메뉴 건너뛰기




Volumn 35, Issue 21, 2007, Pages 7074-7086

Heme oxygenase-1 induction by NRF2 requires inactivation of the transcriptional repressor BACH1

Author keywords

[No Author keywords available]

Indexed keywords

HEME OXYGENASE 1; THIOREDOXIN REDUCTASE; THIOREDOXIN REDUCTASE 1; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR BACH 1; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG;

EID: 37549050907     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm638     Document Type: Article
Times cited : (306)

References (39)
  • 1
    • 17444432962 scopus 로고    scopus 로고
    • Thermodynamics of the As(III)-thiol interaction: Arsenite and monomethylarsenite complexes with glutathione, dihydrolipoic acid, and other thiol ligands
    • Spuches,A.M., Kruszyna,H.G., Rich,A.M. and Wilcox,D.E. (2005) Thermodynamics of the As(III)-thiol interaction: Arsenite and monomethylarsenite complexes with glutathione, dihydrolipoic acid, and other thiol ligands. Inorg. Chem., 44, 2964-2972.
    • (2005) Inorg. Chem , vol.44 , pp. 2964-2972
    • Spuches, A.M.1    Kruszyna, H.G.2    Rich, A.M.3    Wilcox, D.E.4
  • 2
    • 0742289410 scopus 로고    scopus 로고
    • Oxidative mechanism of arsenic toxicity and carcinogenesis
    • Shi,H., Shi,X. and Liu,K.J. (2004) Oxidative mechanism of arsenic toxicity and carcinogenesis. Mol. Cell Biochem., 255, 67-78.
    • (2004) Mol. Cell Biochem , vol.255 , pp. 67-78
    • Shi, H.1    Shi, X.2    Liu, K.J.3
  • 3
    • 24944471482 scopus 로고    scopus 로고
    • Butylhydroquinone protects cells genetically deficient in glutathione biosynthesis from arsenite-induced apoptosis without significantly changing their prooxidant status
    • Kann,S., Estes,C., Reichard,J.F., Huang,M.Y., Sartor,M.A., Schwemberger,S., Chen,Y., Dalton,T.P., Shertzer,H.G. et al. (2005) Butylhydroquinone protects cells genetically deficient in glutathione biosynthesis from arsenite-induced apoptosis without significantly changing their prooxidant status. Toxicol. Sci., 87, 365-384.
    • (2005) Toxicol. Sci , vol.87 , pp. 365-384
    • Kann, S.1    Estes, C.2    Reichard, J.F.3    Huang, M.Y.4    Sartor, M.A.5    Schwemberger, S.6    Chen, Y.7    Dalton, T.P.8    Shertzer, H.G.9
  • 5
    • 0031000208 scopus 로고    scopus 로고
    • Functional antioxidant responsive elements
    • Wasserman,W.W. and Fahl,W.E. (1997) Functional antioxidant responsive elements. Proc. Natl Acad. Sci. USA, 94, 5361-5366.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5361-5366
    • Wasserman, W.W.1    Fahl, W.E.2
  • 6
    • 33748049771 scopus 로고    scopus 로고
    • Cross-species annotation of basic leucine zipper factor interactions: Insight into the evolution of closed interaction networks
    • Deppmann,C.D., Alvania,R.S. and Taparowsky,E.J. (2006) Cross-species annotation of basic leucine zipper factor interactions: Insight into the evolution of closed interaction networks. Mol. Biol. Evol., 23 1480-1492.
    • (2006) Mol. Biol. Evol , vol.23 , pp. 1480-1492
    • Deppmann, C.D.1    Alvania, R.S.2    Taparowsky, E.J.3
  • 7
    • 0037055265 scopus 로고    scopus 로고
    • Integration and diversity of the regulatory network composed of Maf and CNC families of transcription factors
    • Motohashi,H., O'Connor,T., Katsuoka,F., Engel,J.D. and Yamamoto,M. (2002) Integration and diversity of the regulatory network composed of Maf and CNC families of transcription factors. Gene, 294, 1-12.
