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Volumn 70, Issue 4, 2010, Pages 353-361

Overexpression of hepatocyte nuclear factor-3α induces apoptosis through the upregulation and accumulation of cytoplasmic p53 in prostate cancer cells

Author keywords

Apoptosis; HNF 3 ; p53; Prostate cancer

Indexed keywords

ADENOVIRUS VECTOR; CASPASE; CASPASE 8; CYTOCHROME C; DEATH RECEPTOR; HEPATOCYTE NUCLEAR FACTOR 3ALPHA; PROTEIN BAX; PROTEIN P53;

EID: 76149127352     PISSN: 02704137     EISSN: 10970045     Source Type: Journal    
DOI: 10.1002/pros.21069     Document Type: Article
Times cited : (4)

References (45)
  • 1
    • 0028696273 scopus 로고
    • Role of androgens in prostatic cancer
    • Isaacs JT. Role of androgens in prostatic cancer. Vitam Horm 1994;49:433-502.
    • (1994) Vitam Horm , vol.49 , pp. 433-502
    • Isaacs, J.T.1
  • 2
    • 0031914023 scopus 로고    scopus 로고
    • Expression of hepatocyte nuclear factor-3alpha in rat prostate, seminal vesicle, and bladder
    • Kopachik W, Hayward SW, Cunha GR. Expression of hepatocyte nuclear factor-3alpha in rat prostate, seminal vesicle, and bladder. Dev Dynam 1998;211:131-140.
    • (1998) Dev Dynam , vol.211 , pp. 131-140
    • Kopachik, W.1    Hayward, S.W.2    Cunha, G.R.3
  • 3
    • 0031017018 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor-3 alpha promoter regulation involves recognition by cell-specific factors, thyroid transcription factor-1, and autoactivation
    • Peterson RS, Clevidence DE, Ye H, Costa RH. Hepatocyte nuclear factor-3 alpha promoter regulation involves recognition by cell-specific factors, thyroid transcription factor-1, and autoactivation. Cell Growth Differ 1997;8:69-82.
    • (1997) Cell Growth Differ , vol.8 , pp. 69-82
    • Peterson, R.S.1    Clevidence, D.E.2    Ye, H.3    Costa, R.H.4
  • 5
    • 33947274103 scopus 로고    scopus 로고
    • Hedgehog pathway activity in the LADY prostate tumor model
    • Gipp J, Gu G, Crylen C, Susan K, Bushman W. Hedgehog pathway activity in the LADY prostate tumor model. Mol Cancer 2007;7:1-8.
    • (2007) Mol Cancer , vol.7 , pp. 1-8
    • Gipp, J.1    Gu, G.2    Crylen, C.3    Susan, K.4    Bushman, W.5
  • 7
    • 32244431931 scopus 로고    scopus 로고
    • Foxa1 and Foxa2 interact with the androgen receptor to regulate prostate and epididymal genes differentially
    • Yu X, Gupta A, Wang Y, Suzuki K, Mirosevich J, Orgebin-Crist M, Matusik R. Foxa1 and Foxa2 interact with the androgen receptor to regulate prostate and epididymal genes differentially. Ann NY Acad Sci 2005;161:77-93.
    • (2005) Ann NY Acad Sci , vol.161 , pp. 77-93
    • Yu, X.1    Gupta, A.2    Wang, Y.3    Suzuki, K.4    Mirosevich, J.5    Orgebin-Crist, M.6    Matusik, R.7
  • 9
    • 0042266417 scopus 로고    scopus 로고
    • The role of hepatocyte nuclear factor-3 alpha (Forkhead Box A1) and androgen receptor in transcriptional regulation of prostatic genes
    • Gao N, Zhang J, Rao MA, Case TC, Mirosevich J, Wang Y, Jin R, Gupta A, Rennie PS, Matusik RJ. The role of hepatocyte nuclear factor-3 alpha (Forkhead Box A1) and androgen receptor in transcriptional regulation of prostatic genes. Mol Endocrinol 2003;17:1484-1507.
    • (2003) Mol Endocrinol , vol.17 , pp. 1484-1507
    • Gao, N.1    Zhang, J.2    Rao, M.A.3    Case, T.C.4    Mirosevich, J.5    Wang, Y.6    Jin, R.7    Gupta, A.8    Rennie, P.S.9    Matusik, R.J.10
  • 10
    • 38349062191 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor-3 alpha (HNF-3a) negatively regulates androgen receptor transactivation in prostate cancer cells
    • Lee HJ, Hwang MO, Chattopadhyay S, Choi H, Lee K. Hepatocyte nuclear factor-3 alpha (HNF-3a) negatively regulates androgen receptor transactivation in prostate cancer cells. Biochem Biophys Res Commun 2008;367:481-486.
    • (2008) Biochem Biophys Res Commun , vol.367 , pp. 481-486
    • Lee, H.J.1    Hwang, M.O.2    Chattopadhyay, S.3    Choi, H.4    Lee, K.5
  • 12
    • 0024973841 scopus 로고
    • The homeotic gene fork head encodes a nuclear protein and is expressed in the terminal regions of the Drosophila embryo
