메뉴 건너뛰기




Volumn 8, Issue , 2015, Pages 1979-1988

The histone demethylase PHF8 promotes prostate cancer cell growth by activating the oncomir miR-125b

Author keywords

Apoptosis; MiR 125b; PHF8; Prostate cancer

Indexed keywords

HISTONE DEMETHYLASE; MICRORNA 125B; PLANT HOMEODOMAIN FINGER PROTEIN 8; UNCLASSIFIED DRUG;

EID: 84939812426     PISSN: 11786930     EISSN: 11786930     Source Type: Journal    
DOI: 10.2147/OTT.S85443     Document Type: Article
Times cited : (25)

References (30)
  • 2
    • 0037454778 scopus 로고    scopus 로고
    • Current status of the molecular genetics of human prostatic adenocarcinomas
    • Karan D, Lin MF, Johansson SL, Batra SK. Current status of the molecular genetics of human prostatic adenocarcinomas. Int J Cancer. 2003;103: 285-293.
    • (2003) Int J Cancer , vol.103 , pp. 285-293
    • Karan, D.1    Lin, M.F.2    Johansson, S.L.3    Batra, S.K.4
  • 3
    • 0034307013 scopus 로고    scopus 로고
    • Molecular genetics of prostate cancer
    • Abate-Shen C, Shen MM. Molecular genetics of prostate cancer. Genes Dev. 2000;14:2410-2434.
    • (2000) Genesdev , vol.14 , pp. 2410-2434
    • Abate-Shen, C.1    Shen, M.M.2
  • 4
    • 77954957901 scopus 로고    scopus 로고
    • Histone H4K20/H3K9 demethylasePHF8 regulates zebrafish brain and craniofacial development
    • Qi HH, Sarkissian M, Hu GQ, et al. Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development. Nature. 2010; 466:503-507
    • (2010) Nature , vol.466 , pp. 503-507
    • Qi, H.H.1    Sarkissian, M.2    Hu, G.Q.3
  • 5
    • 77954954200 scopus 로고    scopus 로고
    • PHF8 mediates histone H4 lysine20 demethylation events involved in cell cycle progression
    • Liu W, Tanasa B, Tyurina OV, et al. PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression. Nature. 2010;466:508-512.
    • (2010) Nature , vol.466 , pp. 508-512
    • Liu, W.1    Tanasa, B.2    Tyurina, O.V.3
  • 6
    • 77950521594 scopus 로고    scopus 로고
    • PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation
    • Feng W, Yonezawa M, Ye J, Jenuwein T, Grummt I. PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation. Nat Struct Mol Biol. 2010;17:445-450.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 445-450
    • Feng, W.1    Yonezawa, M.2    Ye, J.3    Jenuwein, T.4    Grummt, I.5
  • 7
    • 33847383585 scopus 로고    scopus 로고
    • Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein
    • Lee MG, Norman J, Shilatifard A, Shiekhattar R. Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein. Cell. 2007;128:877-887.
    • (2007) Cell , vol.128 , pp. 877-887
    • Lee, M.G.1    Norman, J.2    Shilatifard, A.3    Shiekhattar, R.4
  • 8
    • 43249116995 scopus 로고    scopus 로고
    • Coordinated regulation of transcriptional repression by the RBP2 H3K4 demethylase and polycomb-repressive complex 2
    • Pasini D, Hansen KH, Christensen J, Agger K, Cloos PA, Helin K. Coordinated regulation of transcriptional repression by the RBP2 H3K4 demethylase and polycomb-repressive complex 2. Genes Dev. 2008;22: 1345-1355.
    • (2008) Genes Dev , vol.22 , pp. 1345-1355
    • Pasini, D.1    Hansen, K.H.2    Christensen, J.3    Agger, K.4    Cloos, P.A.5    Helin, K.6
  • 9
    • 77955710635 scopus 로고    scopus 로고
    • PHF8 is a histone H3K9me2 demethylaseregulating rRNA synthesis