    • (2002) Gene , vol.294 , pp. 1-12
    • Motohashi, H.1    O'Connor, T.2    Katsuoka, F.3    Engel, J.D.4    Yamamoto, M.5
  • 8
    • 0029906134 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:qUinone oxidoreductase1 gene
    • Venugopal,R. and Jaiswal,A.K. (1996) Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:qUinone oxidoreductase1 gene. Proc. Natl Acad. Sci. USA, 93, 14960-14965.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14960-14965
    • Venugopal, R.1    Jaiswal, A.K.2
  • 9
    • 10944235410 scopus 로고    scopus 로고
    • Nrf3 negatively regulates antioxidant-response element-mediated expression and antioxidant induction of NAD(P)H:qUinone oxidoreductase1 gene
    • Sankaranarayanan,K. and Jaiswal,A.K. (2004) Nrf3 negatively regulates antioxidant-response element-mediated expression and antioxidant induction of NAD(P)H:qUinone oxidoreductase1 gene. J. Biol. Chem., 279, 50810-50817.
    • (2004) J. Biol. Chem , vol.279 , pp. 50810-50817
    • Sankaranarayanan, K.1    Jaiswal, A.K.2
  • 10
    • 20444480956 scopus 로고    scopus 로고
    • Bach1 competes with Nrf2 leading to negative regulation of the antioxidant response element (ARE)-mediated NAD(P)H:qUinone oxidoreductase 1 gene expression and induction in response to antioxidants
    • Dhakshinamoorthy,S., Jain,A.K., Bloom,D.A. and Jaiswal,A.K. (2005) Bach1 competes with Nrf2 leading to negative regulation of the antioxidant response element (ARE)-mediated NAD(P)H:qUinone oxidoreductase 1 gene expression and induction in response to antioxidants. J. Biol. Chem. 280, 16891-16900.
    • (2005) J. Biol. Chem , vol.280 , pp. 16891-16900
    • Dhakshinamoorthy, S.1    Jain, A.K.2    Bloom, D.A.3    Jaiswal, A.K.4
  • 11
    • 33847611443 scopus 로고    scopus 로고
    • One billion years of bZIP transcription factor evolution: Conservation and change in dimerization, and DNA-binding site specificity
    • Amoutzias,G., Veron,A., Weiner,A., Robinson-Rechavi,M., Bornberg-Bauer,E., Oliver,S. and Robertson,D. (2006) One billion years of bZIP transcription factor evolution: Conservation and change in dimerization, and DNA-binding site specificity. Mol. Biol. Evol., 24, 827-835.
    • (2006) Mol. Biol. Evol , vol.24 , pp. 827-835
    • Amoutzias, G.1    Veron, A.2    Weiner, A.3    Robinson-Rechavi, M.4    Bornberg-Bauer, E.5    Oliver, S.6    Robertson, D.7
  • 12
    • 0032496139 scopus 로고    scopus 로고
    • Multivalent DNA binding complex generated by small Maf and Bach1 as a possible biochemical basis for beta-globin locus control region complex
    • Igarashi,K., Hoshino,H., Muto,A., Suwabe,N., Nishikawa,S., Nakauchi,H. and Yamamoto,M. (1998) Multivalent DNA binding complex generated by small Maf and Bach1 as a possible biochemical basis for beta-globin locus control region complex. J. Biol. Chem., 273, 11783-11790.
