메뉴 건너뛰기




Volumn 50, Issue 9, 2009, Pages 4072-4079

Molecular sequelae of histone deacetylase inhibition in human retinoblastoma cell lines: Clinical implications

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYCINNAMIC ACID BISHYDROXAMIDE; CASPASE 3; CASPASE 8; CASPASE 9; DOXORUBICIN; EPHRIN; HISTONE DEACETYLASE INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MESSENGER RNA; NOTCH RECEPTOR; PROTEIN P53; UNCLASSIFIED DRUG; VORINOSTAT; BROXURIDINE; CASPASE; CINNAMIC ACID DERIVATIVE; ENZYME INHIBITOR; HISTONE; HISTONE DEACETYLASE; HYDROXAMIC ACID; TUMOR PROTEIN;

EID: 70349247886     PISSN: 01460404     EISSN: 15525783     Source Type: Journal    
DOI: 10.1167/iovs.09-3517     Document Type: Article
Times cited : (17)

References (51)
  • 1
    • 45149116184 scopus 로고    scopus 로고
    • The adverse events of chemotherapy for retinoblastoma: What are they? Do we know?
    • Rizzuti AE, Dunkel IJ, Abramson DH. The adverse events of chemotherapy for retinoblastoma: what are they? Do we know? Arch Ophthalmol. 2008;126:862-865.
    • (2008) Arch Ophthalmol , vol.126 , pp. 862-865
    • Rizzuti, A.E.1    Dunkel, I.J.2    Abramson, D.H.3
  • 3
    • 48149083652 scopus 로고    scopus 로고
    • A phase I/II study of direct intraarterial (ophthalmic artery) chemotherapy with melphalan for intraocular retinoblastoma initial results
    • Abramson DH, Dunkel IJ, Brodie SE, Kim JW, Gobin YP. A phase I/II study of direct intraarterial (ophthalmic artery) chemotherapy with melphalan for intraocular retinoblastoma initial results. Ophthalmology. 2008;115:1398-1404.
    • (2008) Ophthalmology , vol.115 , pp. 1398-1404
    • Abramson, D.H.1    Dunkel, I.J.2    Brodie, S.E.3    Kim, J.W.4    Gobin, Y.P.5
  • 4
    • 77956993222 scopus 로고    scopus 로고
    • Persistence of retinal function after selective ophthalmic artery chemotherapy infusion for retinoblastoma
    • In press
    • Brodie SE, Gobin YP, Dunkel IJ, Kim JW, Abramson DH. Persistence of retinal function after selective ophthalmic artery chemotherapy infusion for retinoblastoma. Doc Ophthalmol. In press.
    • Doc Ophthalmol
    • Brodie, S.E.1    Gobin, Y.P.2    Dunkel, I.J.3    Kim, J.W.4    Abramson, D.H.5
  • 5
    • 0015043748 scopus 로고
    • Mutation and cancer: Statistical study of retinoblastoma
    • Knudson AG Jr. Mutation and cancer: statistical study of retinoblastoma. Proc Natl Acad Sci U S A. 1971;68:820-823.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 820-823
    • Knudson Jr, A.G.1
  • 9
    • 36048958965 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Overview and perspectives
    • Dokmanovic M, Clarke C, Marks PA. Histone deacetylase inhibitors: overview and perspectives. Mol Cancer Res. 2007;5: 981-989.
    • (2007) Mol Cancer Res , vol.5 , pp. 981-989
    • Dokmanovic, M.1    Clarke, C.2    Marks, P.A.3
  • 10
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: Development of this histone deacetylase inhibitor as an anticancer drug
    • Marks PA, Breslow R. Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug. Nat Biotechnol. 2007;25:84-90.
    • (2007) Nat Biotechnol , vol.25 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 11
    • 33847258674 scopus 로고    scopus 로고
    • Discovery and development of SAHA as an anticancer agent
    • Marks PA. Discovery and development of SAHA as an anticancer agent. Oncogene. 2007;26:1351-1356.
    • (2007) Oncogene , vol.26 , pp. 1351-1356
    • Marks, P.A.1
  • 12
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • Finnin MS, Donigian JR, Cohen A, et al. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature. 1999;401:188-193.
    • (1999) Nature , vol.401 , pp. 188-193
    • Finnin, M.S.1    Donigian, J.R.2    Cohen, A.3
  • 13
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action
    • Xu WS, Parmigiani RB, Marks PA. Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene. 2007;26:5541-5552.