    • Zhu Z, Wang Y, Li X, et al. PHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis. Cell Res. 2010;20:794-801.
    • (2010) Cell Res , vol.20 , pp. 794-801
    • Zhu, Z.1    Wang, Y.2    Li, X.3
  • 10
    • 26944461197 scopus 로고    scopus 로고
    • Mutations in PHF8 are associated with X linked mental retardation and cleft lip/cleft palate
    • Laumonnier F, Holbert S, Ronce N, et al. Mutations in PHF8 are associated with X linked mental retardation and cleft lip/cleft palate. J Med Genet. 2005;42:780-786.
    • (2005) J Med Genet , vol.42 , pp. 780-786
    • Laumonnier, F.1    Holbert, S.2    Ronce, N.3
  • 11
    • 84900548218 scopus 로고    scopus 로고
    • Circulating microRNAs areassociated with docetaxel chemotherapy outcome in castration-resistantprostate cancer
    • Lin HM, Castillo L, Mahon KL, et al. Circulating microRNAs are associated with docetaxel chemotherapy outcome in castration-resistant prostate cancer. Br J Cancer. 2014;110:2462-2471.
    • (2014) Br J Cancer , vol.110 , pp. 2462-2471
    • Lin, H.M.1    Castillo, L.2    Mahon, K.L.3
  • 12
    • 84865322800 scopus 로고    scopus 로고
    • Detecting microRNAs of high influence on protein functional interaction networks: A prostate cancer case study
    • Alshalalfa M, Bader GD, Goldenberg A, Morris Q, Alhajj R. Detecting microRNAs of high influence on protein functional interaction networks: a prostate cancer case study. BMC Syst Biol. 2012;6:112.
    • (2012) BMC Syst Biol , vol.6
    • Alshalalfa, M.1    Bader, G.D.2    Goldenberg, A.3    Morris, Q.4    Alhajj, R.5
  • 13
    • 84896394889 scopus 로고    scopus 로고
    • Regulation of several androgen-induced genes through the repression of the miR-99a/let-7c/miR-125b-2 miRNA cluster in prostate cancer cells
    • Sun D, Layer R, Mueller AC, et al. Regulation of several androgen-induced genes through the repression of the miR-99a/let-7c/miR-125b-2 miRNA cluster in prostate cancer cells. Oncogene. 2014;33: 1448-1457.
    • (2014) Oncogene , vol.33 , pp. 1448-1457
    • Sun, D.1    Layer, R.2    Mueller, A.C.3
  • 14
    • 84872905140 scopus 로고    scopus 로고
    • Expression differences of circulating microRNAs in metastatic castration resistant prostate cancer and low-risk, localized prostate cancer
    • Nguyen HC, Xie W, Yang M, et al. Expression differences of circulating microRNAs in metastatic castration resistant prostate cancer and low-risk, localized prostate cancer. Prostate. 2013;73:346-354.
    • (2013) Prostate , vol.73 , pp. 346-354
    • Nguyen, H.C.1    Xie, W.2    Yang, M.3
  • 15
    • 84855189041 scopus 로고    scopus 로고
    • A miR-125b binding site polymorphism in bone morphogenetic protein membrane receptor type IB gene and prostate cancer risk in China
    • Feng N, Xu B, Tao J, et al. A miR-125b binding site polymorphism in bone morphogenetic protein membrane receptor type IB gene and prostate cancer risk in China. Mol Biol Rep. 2012;39:369-373.
    • (2012) Mol Biol Rep , vol.39 , pp. 369-373
    • Feng, N.1    Xu, B.2    Tao, J.3
  • 16
    • 84876046735 scopus 로고    scopus 로고
    • Oncomir miR-125b suppresses p14(ARF) to modulate p53-dependent and p53independent apoptosis in prostate cancer
