메뉴 건너뛰기




Volumn 31, Issue 3, 2011, Pages 359-364

Contribution of decreased expression of Ku70 to enhanced radiosensitivity by sodium butyrate in glioblastoma cell line (U251)

Author keywords

H2AX; DNA double strand breaks; Ku70; Radiosensitivity; Sodium butyrate

Indexed keywords

BUTYRIC ACID DERIVATIVE; CELL NUCLEUS ANTIGEN; DNA BINDING PROTEIN; H2AFX PROTEIN, HUMAN; HISTONE; KU ANTIGEN; MESSENGER RNA;

EID: 80455123679     PISSN: 16720733     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11596-011-0381-8     Document Type: Article
Times cited : (7)

References (42)
  • 1
    • 77952555038 scopus 로고    scopus 로고
    • Exciting new advances in neuro-oncology: The avenue to a cure for malignant glioma
    • Van Meir EG, Hadjipanayis CG, Norden AD, et al. Exciting new advances in neuro-oncology: the avenue to a cure for malignant glioma. CA Cancer J Clin, 2010,60(3): 166-193
    • (2010) CA Cancer J Clin , vol.60 , Issue.3 , pp. 166-193
    • Van Meir, E.G.1    Hadjipanayis, C.G.2    Norden, A.D.3
  • 2
    • 33748360764 scopus 로고    scopus 로고
    • Vorinostat, a histone deacetylase inhibitor, enhances the response of human tumor cells to ionizing radiation through prolongation of γ-H2AX foci
    • DOI 10.1158/1535-7163.MCT-06-0022
    • Munshi A, Tanaka T, Hobbs ML, et al. Vorinostat, a his-tone deacetylase inhibitor, enhances the response of hu-man tumor cells to ionizing radiation through prolongation of gamma-H2AX foci. Mol Cancer Ther, 2006,5(8):1967-1974 (Pubitemid 44336568)
    • (2006) Molecular Cancer Therapeutics , vol.5 , Issue.8 , pp. 1967-1974
    • Munshi, A.1    Tanaka, T.2    Hobbs, M.L.3    Tucker, S.L.4    Richon, V.M.5    Meyn, R.E.6
  • 3
    • 33845741562 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitor LBH589 increases duration of γ-H2AX foci and confines HDAC4 to the cytoplasm in irradiated non-small cell lung cancer
    • DOI 10.1158/0008-5472.CAN-06-0049
    • Geng L, Cuneo KC, Fu A, et al. Histone deacetylase (HDAC) inhibitor LBH589 increases duration of gamma-H2AX foci and confines HDAC4 to the cyto-plasm in irradiated non-small cell lung cancer. Cancer Res, 2006,66(23):11298-11304 (Pubitemid 46009960)
    • (2006) Cancer Research , vol.66 , Issue.23 , pp. 11298-11304
    • Geng, L.1    Cuneo, K.C.2    Fu, A.3    Tu, T.4    Atadja, P.W.5    Hallahan, D.E.6
  • 4
    • 70349938071 scopus 로고    scopus 로고
    • A novel gamma-lactam-based histone deacetylase inhibitor potently inhibits the growth of human breast and renal cancer cells
    • Kwon HK, Ahn SH, Park SH, et al. A novel gamma-lactam-based histone deacetylase inhibitor potently inhibits the growth of human breast and renal cancer cells. Biol Pharm Bull, 2009,32(10):1723-1727
    • (2009) Biol Pharm Bull , vol.32 , Issue.10 , pp. 1723-1727
    • Kwon, H.K.1    Ahn, S.H.2    Park, S.H.3
  • 6
    • 63849300533 scopus 로고    scopus 로고
    • The role of histone deacetylases in prostate cancer
    • Abbas A, Gupta S. The role of histone deacetylases in prostate cancer. Epigenetics, 2008,3(6):300-309
    • (2008) Epigenetics , vol.3 , Issue.6 , pp. 300-309
    • Abbas, A.1    Gupta, S.2
  • 7
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • DOI 10.1038/38664
    • Grunstein M. Histone acetylation in chromatin structure and transcription. Nature, 1997,389(6649):349-352 (Pubitemid 27415209)