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 14
    • 12444321545 scopus 로고    scopus 로고
    • Phase I clinical trial of histone deacetylase inhibitor: Suberoylanilide hydroxamic acid administered intravenously
    • Kelly WK, Richon VM, O'Connor O, et al. Phase I clinical trial of histone deacetylase inhibitor: suberoylanilide hydroxamic acid administered intravenously. Clin Cancer Res. 2003;9:3578-3588.
    • (2003) Clin Cancer Res , vol.9 , pp. 3578-3588
    • Kelly, W.K.1    Richon, V.M.2    O'Connor, O.3
  • 15
    • 39749103428 scopus 로고    scopus 로고
    • Phase I trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) in patients with advanced multiple myeloma
    • Richardson P, Mitsiades C, Colson K, et al. Phase I trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) in patients with advanced multiple myeloma. Leuk Lymphoma. 2008;49:502-507.
    • (2008) Leuk Lymphoma , vol.49 , pp. 502-507
    • Richardson, P.1    Mitsiades, C.2    Colson, K.3
  • 16
    • 21244464349 scopus 로고    scopus 로고
    • Phase I study of an oral histone deacetylase inhibitor, suberoylanilide hydroxamic acid, in patients with advanced cancer
    • Kelly WK, O'Connor OA, Krug LM, et al. Phase I study of an oral histone deacetylase inhibitor, suberoylanilide hydroxamic acid, in patients with advanced cancer. J Clin Oncol. 2005;23:3923-3931.
    • (2005) J Clin Oncol , vol.23 , pp. 3923-3931
    • Kelly, W.K.1    O'Connor, O.A.2    Krug, L.M.3
  • 17
    • 36148950997 scopus 로고    scopus 로고
    • FDA approval summary: Vorinostat for treatment of advanced primary cutaneous T-cell lymphoma
    • Mann BS, Johnson JR, Cohen MH, Justice R, Pazdur R. FDA approval summary: vorinostat for treatment of advanced primary cutaneous T-cell lymphoma. Oncologist. 2007;12:1247-1252.
    • (2007) Oncologist , vol.12 , pp. 1247-1252
    • Mann, B.S.1    Johnson, J.R.2    Cohen, M.H.3    Justice, R.4    Pazdur, R.5
  • 18
    • 33845996135 scopus 로고    scopus 로고
    • Phase 2 trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) for refractory cutaneous T-cell lymphoma (CTCL)
    • Duvic M, Talpur R, Ni X, et al. Phase 2 trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) for refractory cutaneous T-cell lymphoma (CTCL). Blood. 2007;109:31-39.
    • (2007) Blood , vol.109 , pp. 31-39
    • Duvic, M.1    Talpur, R.2    Ni, X.3
  • 19
    • 34547683194 scopus 로고    scopus 로고
    • Phase IIb multicenter trial of vorinostat in patients with persistent, progressive, or treatment refractory cutaneous T-cell lymphoma
    • Olsen EA, Kim YH, Kuzel TM, et al. Phase IIb multicenter trial of vorinostat in patients with persistent, progressive, or treatment refractory cutaneous T-cell lymphoma. J Clin Oncol. 2007;25:3109-3115.
    • (2007) J Clin Oncol , vol.25 , pp. 3109-3115
    • Olsen, E.A.1    Kim, Y.H.2    Kuzel, T.M.3
  • 21
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • Luo RX, Postigo AA, Dean DC. Rb interacts with histone deacetylase to repress transcription. Cell. 1998;92:463-473.
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 22
    • 18844454753 scopus 로고    scopus 로고
    • Novel histone deacetylase inhibitors in the treatment of thyroid cancer
    • Mitsiades CS, Poulaki V, McMullan C, et al. Novel histone deacetylase inhibitors in the treatment of thyroid cancer. Clin Cancer Res. 2005;11:3958-3965.
    • (2005) Clin Cancer Res , vol.11 , pp. 3958-3965
    • Mitsiades, C.S.1    Poulaki, V.2    McMullan, C.3
  • 23
    • 19944414628 scopus 로고    scopus 로고
    • Human retinoblastoma cells are resistant to apoptosis induced by death receptors: Role of caspase-8 gene silencing
    • Poulaki V, Mitsiades CS, McMullan C, et al. Human retinoblastoma cells are resistant to apoptosis induced by death receptors: role of caspase-8 gene silencing. Invest Ophthalmol Vis Sci. 2005;46:358-366.