    • (1998) J. Biol. Chem , vol.273 , pp. 11783-11790
    • Igarashi, K.1    Hoshino, H.2    Muto, A.3    Suwabe, N.4    Nishikawa, S.5    Nakauchi, H.6    Yamamoto, M.7
  • 13
    • 0029805130 scopus 로고    scopus 로고
    • Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site
    • Oyake,T., Itoh,K., Motohashi,H., Hayashi,N., Hoshino,H., Nishizawa,M., Yamamoto,M. and Igarashi,K. (1996) Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site. Mol. Cell. Biol., 16, 6083-6095.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 6083-6095
    • Oyake, T.1    Itoh, K.2    Motohashi, H.3    Hayashi, N.4    Hoshino, H.5    Nishizawa, M.6    Yamamoto, M.7    Igarashi, K.8
  • 15
    • 1242319573 scopus 로고    scopus 로고
    • Heme regulates the dynamic exchange of Bach1 and NF-E2-related factors in the Maf transcription factor network
    • Sun,J., Brand,M., Zenke,Y., Tashiro,S., Groudine,M. and Igarashi,K. (2004) Heme regulates the dynamic exchange of Bach1 and NF-E2-related factors in the Maf transcription factor network. Proc. Natl Acad. Sci. USA, 101, 1461-1466.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1461-1466
    • Sun, J.1    Brand, M.2    Zenke, Y.3    Tashiro, S.4    Groudine, M.5    Igarashi, K.6
  • 16
    • 10644259478 scopus 로고    scopus 로고
    • Role of Bach-1 in regulation of heme oxygenase-1 in human liver cells: Insights from studies with small interfering RNAS
    • Shan,Y., Lambrecht,R.W., Ghaziani,T., Donohue,S.E. and Bonkovsky,H.L. (2004) Role of Bach-1 in regulation of heme oxygenase-1 in human liver cells: Insights from studies with small interfering RNAS. J. Biol. Chem., 279, 51769-51774.
    • (2004) J. Biol. Chem , vol.279 , pp. 51769-51774
    • Shan, Y.1    Lambrecht, R.W.2    Ghaziani, T.3    Donohue, S.E.4    Bonkovsky, H.L.5
  • 17
    • 18044386970 scopus 로고    scopus 로고
    • Redox regulation of the transcriptional repressor Bach1
    • Ishikawa,M., Numazawa,S. and Yoshida,T. (2005) Redox regulation of the transcriptional repressor Bach1. Free Radic. Biol. Med., 38, 1344-1352.
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 1344-1352
    • Ishikawa, M.1    Numazawa, S.2    Yoshida, T.3
  • 18
    • 33644662839 scopus 로고    scopus 로고
    • Heme Oxygenase-1 Gene Enhancer Manifests Silencing Activity in a Chromatin Environment Prior to Oxidative Stress
    • Dohi,Y., Alam,J., Yoshizumi,M., Sun,J. and Igarashi,K. (2006) Heme Oxygenase-1 Gene Enhancer Manifests Silencing Activity in a Chromatin Environment Prior to Oxidative Stress. Antioxid. Redox. Signal., 8, 60-67.
    • (2006) Antioxid. Redox. Signal , vol.8 , pp. 60-67
    • Dohi, Y.1    Alam, J.2    Yoshizumi, M.3    Sun, J.4    Igarashi, K.5
  • 19
    • 33644643191 scopus 로고    scopus 로고
    • The heme-Bach1 pathway in the regulation of oxidative stress response and erythroid differentiation
    • Igarashi,K. and Sun,J. (2006) The heme-Bach1 pathway in the regulation of oxidative stress response and erythroid differentiation. Antioxid. Redox. Signal., 8, 107-118.
    • (2006) Antioxid. Redox. Signal , vol.8 , pp. 107-118
    • Igarashi, K.1    Sun, J.2
  • 20
    • 0037015035 scopus 로고    scopus 로고
    • Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
    • Dinkova-Kostova,A.T., Holtzclaw,W.D., Cole,R.N., Itoh,K., Wakabayashi,N., Katoh,Y., Yamamoto,M. and Talalay,P. (2002) Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc. Natl Acad. Sci. USA, 99, 11908-11913.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3    Itoh, K.4    Wakabayashi, N.5    Katoh, Y.6    Yamamoto, M.7    Talalay, P.8
  • 21
    • 0242580049 scopus 로고    scopus 로고
    • Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress
    • Zhang,D.D. and Hannink,M. (2003) Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol. Cell Biol., 23, 8137-8151.