    • Amir S, Ma AH, Shi XB, Xue L, Kung HJ, Devere White RW. Oncomir miR-125b suppresses p14(ARF) to modulate p53-dependent and p53independent apoptosis in prostate cancer. PLoS One. 2013;8:e61064.
    • (2013) Plos One , vol.8
    • Amir, S.1    Ma, A.H.2    Shi, X.B.3    Xue, L.4    Kung, H.J.5    Devere White, R.W.6
  • 17
    • 84877258964 scopus 로고    scopus 로고
    • Tumor suppressor microR-NAs, miR-100 and -125b, are regulated by 1,25-dihydroxyvitamin D in primary prostate cells and in patient tissue
    • Giangreco AA, Vaishnav A, Wagner D, et al. Tumor suppressor microR-NAs, miR-100 and -125b, are regulated by 1,25-dihydroxyvitamin D in primary prostate cells and in patient tissue. Cancer Prev Res (Phila). 2013;6: 483-494.
    • (2013) Cancer Prev Res (Phila) , vol.6 , pp. 483-494
    • Giangreco, A.A.1    Vaishnav, A.2    Wagner, D.3
  • 18
    • 79951529658 scopus 로고    scopus 로고
    • MiR-125bpromotes growth of prostate cancer xenograft tumor through targeting pro-apoptotic genes
    • Shi XB, Xue L, Ma AH, Tepper CG, Kung HJ, White RW. miR-125b promotes growth of prostate cancer xenograft tumor through targeting pro-apoptotic genes. Prostate. 2011;71:538-549.
    • (2011) Prostate , vol.71 , pp. 538-549
    • Shi, X.B.1    Xue, L.2    Ma, A.H.3    Tepper, C.G.4    Kung, H.J.5    White, R.W.6
  • 19
    • 80055100472 scopus 로고    scopus 로고
    • Feng DD, et al. MiR-125b, a target of CDX2, regulates cell differentiation through repression of the core binding factor in hematopoietic malignancies
    • Lin KY, Zhang XJ, Feng DD, et al. miR-125b, a target of CDX2, regulates cell differentiation through repression of the core binding factor in hematopoietic malignancies. J Biol Chem. 2011;286:38253-38263.
    • (2011) J Biol Chem , vol.286 , pp. 38253-38263
    • Lin, K.Y.1    Zhang, X.J.2
  • 20
    • 84877103458 scopus 로고    scopus 로고
    • RNA-binding protein PCBP2 modulates glioma growth by regulating FHL3
    • Han W, Xin Z, Zhao Z, et al. RNA-binding protein PCBP2 modulates glioma growth by regulating FHL3. J Clin Invest. 2013;123: 2103-2118.
    • (2013) J Clin Invest , vol.123 , pp. 2103-2118
    • Han, W.1    Xin, Z.2    Zhao, Z.3
  • 21
    • 84874487252 scopus 로고    scopus 로고
    • Sirtuin7 oncogenic potential in humanhepatocellular carcinoma and its regulation by the tumor suppressorsMiR-125a-5p and MiR-125b
    • Kim JK, Noh JH, Jung KH, et al. Sirtuin7 oncogenic potential in human hepatocellular carcinoma and its regulation by the tumor suppressors MiR-125a-5p and MiR-125b. Hepatology. 2013;57:1055-1067.
    • (2013) Hepatology , vol.57 , pp. 1055-1067
    • Kim, J.K.1    Noh, J.H.2    Jung, K.H.3
  • 22
    • 34547862845 scopus 로고    scopus 로고
    • Screening of mutations in the PHF8 gene and identification of a novel mutation in a Finnish family with XLMR and cleft lip/cleft palate
    • Koivisto AM, Ala-Mello S, Lemmelä S, Komu HA, Rautio J, Järvelä I. Screening of mutations in the PHF8 gene and identification of a novel mutation in a Finnish family with XLMR and cleft lip/cleft palate. Clin Genet. 2007;72:145-149.
    • (2007) Clin Genet , vol.72 , pp. 145-149
    • Koivisto, A.M.1    Ala-Mello, S.2    Lemmelä, S.3    Komu, H.A.4    Rautio, J.5    Järvelä, I.6
  • 23
    • 77949432014 scopus 로고    scopus 로고
    • PHF8, a gene associated withcleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylase
    • Loenarz C, Ge W, Coleman ML, et al. PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylase. Hum Mol Genet. 2010;19:217-222.
    • (2010) Hum Mol Genet , vol.19 , pp. 217-222
    • Loenarz, C.1    Ge, W.2    Coleman, M.L.3
  • 24
    • 77950893589 scopus 로고    scopus 로고
    • A functional link between the histone demethylase PHF8 and the transcription factorZNF711 in X-linked mental retardation
    • Kleine-Kohlbrecher D, Christensen J, Vandamme J, et al. A functional link between the histone demethylase PHF8 and the transcription factor ZNF711 in X-linked mental retardation. Mol Cell. 2010;38:165-178.
    • (2010) Mol Cell , vol.38 , pp. 165-178
    • Kleine-Kohlbrecher, D.1    Christensen, J.2    Vandamme, J.3
  • 25
    • 77955280094 scopus 로고    scopus 로고
    • The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation
    • Qiu J, Shi G, Jia Y, et al. The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation. Cell Res. 2010;20:908-918.
    • (2010) Cell Res , vol.20 , pp. 908-918
    • Qiu, J.1    Shi, G.2    Jia, Y.3
  • 26
    • 84876443700 scopus 로고    scopus 로고
    • The histone demethylase PHF8governs retinoic acid response in acute promyelocytic leukemia
    • Arteaga MF, Mikesch JH, Qiu J, et al. The histone demethylase PHF8 governs retinoic acid response in acute promyelocytic leukemia. Cancer Cell. 2013;23:376-389.
    • (2013) Cancer Cell , vol.23 , pp. 376-389
    • Arteaga, M.F.1    Mikesch, J.H.2    Qiu, J.3
  • 27
    • 84885392388 scopus 로고    scopus 로고
    • Oncogenic features of PHF8 histone demethylase in esophageal squamous cell carcinoma
    • Sun X, Qiu JJ, Zhu S, et al. Oncogenic features of PHF8 histone demethylase in esophageal squamous cell carcinoma. PLoS One. 2013;8:e77353.
    • (2013) Plos One , vol.8
    • Sun, X.1    Qiu, J.J.2    Zhu, S.3
  • 28
    • 84906223659 scopus 로고    scopus 로고
    • The histone demethylase PHF8 is an oncogenicprotein in human non-small cell lung cancer
    • Shen Y, Pan X, Zhao H. The histone demethylase PHF8 is an oncogenic protein in human non-small cell lung cancer. Biochem Biophys Res Commun. 2014;451:119-125.
    • (2014) Biochem Biophys Res Commun , vol.451 , pp. 119-125
    • Shen, Y.1    Pan, X.2    Zhao, H.3
  • 29
    • 84864128191 scopus 로고    scopus 로고
    • Systematic knockdown ofepigenetic enzymes identifies a novel histone demethylase PHF8 overexpressed in prostate cancer with an impact on cell proliferation, migration and invasion
    • Björkman M, Östling P, Härmä V, et al. Systematic knockdown of epigenetic enzymes identifies a novel histone demethylase PHF8 overexpressed in prostate cancer with an impact on cell proliferation, migration and invasion. Oncogene. 2012;31:3444-3456.
    • (2012) Oncogene , vol.31 , pp. 3444-3456
    • Björkman, M.1    Östling, P.2    Härmä, V.3
  • 30
    • 65349104505 scopus 로고    scopus 로고
    • MicroRNAs and their potential for translation in prostate cancer
    • DeVere White RW, Vinall RL, Tepper CG, Shi XB. MicroRNAs and their potential for translation in prostate cancer. Urol Oncol. 2009;27: 307-311.
    • (2009) Urol Oncol , vol.27 , pp. 307-311
    • Devere White, R.W.1    Vinall, R.L.2    Tepper, C.G.3    Shi, X.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.