    • (2005) Invest Ophthalmol Vis Sci , vol.46 , pp. 358-366
    • Poulaki, V.1    Mitsiades, C.S.2    McMullan, C.3
  • 24
  • 25
    • 35748936774 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib induces apoptosis in human retinoblastoma cell lines in vitro
    • Poulaki V, Mitsiades CS, Kotoula V, et al. The proteasome inhibitor bortezomib induces apoptosis in human retinoblastoma cell lines in vitro. Invest Ophthalmol Vis Sci. 2007;48:4706-4719.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 4706-4719
    • Poulaki, V.1    Mitsiades, C.S.2    Kotoula, V.3
  • 26
    • 0034523818 scopus 로고    scopus 로고
    • Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer SJ, Wei MC, Saito M, Weiler S, Oh KJ, Schlesinger PH. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ. 2000;7:1166-1173.
    • (2000) Cell Death Differ , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 27
    • 0037589018 scopus 로고    scopus 로고
    • Molecular sequelae of histone deacetylase inhibition in human malignant B cells
    • Mitsiades N, Mitsiades CS, Richardson PG, et al. Molecular sequelae of histone deacetylase inhibition in human malignant B cells. Blood. 2003;101:4055-4062.
    • (2003) Blood , vol.101 , pp. 4055-4062
    • Mitsiades, N.1    Mitsiades, C.S.2    Richardson, P.G.3
  • 28
    • 9144220841 scopus 로고    scopus 로고
    • Transcriptional signature of histone deacetylase inhibition in multiple myeloma: Biological and clinical implications
    • Mitsiades CS, Mitsiades NS, McMullan CJ, et al. Transcriptional signature of histone deacetylase inhibition in multiple myeloma: biological and clinical implications. Proc Natl Acad Sci U S A. 2004;101:540-545.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 540-545
    • Mitsiades, C.S.1    Mitsiades, N.S.2    McMullan, C.J.3
  • 29
    • 0026165992 scopus 로고
    • Effect of butyrate and corticosteroids on retinoblastoma in vitro and in vivo
    • Howard MA, Wardwell S, Albert DM. Effect of butyrate and corticosteroids on retinoblastoma in vitro and in vivo. Invest Ophthalmol Vis Sci. 1991;32:1711-1713.
    • (1991) Invest Ophthalmol Vis Sci , vol.32 , pp. 1711-1713
    • Howard, M.A.1    Wardwell, S.2    Albert, D.M.3
  • 30
    • 0021205549 scopus 로고
    • Effects of butyrate, retinol, and retinoic acid on human Y-79 retinoblastoma cells growing in monolayer cultures
    • Kyritsis A, Joseph G, Chader GJ. Effects of butyrate, retinol, and retinoic acid on human Y-79 retinoblastoma cells growing in monolayer cultures. J Natl Cancer Inst. 1984;73:649-654.
    • (1984) J Natl Cancer Inst , vol.73 , pp. 649-654
    • Kyritsis, A.1    Joseph, G.2    Chader, G.J.3
  • 31
    • 0028809535 scopus 로고
    • Induction of apoptosis by sodium butyrate in the human Y-79 retinoblastoma cell line
    • Conway RM, Madigan MC, Penfold PL, Billson FA. Induction of apoptosis by sodium butyrate in the human Y-79 retinoblastoma cell line. Oncology Res. 1995;7:289-297.
    • (1995) Oncology Res , vol.7 , pp. 289-297
    • Conway, R.M.1    Madigan, M.C.2    Penfold, P.L.3    Billson, F.A.4
  • 32
    • 0033230594 scopus 로고    scopus 로고
    • The apoptotic effects and synergistic interaction of sodium butyrate and MG132 in human retinoblastoma Y79 cells
    • Giuliano M, Lauricella M, Calvaruso G, et al. The apoptotic effects and synergistic interaction of sodium butyrate and MG132 in human retinoblastoma Y79 cells. Cancer Res. 1999;59:5586-5595.
