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Volumn 13, Issue 24, 2007, Pages 7237-7242

Mechanisms of resistance to histone deacetylase inhibitors and their therapeutic implications

Author keywords

[No Author keywords available]

Indexed keywords

2 METHOXYESTRADIOL; 5 AZA 2' DEOXYCYTIDINE; ARYLBUTYRIC ACID DERIVATIVE; AZACITIDINE; BORTEZOMIB; BUTYRIC ACID; DOXORUBICIN; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; PANOBINOSTAT; PIVALOYLOXYMETHYL BUTYRATE; RETINOIC ACID; ROMIDEPSIN; SNDX 275; SODIUM PHENYLBUTYRATE; TRICHOSTATIN A; UNCLASSIFIED DRUG; VALPROIC ACID; VORINOSTAT;

EID: 37549043547     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: 10.1158/1078-0432.CCR-07-2114     Document Type: Review
Times cited : (105)

References (69)
  • 1
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • Gregoretti IV, Lee YM, Goodson HV. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J Mol Biol 2004;338:17-31.
    • (2004) J Mol Biol , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 2
    • 28644440158 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Discovery and development as anticancer agents
    • Marks PA, Dokmanovic M. Histone deacetylase inhibitors: discovery and development as anticancer agents. Expert Opin Investig Drugs 2005;14:1497-511.
    • (2005) Expert Opin Investig Drugs , vol.14 , pp. 1497-1511
    • Marks, P.A.1    Dokmanovic, M.2
  • 3
    • 34247880441 scopus 로고    scopus 로고
    • Development of histone deacetylase inhibitors for cancer treatment
    • Marchion D, Munster P. Development of histone deacetylase inhibitors for cancer treatment. Expert Rev Anticancer Ther 2007;7:583-98.
    • (2007) Expert Rev Anticancer Ther , vol.7 , pp. 583-598
    • Marchion, D.1    Munster, P.2
  • 4
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci S, Pelicci PG. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 2006;6:38-51.
    • (2006) Nat Rev Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 6
    • 0037052687 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SAHA) overcomes multidrug resistance and induces cell death in P-glycoprotein-expressing cells
    • Ruefli AA, Bernhard D, Tainton KM, et al. Suberoylanilide hydroxamic acid (SAHA) overcomes multidrug resistance and induces cell death in P-glycoprotein-expressing cells. Int J Cancer 2002;99:292-8.
    • (2002) Int J Cancer , vol.99 , pp. 292-298
    • Ruefli, A.A.1    Bernhard, D.2    Tainton, K.M.3
  • 7
    • 33748353002 scopus 로고    scopus 로고
    • Activity of PXD101, a histone deacetylase inhibitor, in preclinical ovarian cancer studies
    • Qian X, LaRochelle WJ, Ara G, et al. Activity of PXD101, a histone deacetylase inhibitor, in preclinical ovarian cancer studies. Mol Cancer Ther 2006;5:2086-95.
    • (2006) Mol Cancer Ther , vol.5 , pp. 2086-2095
    • Qian, X.1    LaRochelle, W.J.2    Ara, G.3
  • 8
    • 0036839093 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor AN-9 has selective toxicity to acute leukemia and drug-resistant primary leukemia and cancer cell lines
    • Batova A, Shao LE, Diccianni MB, et al. The histone deacetylase inhibitor AN-9 has selective toxicity to acute leukemia and drug-resistant primary leukemia and cancer cell lines. Blood 2002;100:3319-24.
    • (2002) Blood , vol.100 , pp. 3319-3324
    • Batova, A.1    Shao, L.E.2    Diccianni, M.B.3
  • 9
    • 20144385974 scopus 로고    scopus 로고
    • Efflux of depsipeptide FK228 (FR901228, NSC-630176) is mediated by P-glycoprotein and multidrug resistance-associated protein 1
    • Xiao JJ, Foraker AB, Swaan PW, et al. Efflux of depsipeptide FK228 (FR901228, NSC-630176) is mediated by P-glycoprotein and multidrug resistance-associated protein 1. J Pharmacol Exp Ther 2005;313:268-76.
