메뉴 건너뛰기




Volumn 361, Issue 1, 2007, Pages 243-248

1,2-Naphthoquinone disrupts the function of cAMP response element-binding protein through covalent modification

Author keywords

Bcl 2; CREB; Electrophile; Quinone

Indexed keywords

1,2 NAPHTHOQUINONE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; DITHIOTHREITOL; HYDROCARBON; LUCIFERASE; NAPHTHALENE; PROTEIN BCL 2;

EID: 34547133038     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.07.024     Document Type: Article
Times cited : (29)

References (30)
  • 3
    • 33750530167 scopus 로고    scopus 로고
    • 15-deoxy-Delta12,14-prostaglandin J2 as a potential endogenous regulator of redox-sensitive transcription factors
    • Kim E.H., and Surh Y.J. 15-deoxy-Delta12,14-prostaglandin J2 as a potential endogenous regulator of redox-sensitive transcription factors. Biochem. Pharmacol. 72 (2006) 1516-1528
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 1516-1528
    • Kim, E.H.1    Surh, Y.J.2
  • 4
    • 34047274821 scopus 로고    scopus 로고
    • 15-deoxy-Delta12,14-prostaglandin J2 inhibits transcriptional activity of estrogen receptor-alpha via covalent modification of DNA-binding domain
    • Kim H.J., Kim J.Y., Meng Z., Wang L.H., Liu F., Conrads T.P., Burke T.R., Veenstra T.D., and Farrar W.L. 15-deoxy-Delta12,14-prostaglandin J2 inhibits transcriptional activity of estrogen receptor-alpha via covalent modification of DNA-binding domain. Cancer Res. 67 (2007) 2595-2602
    • (2007) Cancer Res. , vol.67 , pp. 2595-2602
    • Kim, H.J.1    Kim, J.Y.2    Meng, Z.3    Wang, L.H.4    Liu, F.5    Conrads, T.P.6    Burke, T.R.7    Veenstra, T.D.8    Farrar, W.L.9
  • 5
    • 0035430282 scopus 로고    scopus 로고
    • Transcriptional regulation by the phosphorylation-dependent factor CREB
    • Mayr B., and Montminy M. Transcriptional regulation by the phosphorylation-dependent factor CREB. Nat. Rev. Mol. Cell Biol. 2 (2001) 599-609
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 599-609
    • Mayr, B.1    Montminy, M.2
  • 6
    • 0033516488 scopus 로고    scopus 로고
    • Critical role of cAMP response element binding protein expression in hypoxia-elicited induction of epithelial tumor necrosis factor-alpha
    • Taylor C.T., Fueki N., Agah A., Hershberg R.M., and Colgan S.P. Critical role of cAMP response element binding protein expression in hypoxia-elicited induction of epithelial tumor necrosis factor-alpha. J. Biol. Chem. 274 (1999) 19447-19454
    • (1999) J. Biol. Chem. , vol.274 , pp. 19447-19454
    • Taylor, C.T.1    Fueki, N.2    Agah, A.3    Hershberg, R.M.4    Colgan, S.P.5
  • 7
    • 0033769153 scopus 로고    scopus 로고
    • Transcriptional regulation by cAMP in the heart
    • Muller F.U., Neumann J., and Schmitz W. Transcriptional regulation by cAMP in the heart. Mol. Cell Biochem. 212 (2000) 11-17
    • (2000) Mol. Cell Biochem. , vol.212 , pp. 11-17
    • Muller, F.U.1    Neumann, J.2    Schmitz, W.3
  • 8
    • 0030726539 scopus 로고    scopus 로고
    • Dominant-negative CREB inhibits tumor growth and metastasis of human melanoma cells
    • Xie S., Price J.E., Luca M., Jean D., Ronai Z., and Bar-Eli M. Dominant-negative CREB inhibits tumor growth and metastasis of human melanoma cells. Oncogene 15 (1997) 2069-2075
    • (1997) Oncogene , vol.15 , pp. 2069-2075
    • Xie, S.1    Price, J.E.2    Luca, M.3    Jean, D.4    Ronai, Z.5    Bar-Eli, M.6
  • 12
    • 0037500306 scopus 로고    scopus 로고
    • Persistent ERK phosphorylation negatively regulates cAMP response element-binding protein (CREB) activity via recruitment of CREB-binding protein to pp90RSK
    • Wang Z., Zhang B., Wang M., and Carr B.I. Persistent ERK phosphorylation negatively regulates cAMP response element-binding protein (CREB) activity via recruitment of CREB-binding protein to pp90RSK. J. Biol. Chem. 278 (2003) 11138-11144
    • (2003) J. Biol. Chem. , vol.278 , pp. 11138-11144
    • Wang, Z.1    Zhang, B.2    Wang, M.3    Carr, B.I.4