    • (1999) Cancer Res , vol.59 , pp. 5586-5595
    • Giuliano, M.1    Lauricella, M.2    Calvaruso, G.3
  • 33
    • 0032188984 scopus 로고    scopus 로고
    • Vincristine- and cisplatin-induced apoptosis in human retinoblastoma: Potentiation by sodium butyrate
    • Conway RM, Madigan MC, Billson FA, Penfold PL. Vincristine- and cisplatin-induced apoptosis in human retinoblastoma: potentiation by sodium butyrate. Eur J Cancer. 1998;34:1741-1748.
    • (1998) Eur J Cancer , vol.34 , pp. 1741-1748
    • Conway, R.M.1    Madigan, M.C.2    Billson, F.A.3    Penfold, P.L.4
  • 34
    • 0017886958 scopus 로고
    • Sodium butyrate inhibits histone deacetylation in cultured cells
    • Candido EP, Reeves R, Davie JR. Sodium butyrate inhibits histone deacetylation in cultured cells. Cell. 1978;14:105-113.
    • (1978) Cell , vol.14 , pp. 105-113
    • Candido, E.P.1    Reeves, R.2    Davie, J.R.3
  • 35
    • 0034596309 scopus 로고    scopus 로고
    • Histone deacetylase inhibiors: Inducers of differentiation or apoptosis of transformed cells
    • Marks PA, Richon VM, Rifkind RA. Histone deacetylase inhibiors: inducers of differentiation or apoptosis of transformed cells. J Natl Cancer Inst. 2000;92:1210-1216.
    • (2000) J Natl Cancer Inst , vol.92 , pp. 1210-1216
    • Marks, P.A.1    Richon, V.M.2    Rifkind, R.A.3
  • 37
    • 0035046529 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Development of suberoylanilide hydroxamic acid (SAHA) for the treatment of cancers
    • Richon VM, Zhou X, Rifkind RA, Marks PA. Histone deacetylase inhibitors: development of suberoylanilide hydroxamic acid (SAHA) for the treatment of cancers. Blood Cells Mol Dis. 2001; 27:260-264.
    • (2001) Blood Cells Mol Dis , vol.27 , pp. 260-264
    • Richon, V.M.1    Zhou, X.2    Rifkind, R.A.3    Marks, P.A.4
  • 38
    • 0032539890 scopus 로고    scopus 로고
    • A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases
    • Richon VM, Emiliani S, Verdin E, et al. A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases. Proc Natl Acad Sci U S A. 1998;95:3003-3007.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3003-3007
    • Richon, V.M.1    Emiliani, S.2    Verdin, E.3
  • 39
    • 0035965343 scopus 로고    scopus 로고
    • Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen
    • Phiel CJ, Zhang F, Huang EY, Guenther MG, Lazar MA, Klein PS. Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J Biol Chem. 2001; 276:36734-36741.
    • (2001) J Biol Chem , vol.276 , pp. 36734-36741
    • Phiel, C.J.1    Zhang, F.2    Huang, E.Y.3    Guenther, M.G.4    Lazar, M.A.5    Klein, P.S.6
  • 40
    • 0036301281 scopus 로고    scopus 로고
    • Phase I trial of the histone deacetylase inhibitor, depsipeptide (FR901228, NSC 630176), in patients with refractory neoplasms
    • Sandor V, Bakke S, Robey RW, et al. Phase I trial of the histone deacetylase inhibitor, depsipeptide (FR901228, NSC 630176), in patients with refractory neoplasms. Clin Cancer Res. 2002;8:718-728.
    • (2002) Clin Cancer Res , vol.8 , pp. 718-728
    • Sandor, V.1    Bakke, S.2    Robey, R.W.3
  • 41
    • 49649085534 scopus 로고    scopus 로고
    • Evaluation of the in vitro and in vivo antitumor activity of histone deacetylase inhibitors for the therapy of retinoblastoma
    • Dalgard CL, Van Quill KR, O'Brien JM. Evaluation of the in vitro and in vivo antitumor activity of histone deacetylase inhibitors for the therapy of retinoblastoma. Clin Cancer Res. 2008;14:3113-3123.
    • (2008) Clin Cancer Res , vol.14 , pp. 3113-3123
    • Dalgard, C.L.1    van Quill, K.R.2    O'Brien, J.M.3
  • 42
    • 14944356392 scopus 로고    scopus 로고
    • Effects of the histone deacetylase inhibitor valproic acid on Notch signaling in human neuroblastoma cells
    • Stockhausen MT, Sjolund J, Manetopoulos C, Axelson H. Effects of the histone deacetylase inhibitor valproic acid on Notch signaling in human neuroblastoma cells. Br J Cancer. 2005;92:751-759.