    • (2005) J Pharmacol Exp Ther , vol.313 , pp. 268-276
    • Xiao, J.J.1    Foraker, A.B.2    Swaan, P.W.3
  • 10
    • 23044440043 scopus 로고    scopus 로고
    • Xiao JJ, Huang Y, Dai Z, et al. Chemoresistance to depsipeptide FK228 [(E)-(1S,4S,10S,21R)-7-[(Z)-ethylidene]-4,21-diisopropyl-2-oxa-12,13-dithia-5,8, 20,23-tetraazabicyclo[8,7,6]-tricos-16-ene-3,6,9,22-pentanone] is mediated by reversible MDR1 induction in human cancer cell lines. J Pharmacol Exp Ther 2005;314:467-75.
    • Xiao JJ, Huang Y, Dai Z, et al. Chemoresistance to depsipeptide FK228 [(E)-(1S,4S,10S,21R)-7-[(Z)-ethylidene]-4,21-diisopropyl-2-oxa-12,13-dithia-5,8, 20,23-tetraazabicyclo[8,7,6]-tricos-16-ene-3,6,9,22-pentanone] is mediated by reversible MDR1 induction in human cancer cell lines. J Pharmacol Exp Ther 2005;314:467-75.
  • 11
    • 32644438678 scopus 로고    scopus 로고
    • Up-regulation of MDR1 and induction of doxorubicin resistance by histone deacetylase inhibitor depsipeptide (FK228) and ATRA in acute promyelocytic leukemia cells
    • Tabe Y, Konopleva M, Contractor R, et al. Up-regulation of MDR1 and induction of doxorubicin resistance by histone deacetylase inhibitor depsipeptide (FK228) and ATRA in acute promyelocytic leukemia cells. Blood 2006;107:1546-54.
    • (2006) Blood , vol.107 , pp. 1546-1554
    • Tabe, Y.1    Konopleva, M.2    Contractor, R.3
  • 12
    • 0028283519 scopus 로고
    • Reversible transcriptional activation of mdr1 by sodium butyrate treatment of human colon cancer cells
    • Morrow CS, Nakagawa M, Goldsmith ME, et al. Reversible transcriptional activation of mdr1 by sodium butyrate treatment of human colon cancer cells. J Biol Chem 1994;269:10739-46.
    • (1994) J Biol Chem , vol.269 , pp. 10739-10746
    • Morrow, C.S.1    Nakagawa, M.2    Goldsmith, M.E.3
  • 13
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M, Kijima M, Akita M, et al. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem 1990;265:17174-9.
    • (1990) J Biol Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3
  • 14
    • 7444256739 scopus 로고    scopus 로고
    • Overexpression of histone deacetylase 1 confers resistance to sodium butyrate-mediated apoptosis in melanoma cells through a p53-mediated pathway
    • Bandyopadhyay D, Mishra A, Medrano EE. Overexpression of histone deacetylase 1 confers resistance to sodium butyrate-mediated apoptosis in melanoma cells through a p53-mediated pathway. Cancer Res 2004;64:7706-10.
    • (2004) Cancer Res , vol.64 , pp. 7706-7710
    • Bandyopadhyay, D.1    Mishra, A.2    Medrano, E.E.3
  • 15
    • 33646354640 scopus 로고    scopus 로고
    • A truncating mutation of HDAC2 in human cancers confers resistance to histone deacetylase inhibition
    • Ropero S, Fraga MF, Ballestar E, et al. A truncating mutation of HDAC2 in human cancers confers resistance to histone deacetylase inhibition. Nat Genet 2006;38:566-9.
    • (2006) Nat Genet , vol.38 , pp. 566-569
    • Ropero, S.1    Fraga, M.F.2    Ballestar, E.3
  • 16
    • 0032960181 scopus 로고    scopus 로고
    • Cancer epigenetics comes of age
    • Jones PA, Laird PW. Cancer epigenetics comes of age. Nat Genet 1999;21:163-7.