  • 14
    • 0025077481 scopus 로고
    • Redox regulation of fos and jun DNA-binding activity in vitro
    • Abate C., Patel L., Rauscher III F.J., and Curran T. Redox regulation of fos and jun DNA-binding activity in vitro. Science 249 (1990) 1157-1161
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher III, F.J.3    Curran, T.4
  • 15
    • 33646157076 scopus 로고    scopus 로고
    • Deciphering B-ZIP transcription factor interactions in vitro and in vivo
    • Vinson C., Acharya A., and Taparowsky E.J. Deciphering B-ZIP transcription factor interactions in vitro and in vivo. Biochim. Biophys. Acta 1759 (2006) 4-12
    • (2006) Biochim. Biophys. Acta , vol.1759 , pp. 4-12
    • Vinson, C.1    Acharya, A.2    Taparowsky, E.J.3
  • 16
    • 0346435097 scopus 로고    scopus 로고
    • Molecular basis for the direct inhibition of AP-1 DNA binding by 15-deoxy-Delta 12,14-prostaglandin J2
    • Perez-Sala D., Cernuda-Morollon E., and Canada F.J. Molecular basis for the direct inhibition of AP-1 DNA binding by 15-deoxy-Delta 12,14-prostaglandin J2. J. Biol. Chem. 278 (2003) 51251-51260
    • (2003) J. Biol. Chem. , vol.278 , pp. 51251-51260
    • Perez-Sala, D.1    Cernuda-Morollon, E.2    Canada, F.J.3
  • 17
    • 0037192626 scopus 로고    scopus 로고
    • Site-directed mutagenesis of cysteine to serine in the DNA binding region of Nrf2 decreases its capacity to upregulate antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductase1 gene
    • Bloom D., Dhakshinamoorthy S., and Jaiswal A.K. Site-directed mutagenesis of cysteine to serine in the DNA binding region of Nrf2 decreases its capacity to upregulate antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductase1 gene. Oncogene 21 (2002) 2191-2200
    • (2002) Oncogene , vol.21 , pp. 2191-2200
    • Bloom, D.1    Dhakshinamoorthy, S.2    Jaiswal, A.K.3
  • 18
    • 0029683998 scopus 로고    scopus 로고
    • Development of polyclonal antibodies for detection of protein modification by 1,2-naphthoquinone
    • Zheng J., and Hammock B.D. Development of polyclonal antibodies for detection of protein modification by 1,2-naphthoquinone. Chem. Res. Toxicol. 9 (1996) 904-909
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 904-909
    • Zheng, J.1    Hammock, B.D.2
  • 19
    • 0035798407 scopus 로고    scopus 로고
    • Two cysteine residues in the DNA-binding domain of CREB control binding to CRE and CREB-mediated gene expression
    • Goren I., Tavor E., Goldblum A., and Honigman A. Two cysteine residues in the DNA-binding domain of CREB control binding to CRE and CREB-mediated gene expression. J. Mol. Biol. 313 (2001) 695-709
    • (2001) J. Mol. Biol. , vol.313 , pp. 695-709
    • Goren, I.1    Tavor, E.2    Goldblum, A.3    Honigman, A.4
  • 20
    • 0036667355 scopus 로고    scopus 로고
    • Stability of hemoglobin and albumin adducts of naphthalene oxide, 1,2-naphthoquinone, and 1,4-naphthoquinone
    • Troester M.A., Lindstrom A.B., Waidyanatha S., Kupper L.L., and Rappaport S.M. Stability of hemoglobin and albumin adducts of naphthalene oxide, 1,2-naphthoquinone, and 1,4-naphthoquinone. Toxicol. Sci. 68 (2002) 314-321
    • (2002) Toxicol. Sci. , vol.68 , pp. 314-321
    • Troester, M.A.1    Lindstrom, A.B.2    Waidyanatha, S.3    Kupper, L.L.4    Rappaport, S.M.5
  • 21
    • 0037145418 scopus 로고    scopus 로고
    • Measurement of hemoglobin and albumin adducts of naphthalene-1,2-oxide, 1,2-naphthoquinone and 1,4-naphthoquinone after administration of naphthalene to F344 rats
    • Waidyanatha S., Troester M.A., Lindstrom A.B., and Rappaport S.M. Measurement of hemoglobin and albumin adducts of naphthalene-1,2-oxide, 1,2-naphthoquinone and 1,4-naphthoquinone after administration of naphthalene to F344 rats. Chem. Biol. Interact. 141 (2002) 189-210
    • (2002) Chem. Biol. Interact. , vol.141 , pp. 189-210
    • Waidyanatha, S.1    Troester, M.A.2    Lindstrom, A.B.3    Rappaport, S.M.4
  • 22