    • (2005) Br J Cancer , vol.92 , pp. 751-759
    • Stockhausen, M.T.1    Sjolund, J.2    Manetopoulos, C.3    Axelson, H.4
  • 44
    • 34548463002 scopus 로고    scopus 로고
    • Valproic acid activates notch-1 signaling and regulates the neuroendocrine phenotype in carcinoid cancer cells
    • Greenblatt DY, Vaccaro AM, Jaskula-Sztul R, et al. Valproic acid activates notch-1 signaling and regulates the neuroendocrine phenotype in carcinoid cancer cells. Oncologist. 2007;12:942-951.
    • (2007) Oncologist , vol.12 , pp. 942-951
    • Greenblatt, D.Y.1    Vaccaro, A.M.2    Jaskula-Sztul, R.3
  • 45
    • 48749119660 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors upregulate Notch-1 and inhibit growth in pheochromocytoma cells
    • discussion 961-952
    • Adler JT, Hottinger DG, Kunnimalaiyaan M, Chen H. Histone deacetylase inhibitors upregulate Notch-1 and inhibit growth in pheochromocytoma cells. Surgery. 144:956-961, 2008; discussion 961-952.
    • (2008) Surgery , vol.144 , pp. 956-961
    • Adler, J.T.1    Hottinger, D.G.2    Kunnimalaiyaan, M.3    Chen, H.4
  • 46
    • 51749123773 scopus 로고    scopus 로고
    • Valproic acid induces Notch1 signaling in small cell lung cancer cells
    • Platta CS, Greenblatt DY, Kunnimalaiyaan M, Chen H. Valproic acid induces Notch1 signaling in small cell lung cancer cells. J Surg Res. 2008;148:31-37.
    • (2008) J Surg Res , vol.148 , pp. 31-37
    • Platta, C.S.1    Greenblatt, D.Y.2    Kunnimalaiyaan, M.3    Chen, H.4
  • 47
    • 21744442937 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor valproic acid alters sensitivity towards all-trans retinoic acid in acute myeloblastic leukemia cells
    • Trus MR, Yang L, Suarez Saiz F, Bordeleau L, Jurisica I, Minden MD. The histone deacetylase inhibitor valproic acid alters sensitivity towards all-trans retinoic acid in acute myeloblastic leukemia cells. Leukemia. 2005;19:1161-1168.
    • (2005) Leukemia , vol.19 , pp. 1161-1168
    • Trus, M.R.1    Yang, L.2    Suarez, S.F.3    Bordeleau, L.4    Jurisica, I.5    Minden, M.D.6
  • 48
    • 41149084179 scopus 로고    scopus 로고
    • Eph-ephrin bidirectional signaling in physiology and disease
    • Pasquale EB. Eph-ephrin bidirectional signaling in physiology and disease. Cell. 2008;133:38-52.
    • (2008) Cell , vol.133 , pp. 38-52
    • Pasquale, E.B.1
  • 49
    • 41549139097 scopus 로고    scopus 로고
    • Eph-ephrin signalling in adult tissues and cancer
    • Merlos-Suarez A, Batlle E. Eph-ephrin signalling in adult tissues and cancer. Curr Opin Cell Biol. 2008;20:194-200.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 194-200
    • Merlos-Suarez, A.1    Batlle, E.2
  • 50
    • 21344460054 scopus 로고    scopus 로고
    • EphB receptor activity suppresses colorectal cancer progression
    • Batlle E, Bacani J, Begthel H, et al. EphB receptor activity suppresses colorectal cancer progression. Nature. 2005;435:1126-1130.
    • (2005) Nature , vol.435 , pp. 1126-1130
    • Batlle, E.1    Bacani, J.2    Begthel, H.3
  • 51
    • 35548976379 scopus 로고    scopus 로고
    • EphB-ephrin-B interactions suppress colorectal cancer progression by compartmentalizing tumor cells
    • Cortina C, Palomo-Ponce S, Iglesias M, et al. EphB-ephrin-B interactions suppress colorectal cancer progression by compartmentalizing tumor cells. Nat Genet. 2007;39:1376-1383.
    • (2007) Nat Genet , vol.39 , pp. 1376-1383
    • Cortina, C.1    Palomo-Ponce, S.2    Iglesias, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.