    • Weigel D, Jurgens G, Kuttner F, Seifert E, Jackle H. The homeotic gene fork head encodes a nuclear protein and is expressed in the terminal regions of the Drosophila embryo. Cell 1989;57:645-658.
    • (1989) Cell , vol.57 , pp. 645-658
    • Weigel, D.1    Jurgens, G.2    Kuttner, F.3    Seifert, E.4    Jackle, H.5
  • 13
    • 0035300430 scopus 로고    scopus 로고
    • Expression profiling suggested a regulatory role of liver-enriched transcription factors in human hepatocellular carcinoma
    • Xu L, Hui L, Wang S, Gong J, Jin Y, Wang Y, Ji Y, Wu X, Han Z, Hu G. Expression profiling suggested a regulatory role of liver-enriched transcription factors in human hepatocellular carcinoma. Cancer Res 2001;61:3176-3181.
    • (2001) Cancer Res , vol.61 , pp. 3176-3181
    • Xu, L.1    Hui, L.2    Wang, S.3    Gong, J.4    Jin, Y.5    Wang, Y.6    Ji, Y.7    Wu, X.8    Han, Z.9    Hu, G.10
  • 14
    • 3042662966 scopus 로고    scopus 로고
    • A transcriptional profiling study of CCAAT/enhancer binding protein targets identifies hepatocyte nuclear factor 3 beta as a novel tumor suppressor in lung cancer
    • Halmos B, Basseres DS, Monti S, D'Alo F, Dayaram T, Ferenczi K, Wouters BJ, Huettner CS, Golub TR, Tenen DG. A transcriptional profiling study of CCAAT/enhancer binding protein targets identifies hepatocyte nuclear factor 3 beta as a novel tumor suppressor in lung cancer. Cancer Res 2004;64:4137-4147.
    • (2004) Cancer Res , vol.64 , pp. 4137-4147
    • Halmos, B.1    Basseres, D.S.2    Monti, S.3    D'Alo, F.4    Dayaram, T.5    Ferenczi, K.6    Wouters, B.J.7    Huettner, C.S.8    Golub, T.R.9    Tenen, D.G.10
  • 19
    • 4344601432 scopus 로고    scopus 로고
    • MED16 and MED23 of mediator are coactivators of lipopolysaccharide-and heat-shock-induced transcriptional activators
    • Kim TW, Kwon YJ, Kim JM, Song YH, Kim SN, Kim YJ. MED16 and MED23 of mediator are coactivators of lipopolysaccharide-and heat-shock-induced transcriptional activators. Proc Natl Acad Sci USA 2004;101:12153-12158.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12153-12158
    • Kim, T.W.1    Kwon, Y.J.2    Kim, J.M.3    Song, Y.H.4    Kim, S.N.5    Kim, Y.J.6
  • 20
    • 0034616945 scopus 로고    scopus 로고
    • Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000;102:33-42.
    • Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000;102:33-42.
  • 21
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997;91:479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 22
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c. Cell 1996;86:147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 24
    • 0029972806 scopus 로고    scopus 로고
    • Ko LJ, Prives C. p53: Puzzle and paradigm. Genes Dev 1996; 10:1054-1072.
    • Ko LJ, Prives C. p53: Puzzle and paradigm. Genes Dev 1996; 10:1054-1072.
  • 25
    • 0038418297 scopus 로고    scopus 로고
    • p53 physically interacts with mitochondrial transcription factor A and differentially regulates binding to damaged DNA
    • Yoshida Y, Izumi H, Torigoe T, Ishiguchi H, Itoh H, Kang D, Kohno K. p53 physically interacts with mitochondrial transcription factor A and differentially regulates binding to damaged DNA. Cancer Res 2003;63:3729-3734.
    • (2003) Cancer Res , vol.63 , pp. 3729-3734
    • Yoshida, Y.1    Izumi, H.2    Torigoe, T.3    Ishiguchi, H.4    Itoh, H.5    Kang, D.6    Kohno, K.7
  • 26
    • 0038409927 scopus 로고    scopus 로고
    • p53 represses cyclin D1 transcription through down regulation of Bcl-3 and inducing increased association the p52NF-κB subunit with histone deacetylase 1
    • Rocha S, Martin AM, Meek DW, Perkins ND. p53 represses cyclin D1 transcription through down regulation of Bcl-3 and inducing increased association the p52NF-κB subunit with histone deacetylase 1. Mol Cell Biol 2003;23:4713-4727.
    • (2003) Mol Cell Biol , vol.23 , pp. 4713-4727
    • Rocha, S.1    Martin, A.M.2    Meek, D.W.3    Perkins, N.D.4
  • 27
    • 0242522206 scopus 로고    scopus 로고
    • Regulation of apoptosis by Bcl-2 family proteins