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB
    • Deak M., Clifton A.D., Lucocq L.M., and Alessi D.R. Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. Embo. J. 17 (1998) 4426-4441
    • (1998) Embo. J. , vol.17 , pp. 4426-4441
    • Deak, M.1    Clifton, A.D.2    Lucocq, L.M.3    Alessi, D.R.4
  • 23
    • 0032484019 scopus 로고    scopus 로고
    • CREB is a regulatory target for the protein kinase Akt/PKB
    • Du K., and Montminy M. CREB is a regulatory target for the protein kinase Akt/PKB. J. Biol. Chem. 273 (1998) 32377-32379
    • (1998) J. Biol. Chem. , vol.273 , pp. 32377-32379
    • Du, K.1    Montminy, M.2
  • 24
    • 0027981633 scopus 로고
    • Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression
    • Matthews R.P., Guthrie C.R., Wailes L.M., Zhao X., Means A.R., and McKnight G.S. Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression. Mol. Cell Biol. 14 (1994) 6107-6116
    • (1994) Mol. Cell Biol. , vol.14 , pp. 6107-6116
    • Matthews, R.P.1    Guthrie, C.R.2    Wailes, L.M.3    Zhao, X.4    Means, A.R.5    McKnight, G.S.6
  • 25
    • 0027943988 scopus 로고
    • Differential activation of CREB by Ca2+/calmodulin-dependent protein kinases type II and type IV involves phosphorylation of a site that negatively regulates activity
    • Sun P., Enslen H., Myung P.S., and Maurer R.A. Differential activation of CREB by Ca2+/calmodulin-dependent protein kinases type II and type IV involves phosphorylation of a site that negatively regulates activity. Genes Dev. 8 (1994) 2527-2539
    • (1994) Genes Dev. , vol.8 , pp. 2527-2539
    • Sun, P.1    Enslen, H.2    Myung, P.S.3    Maurer, R.A.4
  • 26
    • 0029790656 scopus 로고    scopus 로고
    • FGF and stress regulate CREB and ATF-1 via a pathway involving p38 MAP kinase and MAPKAP kinase-2
    • Tan Y., Rouse J., Zhang A., Cariati S., Cohen P., and Comb M.J. FGF and stress regulate CREB and ATF-1 via a pathway involving p38 MAP kinase and MAPKAP kinase-2. Embo. J. 15 (1996) 4629-4642
    • (1996) Embo. J. , vol.15 , pp. 4629-4642
    • Tan, Y.1    Rouse, J.2    Zhang, A.3    Cariati, S.4    Cohen, P.5    Comb, M.J.6
  • 27
    • 0029789643 scopus 로고    scopus 로고
    • Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase
    • Xing J., Ginty D.D., and Greenberg M.E. Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. Science 273 (1996) 959-963
    • (1996) Science , vol.273 , pp. 959-963
    • Xing, J.1    Ginty, D.D.2    Greenberg, M.E.3
  • 28
    • 0023712739 scopus 로고
    • Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB
    • Yamamoto K.K., Gonzalez G.A., Biggs III W.H., and Montminy M.R. Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB. Nature 334 (1988) 494-498
    • (1988) Nature , vol.334 , pp. 494-498
    • Yamamoto, K.K.1    Gonzalez, G.A.2    Biggs III, W.H.3    Montminy, M.R.4
  • 29
    • 0034059440 scopus 로고    scopus 로고
    • Bcl-2 inhibits Bax translocation from cytosol to mitochondria during drug-induced apoptosis of human tumor cells
    • Murphy K.M., Ranganathan V., Farnsworth M.L., Kavallaris M., and Lock R.B. Bcl-2 inhibits Bax translocation from cytosol to mitochondria during drug-induced apoptosis of human tumor cells. Cell Death Differ. 7 (2000) 102-111
    • (2000) Cell Death Differ. , vol.7 , pp. 102-111
    • Murphy, K.M.1    Ranganathan, V.2    Farnsworth, M.L.3    Kavallaris, M.4    Lock, R.B.5
  • 30
    • 33745153095 scopus 로고    scopus 로고
    • Cilostazol protects against brain white matter damage and cognitive impairment in a rat model of chronic cerebral hypoperfusion
    • Watanabe T., Zhang N., Liu M., Tanaka R., Mizuno Y., and Urabe T. Cilostazol protects against brain white matter damage and cognitive impairment in a rat model of chronic cerebral hypoperfusion. Stroke 37 (2006) 1539-1545
    • (2006) Stroke , vol.37 , pp. 1539-1545
    • Watanabe, T.1    Zhang, N.2    Liu, M.3    Tanaka, R.4    Mizuno, Y.5    Urabe, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.