    • (1999) Nat Genet , vol.21 , pp. 163-167
    • Jones, P.A.1    Laird, P.W.2
  • 17
    • 0036274359 scopus 로고    scopus 로고
    • The fundamental role of epigenetic events in cancer
    • Jones PA, Baylin SB. The fundamental role of epigenetic events in cancer. Nat Rev Genet 2002;3:415-28.
    • (2002) Nat Rev Genet , vol.3 , pp. 415-428
    • Jones, P.A.1    Baylin, S.B.2
  • 18
    • 0032732788 scopus 로고    scopus 로고
    • Relationships between chromatin organization and DNA methylation in determining gene expression
    • Jones PL, Wolffe AP. Relationships between chromatin organization and DNA methylation in determining gene expression. Semin Cancer Biol 1999;9:339-47.
    • (1999) Semin Cancer Biol , vol.9 , pp. 339-347
    • Jones, P.L.1    Wolffe, A.P.2
  • 19
    • 0033601073 scopus 로고    scopus 로고
    • Methylation-induced repression-belts, braces, and chromatin
    • Bird AP, Wolffe AP. Methylation-induced repression-belts, braces, and chromatin. Cell 1999;99:451-4.
    • (1999) Cell , vol.99 , pp. 451-454
    • Bird, A.P.1    Wolffe, A.P.2
  • 20
    • 0842278570 scopus 로고    scopus 로고
    • Epigenetic changes in colorectal cancer
    • Kondo Y, Issa JP. Epigenetic changes in colorectal cancer. Cancer Metastasis Rev 2004;23:29-39.
    • (2004) Cancer Metastasis Rev , vol.23 , pp. 29-39
    • Kondo, Y.1    Issa, J.P.2
  • 21
    • 0034968451 scopus 로고    scopus 로고
    • Emerging connections between DNA methylation and histone acetylation
    • Dobosy JR, Selker EU. Emerging connections between DNA methylation and histone acetylation. Cell Mol Life Sci 2001;58:721-7.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 721-727
    • Dobosy, J.R.1    Selker, E.U.2
  • 22
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • Jones PA, Baylin SB. The epigenomics of cancer. Cell 2007;128:683-92.
    • (2007) Cell , vol.128 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 23
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron EE, Bachman KE, Myohanen S, et al. Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nat Genet 1999;21:103-7.
    • (1999) Nat Genet , vol.21 , pp. 103-107
    • Cameron, E.E.1    Bachman, K.E.2    Myohanen, S.3
  • 24
    • 0037115392 scopus 로고    scopus 로고
    • Dependence of histone modifications and gene expression on DNA hypermethylation in cancer
    • Fahrner JA, Eguchi S, Herman JG, et al. Dependence of histone modifications and gene expression on DNA hypermethylation in cancer. Cancer Res 2002;62:7213-8.
    • (2002) Cancer Res , vol.62 , pp. 7213-7218
    • Fahrner, J.A.1    Eguchi, S.2    Herman, J.G.3
  • 25
    • 33744829728 scopus 로고    scopus 로고
    • Promoter demethylation and histone acetylation mediate gene expression of MAGE-A1, -A2, -A3, and -A12 in human cancer cells
    • Wischnewski F, Pantel K, Schwarzenbach H. Promoter demethylation and histone acetylation mediate gene expression of MAGE-A1, -A2, -A3, and -A12 in human cancer cells. Mol Cancer Res 2006;4:339-49.
    • (2006) Mol Cancer Res , vol.4 , pp. 339-349
    • Wischnewski, F.1    Pantel, K.2    Schwarzenbach, H.3
  • 26
    • 34249774568 scopus 로고    scopus 로고
    • Transcriptional silencing of the TMS1/ASC tumour suppressor gene by an epigenetic mechanism in hepatocellular carcinoma cells
    • Zhang C, Li H, Zhou G, et al. Transcriptional silencing of the TMS1/ASC tumour suppressor gene by an epigenetic mechanism in hepatocellular carcinoma cells. J Pathol 2007;212:134-42.