    • Burlacu A. Regulation of apoptosis by Bcl-2 family proteins. J Cell Mol Med 2003;7:249-257.
    • (2003) J Cell Mol Med , vol.7 , pp. 249-257
    • Burlacu, A.1
  • 31
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 1998; 281:1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 32
    • 0036307307 scopus 로고    scopus 로고
    • p53 Stability and activity is regulated by Mdm2-mediated induction of alternative p53 translation products
    • Yin Y, Stephen CW, Luciani MG, Fahraeus R. p53 Stability and activity is regulated by Mdm2-mediated induction of alternative p53 translation products. Nat Cell Biol 2002;4:462-467.
    • (2002) Nat Cell Biol , vol.4 , pp. 462-467
    • Yin, Y.1    Stephen, C.W.2    Luciani, M.G.3    Fahraeus, R.4
  • 34
    • 0033552613 scopus 로고    scopus 로고
    • Regulation of p53 stability
    • Ashcroft M, Vousden KH. Regulation of p53 stability. Oncogene 1999;18:7637-7643.
    • (1999) Oncogene , vol.18 , pp. 7637-7643
    • Ashcroft, M.1    Vousden, K.H.2
  • 35
    • 0037075898 scopus 로고    scopus 로고
    • Activation of the p53 tumor suppressor protein
    • Vousden KH. Activation of the p53 tumor suppressor protein. Biochem Biophys Acta 2002;1606:47-59.
    • (2002) Biochem Biophys Acta , vol.1606 , pp. 47-59
    • Vousden, K.H.1
  • 37
    • 0037378516 scopus 로고    scopus 로고
    • Coactivator- dependent acetylation stabilizes members of the SREBP family of transcription factors
    • Giandomenico V, Simonsson M, Gronroos E, Ericsson J. Coactivator- dependent acetylation stabilizes members of the SREBP family of transcription factors. Mol Cell Biol 2003;23: 2587-2599.
    • (2003) Mol Cell Biol , vol.23 , pp. 2587-2599
    • Giandomenico, V.1    Simonsson, M.2    Gronroos, E.3    Ericsson, J.4
  • 38
    • 0142182771 scopus 로고    scopus 로고
    • Hepatitis B virus X protein regulates transactivation activity and protein stability of the cancer-amplified transcription coactivator ASC-2
    • Kong HJ, Park MJ, Hong S, Yu HJ, Lee YC, Choi YH, Cheong J. Hepatitis B virus X protein regulates transactivation activity and protein stability of the cancer-amplified transcription coactivator ASC-2. Hepatology 2003;38:1258-1266.
    • (2003) Hepatology , vol.38 , pp. 1258-1266
    • Kong, H.J.1    Park, M.J.2    Hong, S.3    Yu, H.J.4    Lee, Y.C.5    Choi, Y.H.6    Cheong, J.7
  • 39
    • 0030905284 scopus 로고    scopus 로고
    • MDM2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M. MDM2 promotes the rapid degradation of p53. Nature 1997;387:296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 40
    • 0036517104 scopus 로고    scopus 로고
    • Nuclear degradation of p53 occurs during down-regulation of the p53 response after DNA damage
    • Shirangi TR, Zaika A, Moll UM. Nuclear degradation of p53 occurs during down-regulation of the p53 response after DNA damage. FASEB J 2002;16:420-422.
    • (2002) FASEB J , vol.16 , pp. 420-422
    • Shirangi, T.R.1    Zaika, A.2    Moll, U.M.3
  • 42
    • 1342306819 scopus 로고    scopus 로고
    • Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3
    • Lin B, Kolluri SK, Lin F, Liu W, Han YH, Cao X, Dawson MI, Reed JC, Zhang XK. Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3. Cell 2004; 116:527-540.
    • (2004) Cell , vol.116 , pp. 527-540
    • Lin, B.1    Kolluri, S.K.2    Lin, F.3    Liu, W.4    Han, Y.H.5    Cao, X.6    Dawson, M.I.7    Reed, J.C.8    Zhang, X.K.9
  • 44
    • 0034717014 scopus 로고    scopus 로고
    • Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling
    • Marchenko ND, Zaika A, Moll UM. Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling. J Biol Chem 2000;275:16202-16212.
    • (2000) J Biol Chem , vol.275 , pp. 16202-16212
    • Marchenko, N.D.1    Zaika, A.2    Moll, U.M.3
  • 45
    • 24644457314 scopus 로고    scopus 로고
    • Complicating the complexity of p53
    • Yee KS, Vousden KH. Complicating the complexity of p53. Carcinogenesis 2005;26:1317-1322.
    • (2005) Carcinogenesis , vol.26 , pp. 1317-1322
    • Yee, K.S.1    Vousden, K.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.