    • (2003) Mol. Cell Biol , vol.23 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 22
    • 29644443964 scopus 로고    scopus 로고
    • Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane
    • Hong,F., Freeman,M.L. and Liebler,D.C. (2005) Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane. Chem. Res. Toxicol., 18, 1917-1926.
    • (2005) Chem. Res. Toxicol , vol.18 , pp. 1917-1926
    • Hong, F.1    Freeman, M.L.2    Liebler, D.C.3
  • 23
    • 33747643517 scopus 로고    scopus 로고
    • Arsenic induces NAD(P)H-quinone oxidoreductase I by disrupting the Nrf2 x Keap1 x Cul3 complex and recruiting Nrf2 x Maf to the antioxidant response element enhancer
    • He,X., Chen,M.G., Lin,G.X. and Ma,Q. (2006) Arsenic induces NAD(P)H-quinone oxidoreductase I by disrupting the Nrf2 x Keap1 x Cul3 complex and recruiting Nrf2 x Maf to the antioxidant response element enhancer. J. Biol. Chem., 281, 23620-23631.
    • (2006) J. Biol. Chem , vol.281 , pp. 23620-23631
    • He, X.1    Chen, M.G.2    Lin, G.X.3    Ma, Q.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,J.D. and Yamamoto,M. (1999) Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev., 13, 76-86.
    • (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
    • 0013282861 scopus 로고    scopus 로고
    • Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26S proteasome
    • Nguyen,T., Sherratt,P.J., Huang,H.C., Yang,C.S. and Pickett,C.B. (2003) Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26S proteasome. J. Biol. Chem., 278 4536-4541.
    • (2003) J. Biol. Chem , vol.278 , pp. 4536-4541
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.C.3    Yang, C.S.4    Pickett, C.B.5
  • 27
    • 17944372665 scopus 로고    scopus 로고
    • Heme mediates derepression of Maf recognition element through direct binding to transcription repressor Bach1
    • Ogawa,K., Sun,J., Taketani,S., Nakajima,O., Nishitani,C., Sassa,S., Hayashi,N., Yamamoto,M., Shibahara,S. et al. (2001) Heme mediates derepression of Maf recognition element through direct binding to transcription repressor Bach1. EMBO J., 20, 2835-2843.
    • (2001) EMBO J , vol.20 , pp. 2835-2843
    • Ogawa, K.1    Sun, J.2    Taketani, S.3    Nakajima, O.4    Nishitani, C.5    Sassa, S.6    Hayashi, N.7    Yamamoto, M.8    Shibahara, S.9
  • 30
    • 18244386712 scopus 로고    scopus 로고
    • Transcriptional regulation of thioredoxin reductase 1 expression by cadmium in vascular endothelial cells: Role of NF-E2-related factor-2
    • Sakurai,A., Nishimoto,M., Himeno,S., Imura,N., Tsujimoto,M., Kunimoto,M. and Hara,S. (2005) Transcriptional regulation of thioredoxin reductase 1 expression by cadmium in vascular endothelial cells: Role of NF-E2-related factor-2. J. Cell Physiol, 203, 529-537.
    • (2005) J. Cell Physiol , vol.203 , pp. 529-537
    • Sakurai, A.1    Nishimoto, M.2    Himeno, S.3    Imura, N.4    Tsujimoto, M.5    Kunimoto, M.6    Hara, S.7
  • 31
    • 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. and Pickett,C.B. (1991) The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J. Biol. Chem., 266, 11632-11639.
    • (1991) J. Biol. Chem , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 32
    • 0037163092 scopus 로고    scopus 로고
    • Identification of a variant antioxidant response element in the promoter of the human glutamate-cysteine ligase modifier subunit gene. Revision of the ARE consensus sequence
    • Erickson,A.M., Nevarea,Z., Gipp,J.J. and Mulcahy,R.T. (2002) Identification of a variant antioxidant response element in the promoter of the human glutamate-cysteine ligase modifier subunit gene. Revision of the ARE consensus sequence. J. Biol. Chem., 277, 30730-30737.