    • (2007) J Pathol , vol.212 , pp. 134-142
    • Zhang, C.1    Li, H.2    Zhou, G.3
  • 27
    • 33947368681 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor Trichostatin A induces global and gene-specific DNA demethylation in human cancer cell lines
    • Ou JN, Torrisani J, Unterberger A, et al. Histone deacetylase inhibitor Trichostatin A induces global and gene-specific DNA demethylation in human cancer cell lines. Biochem Pharmacol 2007;73:1297-307.
    • (2007) Biochem Pharmacol , vol.73 , pp. 1297-1307
    • Ou, J.N.1    Torrisani, J.2    Unterberger, A.3
  • 28
    • 34047170360 scopus 로고    scopus 로고
    • Valproate induces widespread epigenetic reprogramming which involves demethylation of specific genes
    • Milutinovic S, D'Alessio AC, Detich N, et al. Valproate induces widespread epigenetic reprogramming which involves demethylation of specific genes. Carcinogenesis 2007;28:560-71.
    • (2007) Carcinogenesis , vol.28 , pp. 560-571
    • Milutinovic, S.1    D'Alessio, A.C.2    Detich, N.3
  • 29
    • 0142121430 scopus 로고    scopus 로고
    • Elevated levels of polyamines alter chromatin in murine skin and tumors without global changes in nucleosome acetylation
    • Hobbs CA, Paul BA, Gilmour SK. Elevated levels of polyamines alter chromatin in murine skin and tumors without global changes in nucleosome acetylation. Exp Cell Res 2003;290:427-36.
    • (2003) Exp Cell Res , vol.290 , pp. 427-436
    • Hobbs, C.A.1    Paul, B.A.2    Gilmour, S.K.3
  • 31
    • 0033569769 scopus 로고    scopus 로고
    • Functional interaction between GCN5 and polyamines: A new role for core histone acetylation
    • Pollard KJ, Samuels ML, Crowley KA, et al. Functional interaction between GCN5 and polyamines: a new role for core histone acetylation. EMBO J 1999;18:5622-33.
    • (1999) EMBO J , vol.18 , pp. 5622-5633
    • Pollard, K.J.1    Samuels, M.L.2    Crowley, K.A.3
  • 32
    • 33845231990 scopus 로고    scopus 로고
    • Ornithine decarboxylase activity in tumor cell lines correlates with sensitivity to cell death induced by histone deacetylase inhibitors
    • Saunders LR, Verdin E. Ornithine decarboxylase activity in tumor cell lines correlates with sensitivity to cell death induced by histone deacetylase inhibitors. Mol Cancer Ther 2006;5:2777-85.
    • (2006) Mol Cancer Ther , vol.5 , pp. 2777-2785
    • Saunders, L.R.1    Verdin, E.2
  • 33
    • 0035845541 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species
    • Ruefli AA, Ausserlechner MJ, Bernhard D, et al. The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species. Proc Natl Acad Sci U S A 2001;98:10833-8.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 10833-10838
    • Ruefli, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3
  • 34
    • 0038079767 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor MS-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21CIP1/WAF1 1
    • Rosato RR, Almenara JA, Grant S. The histone deacetylase inhibitor MS-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21CIP1/WAF1 1. Cancer Res 2003;63:3637-45.
    • (2003) Cancer Res , vol.63 , pp. 3637-3645
    • Rosato, R.R.1    Almenara, J.A.2    Grant, S.3
  • 35
    • 14944375437 scopus 로고    scopus 로고
    • The histone deacetylase 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 deacetylase inhibitor sodium butyrate induces breast cancer cell apoptosis through diverse cytotoxic actions including glutathione depletion and oxidative stress. Int J Oncol 2004;25:1701-11.
    • (2004) Int J Oncol , vol.25 , pp. 1701-1711
    • Louis, M.1    Rosato, R.R.2    Brault, L.3
  • 36
    • 2542616162 scopus 로고    scopus 로고
    • Synergistic effect of histone deacetylase inhibitors FK228 and m-carboxycinnamic acid bis-hydroxamide with proteasome inhibitors PSI and PS-341 against gastrointestinal adenocarcinoma cells
    • Adachi M, Zhang Y, Zhao X, et al. Synergistic effect of histone deacetylase inhibitors FK228 and m-carboxycinnamic acid bis-hydroxamide with proteasome inhibitors PSI and PS-341 against gastrointestinal adenocarcinoma cells. Clin Cancer Res 2004;10:3853-62.