    • (1997) Nature , vol.389 , Issue.6649 , pp. 349-352
    • Grunstein, M.1
  • 8
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl K. Histone acetylation and transcriptional regula-tory mechanisms. Genes Dev, 1998,12(5):599-606 (Pubitemid 28134293)
    • (1998) Genes and Development , vol.12 , Issue.5 , pp. 599-606
    • Struhl, K.1
  • 9
    • 0033767848 scopus 로고    scopus 로고
    • Mechanism of cell cycle arrest caused by histone deacetylase inhibitors in human carcinoma cells
    • Kim YB, Ki SW, Yoshida M, et al. Mechanism of cell cycle arrest caused by histone deacetylase inhibitors in human carcinoma cells. J Antibiot (Tokyo), 2000,53(10): 1191-1200
    • (2000) J Antibiot (Tokyo) , vol.53 , Issue.10 , pp. 1191-1200
    • Kim, Y.B.1    Ki, S.W.2    Yoshida, M.3
  • 11
    • 0034071282 scopus 로고    scopus 로고
    • The intracellular target of butyrate's actions: HDAC or HDON'T?
    • DOI 10.1136/gut.46.4.447
    • Gibson PR. The intracellular target of butyrate's actions: HDAC or HDON'TII Gut, 2000,46(4):447-448 (Pubitemid 30305801)
    • (2000) Gut , vol.46 , Issue.4 , pp. 447-448
    • Gibson, P.R.1
  • 13
    • 0022366477 scopus 로고
    • Enhancement of radiation injury in human colon tumor cells by the maturational agent sodium butyrate (NaB)
    • Arundel CM, Glicksman AS, Leith JT. Enhancement of radiation injury in human colon tumor cells by the matu-rational agent sodium butyrate (NaB). Radiat Res, 1985,104(3):443-448 (Pubitemid 16146490)
    • (1985) Radiation Research , vol.104 , Issue.3 , pp. 443-448
    • Arundel, C.M.1    Glicksman, A.S.2    Leith, J.T.3
  • 15
    • 59549097382 scopus 로고    scopus 로고
    • Vitro and in vivo radiosensitization of glioblastoma cells by the poly (ADP-ribose) polymerase inhibitor E7016
    • Russo AL, Kwon HC, Burgan WE, et al. In vitro and in vivo radiosensitization of glioblastoma cells by the poly (ADP-ribose) polymerase inhibitor E7016. Clin Cancer Res, 2009,15(2):607-612
    • (2009) Clin Cancer Res , vol.15 , Issue.2 , pp. 607-612
    • Russo, A.L.1    Kwon, H.C.2    Burgan, W.E.3
  • 16
    • 40549111956 scopus 로고    scopus 로고
    • Influence of sodium butyrate on hepatocellular carcinoma (HepG2) and glioblastoma (C6) cell lines in vitro
    • Joachimiak R, Kaznica A, Drewa T. Influence of sodium butyrate on hepatocellular carcinoma (hepG2) and glioblastoma (C6) cell lines in vitro. Acta Pol Pharm, 2007,64(6):561-563 (Pubitemid 351360389)
    • (2007) Acta Poloniae Pharmaceutica - Drug Research , vol.64 , Issue.6 , pp. 561-563
    • Joachimiak, R.1    Kaznica, A.2    Drewa, T.3
  • 17
    • 14944375437 scopus 로고    scopus 로고
    • The histone deace-tylase inhibitor sodium butyrate induces breast cancer cell apoptosis through diverse cytotoxic actions including glutathione depletion and oxidative stress
    • Louis M, Rosato RR, Brault L, et al. The histone deace-tylase inhibitor sodium butyrate induces breast cancer cell apoptosis through diverse cytotoxic actions including glutathione depletion and oxidative stress. Int J Oncol, 2004,25(6):1701-1711
    • (2004) Int J Oncol , vol.25 , Issue.6 , pp. 1701-1711
    • Louis, M.1    Rosato, R.R.2    Brault, L.3
  • 18
    • 70349240449 scopus 로고    scopus 로고
    • Sodium butyrate induces human colon carcinoma HT-29 cell apoptosis through a mito-chondrial pathway
