcahy, R.T.2


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