    • (2002) J. Biol. Chem , vol.277 , pp. 30730-30737
    • Erickson, A.M.1    Nevarea, Z.2    Gipp, J.J.3    Mulcahy, R.T.4
  • 33
    • 0042330074 scopus 로고    scopus 로고
    • Identification of a novel Nrf2-regulated antioxidant response element (ARE) in the mouse NAD(PRH:qUinone oxidoreductase 1 gene: Reassessment of the ARE consensus sequence
    • Nioi,P., McMahon,M., Itoh,K., Yamamoto,M. and Hayes,J.D. (2003) Identification of a novel Nrf2-regulated antioxidant response element (ARE) in the mouse NAD(PRH:qUinone oxidoreductase 1 gene: reassessment of the ARE consensus sequence. Biochem. J., 374, 337-348.
    • (2003) Biochem. J , vol.374 , pp. 337-348
    • Nioi, P.1    McMahon, M.2    Itoh, K.3    Yamamoto, M.4    Hayes, J.D.5
  • 34
    • 4744356825 scopus 로고    scopus 로고
    • Heme-dependent up-regulation of the alpha-globin gene expression by transcriptional repressor Bach1 in erythroid cells
    • Tahara,T., Sun,J., Igarashi,K. and Taketani,S. (2004) Heme-dependent up-regulation of the alpha-globin gene expression by transcriptional repressor Bach1 in erythroid cells. Biochem. Biophys. Res. Commun. 324, 77-85.
    • (2004) Biochem. Biophys. Res. Commun , vol.324 , pp. 77-85
    • Tahara, T.1    Sun, J.2    Igarashi, K.3    Taketani, S.4
  • 35
    • 0037821802 scopus 로고    scopus 로고
    • Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression
    • McMahon,M., Itoh,K., Yamamoto,M. and Hayes,J.D. (2003) Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression. J. Biol. Chem., 278, 21592-21600.
    • (2003) J. Biol. Chem , vol.278 , pp. 21592-21600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4
  • 36
    • 11144264663 scopus 로고    scopus 로고
    • BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase
    • Furukawa,M. and Xiong,Y. (2005) BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. Mol. Cell Biol., 25, 162-171.
    • (2005) Mol. Cell Biol , vol.25 , pp. 162-171
    • Furukawa, M.1    Xiong, Y.2
  • 37
    • 0037183998 scopus 로고    scopus 로고
    • The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
    • Zipper,L.M. and Mulcahy,R.T. (2002) The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm. J. Biol. Chem. 277, 36544-36552.
    • (2002) J. Biol. Chem , vol.277 , pp. 36544-36552
    • Zipper, L.M.1    Mulcahy, R.T.2
  • 38
    • 24044466764 scopus 로고    scopus 로고
    • Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway
    • Zhang,D.D., Lo,S.C., Sun,Z., Habib,G.M., Lieberman,M.W. and Hannink,M. (2005) Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway. J. Biol. Chem., 280, 30091-30099.
    • (2005) J. Biol. Chem , vol.280 , pp. 30091-30099
    • Zhang, D.D.1    Lo, S.C.2    Sun, Z.3    Habib, G.M.4    Lieberman, M.W.5    Hannink, M.6
  • 39
    • 1642494891 scopus 로고    scopus 로고
    • Monomeric and dimeric bZIP transcription factor GCN4 bind at the same rate to their target DNA site
    • Cranz,S., Berger,C., Baici,A., Jelesarov,I. and Bosshard,H.R. (2004) Monomeric and dimeric bZIP transcription factor GCN4 bind at the same rate to their target DNA site. Biochemistry, 43, 718-727.
    • (2004) Biochemistry , vol.43 , pp. 718-727
    • Cranz, S.1    Berger, C.2    Baici, A.3    Jelesarov, I.4    Bosshard, H.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.