    • Wang L, Luo HS, Xia H. Sodium butyrate induces human colon carcinoma HT-29 cell apoptosis through a mito-chondrial pathway. J Int Med Res, 2009,37(3): 803-811
    • (2009) J Int Med Res , vol.37 , Issue.3 , pp. 803-811
    • Wang, L.1    Luo, H.S.2    Xia, H.3
  • 19
  • 20
    • 65949105730 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor sodium butyrate enhances the cell killing effect of psoralen plus UVA by attenuating nucleotide excision repair
    • Toyooka T, Ibuki Y. Histone deacetylase inhibitor sodium butyrate enhances the cell killing effect of psoralen plus UVA by attenuating nucleotide excision repair. Cancer Res, 2009,69(8):3492-3500
    • (2009) Cancer Res , vol.69 , Issue.8 , pp. 3492-3500
    • Toyooka, T.1    Ibuki, Y.2
  • 21
    • 48749114296 scopus 로고    scopus 로고
    • Enhancement of sodium butyrate-induced cell death and apoptosis by X-irradiation in the human colorectal cancer cell line HCT 116
    • Wei ZL, Zhao QL, Yu DY, et al. Enhancement of sodium butyrate-induced cell death and apoptosis by X-irradiation in the human colorectal cancer cell line HCT 116. Oncol Rep, 2008,20(2):397-403
    • (2008) Oncol Rep , vol.20 , Issue.2 , pp. 397-403
    • Wei, Z.L.1    Zhao, Q.L.2    Yu, D.Y.3
  • 22
    • 37649015347 scopus 로고    scopus 로고
    • HDAC inhibi-tor PCI-24781 decreases RAD51 expression and inhibits homologous recombination
    • Adimoolam S, Sirisawad M, Chen J, et al. HDAC inhibi- tor PCI-24781 decreases RAD51 expression and inhibits homologous recombination. Proc Natl Acad Sci U S A, 2007,104(49):19482-19487
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.49 , pp. 19482-19487
    • Adimoolam, S.1    Sirisawad, M.2    Chen, J.3
  • 23
    • 34548564426 scopus 로고    scopus 로고
    • Attenuated DNA damage repair by trichostatin a through BRCA1 suppression
    • DOI 10.1667/RR0811.1
    • Zhang Y, Carr T, Dimtchev A, et al. Attenuated DNA damage repair by trichostatin A through BRCA1 suppression. Radiat Res, 2007,168(1):115-124 (Pubitemid 351292932)
    • (2007) Radiation Research , vol.168 , Issue.1 , pp. 115-124
    • Zhang, Y.1    Carr, T.2    Dimtchev, A.3    Zaer, N.4    Dritschilo, A.5    Jung, M.6
  • 24
    • 68149170764 scopus 로고    scopus 로고
    • Sensitization to gamma-irradiation-induced cell cycle arrest and apoptosis by the histone deacetylase inhibitor trichostatin A in non-small cell lung cancer (NSCLC) cells
    • Zhang F, Zhang T, Teng ZH, et al. Sensitization to gamma-irradiation- induced cell cycle arrest and apoptosis by the histone deacetylase inhibitor trichostatin A in non-small cell lung cancer (NSCLC) cells. Cancer Biol Ther, 2009,8(9):823-831
    • (2009) Cancer Biol Ther , vol.8 , Issue.9 , pp. 823-831
    • Zhang, F.1    Zhang, T.2    Teng, Z.H.3
  • 26
    • 10044280340 scopus 로고    scopus 로고
    • 1 arrest in fibroblasts
    • DOI 10.1002/jcp.20094
    • Chen JS, Faller DV. Histone deacetylase inhibition-mediated post-translational elevation of p27KIP1 protein levels is required for G1 arrest in fibroblasts. J Cell Physiol, 2005,202(1):87-99 (Pubitemid 39603365)
    • (2005) Journal of Cellular Physiology , vol.202 , Issue.1 , pp. 87-99
    • Chen, J.S.1    Faller, D.V.2
  • 28
    • 67349285731 scopus 로고    scopus 로고
    • Enhancing the apop-totic and therapeutic effects of HDAC inhibitors
    • Frew AJ, Johnstone RW, Bolden JE. Enhancing the apop-totic and therapeutic effects of HDAC inhibitors. Cancer Lett, 2009,280(2):125-133
    • (2009) Cancer Lett , vol.280 , Issue.2 , pp. 125-133
    • Frew, A.J.1    Johnstone, R.W.2    Bolden, J.E.3
  • 29
    • 0031742958 scopus 로고    scopus 로고
    • The role of DNA single- and double-strand breaks in cell killing by ionizing radiation
    • Olive PL. The role of DNA single- and double-strand breaks in cell killing by ionizing radiation. Radiat Res, 1998,150(5 Suppl):S42-51 (Pubitemid 28519050)
    • (1998) Radiation Research , vol.150 , Issue.5 SUPPL.
    • Olive, P.L.1
  • 35
    • 65449169699 scopus 로고    scopus 로고
    • Gamma H2AX in the recognition of DNA double-strand breaks
    • Podhorecka M. Gamma H2AX in the recognition of DNA double-strand breaks. Postepy Hig Med Dosw (Online), 2009,63:92-98
    • (2009) Postepy Hig Med Dosw (Online) , vol.63 , pp. 92-98
    • Podhorecka, M.1
  • 36
    • 0036789173 scopus 로고    scopus 로고
    • Quan-titative detection of (125)IdU-induced DNA dou-ble-strand breaks with gamma-H2AX antibody
    • Sedelnikova OA, Rogakou EP, Panyutin IG, et al. Quan-titative detection of (125)IdU-induced DNA dou-ble-strand breaks with gamma-H2AX antibody. Radiat Res, 2002,158(4):486-492
    • (2002) Radiat Res , vol.158 , Issue.4 , pp. 486-492
    • Sedelnikova, O.A.1    Rogakou, E.P.2    Panyutin, I.G.3
  • 38
    • 4944234150 scopus 로고    scopus 로고
    • Radiation sensitivity, H2AX phosphorylation, and kinetics of repair of DNA strand breaks in irradiated cervical cancer cell lines
    • DOI 10.1158/0008-5472.CAN-04-1433
    • Banath JP, Macphail SH, Olive PL. Radiation sensitivity, H2AX phosphorylation, and kinetics of repair of DNA strand breaks in irradiated cervical cancer cell lines. Cancer Res, 2004,64(19):7144-7149 (Pubitemid 39331029)
    • (2004) Cancer Research , vol.64 , Issue.19 , pp. 7144-7149
    • Banath, J.P.1    MacPhail, S.H.2    Olive, P.L.3
  • 40
    • 75749130671 scopus 로고    scopus 로고
    • Mechanism of elimination of phosphorylated histone H2AX from chro-matin after repair of DNA double-strand breaks
    • Svetlova MP, Solovjeva LV, Tomilin NV. Mechanism of elimination of phosphorylated histone H2AX from chro-matin after repair of DNA double-strand breaks. Mutat Res, 2010,685(1-2):54-60
    • (2010) Mutat Res , vol.685 , Issue.1-2 , pp. 54-60
    • Svetlova, M.P.1    Solovjeva, L.V.2    Tomilin, N.V.3
  • 41
    • 70549088952 scopus 로고    scopus 로고
    • Scriptaid, a novel histone deacetylase inhibitor, enhances the response of human tumor cells to radiation
    • Kuribayashi T, Ohara M, Sora S, et al. Scriptaid, a novel histone deacetylase inhibitor, enhances the response of human tumor cells to radiation. Int J Mol Med, 2010,25(1):25-29
    • (2010) Int J Mol Med , vol.25 , Issue.1 , pp. 25-29
    • Kuribayashi, T.1    Ohara, M.2    Sora, S.3
  • 42
    • 77954024844 scopus 로고    scopus 로고
    • HDAC inhibi-tor-mediated radiosensitization in human carcinoma cells: A general phenomenonII
    • Kim IA, Kim IH, Kim HJ, et al. HDAC inhibi- tor-mediated radiosensitization in human carcinoma cells: a general phenomenonII J Radiat Res (Tokyo), 2010,51(3):257-263
    • (2010) J Radiat Res (Tokyo) , vol.51 , Issue.3 , pp. 257-263
    • Kim, I.A.1    Kim, I.H.2    Kim, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.