    • (2004) Clin Cancer Res , vol.10 , pp. 3853-3862
    • Adachi, M.1    Zhang, Y.2    Zhao, X.3
  • 37
    • 30044434594 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor LAQ824 induces human leukemia cell death through a process involving XIAP down-regulation, oxidative injury, and the acid sphingomyelinase-dependent generation of ceramide
    • Rosato RR, Maggio SC, Almenara JA, et al. The histone deacetylase inhibitor LAQ824 induces human leukemia cell death through a process involving XIAP down-regulation, oxidative injury, and the acid sphingomyelinase-dependent generation of ceramide. Mol Pharmacol 2006;69:216-25.
    • (2006) Mol Pharmacol , vol.69 , pp. 216-225
    • Rosato, R.R.1    Maggio, S.C.2    Almenara, J.A.3
  • 38
    • 1542577586 scopus 로고    scopus 로고
    • + cells by histone deacetylase inhibitors involves reciprocal effects on the RAF/MEK/ERK and JNK pathways
    • + cells by histone deacetylase inhibitors involves reciprocal effects on the RAF/MEK/ERK and JNK pathways. Cancer Biol Ther 2003;2:544-51.
    • (2003) Cancer Biol Ther , vol.2 , pp. 544-551
    • Yu, C.1    Subler, M.2    Rahmani, M.3
  • 39
    • 34548067718 scopus 로고    scopus 로고
    • Thioredoxin signaling as a target for cancer therapy
    • Powis G, Kirkpatrick DL. Thioredoxin signaling as a target for cancer therapy. Curr Opin Pharmacol 2007;7:392-7.
    • (2007) Curr Opin Pharmacol , vol.7 , pp. 392-397
    • Powis, G.1    Kirkpatrick, D.L.2
  • 40
    • 0037015071 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin
    • Butler LM, Zhou X, Xu WS, et al. The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin. Proc Natl Acad Sci U S A 2002;99:11700-5.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11700-11705
    • Butler, L.M.1    Zhou, X.2    Xu, W.S.3
  • 41
    • 20044390016 scopus 로고    scopus 로고
    • Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors
    • Ungerstedt JS, Sowa Y, Xu WS, et al. Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors. Proc Natl Acad Sci U S A 2005;102:673-8.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 673-678
    • Ungerstedt, J.S.1    Sowa, Y.2    Xu, W.S.3
  • 42
    • 33750288048 scopus 로고    scopus 로고
    • Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor
    • Xu W, Ngo L, Perez G, et al. Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor. Proc Natl Acad Sci U S A 2006;103:15540-5.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15540-15545
    • Xu, W.1    Ngo, L.2    Perez, G.3
  • 43
    • 0030741385 scopus 로고    scopus 로고
    • Apoptotic death in adenocarcinoma cell lines induced by butyrate and other histone deacetylase inhibitors
    • McBain JA, Eastman A, Nobel CS, et al. Apoptotic death in adenocarcinoma cell lines induced by butyrate and other histone deacetylase inhibitors. Biochem Pharmacol 1997;53:1357-68.
    • (1997) Biochem Pharmacol , vol.53 , pp. 1357-1368
    • McBain, J.A.1    Eastman, A.2    Nobel, C.S.3
  • 44
    • 0030796349 scopus 로고    scopus 로고
    • Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): Dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway
    • Medina V, Edmonds B, Young GP, et al. Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway. Cancer Res 1997;57:3697-707.
    • (1997) Cancer Res , vol.57 , pp. 3697-3707
    • Medina, V.1    Edmonds, B.2    Young, G.P.3
  • 45
    • 0033199896 scopus 로고    scopus 로고
    • Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/CD95 ligand expression in human neuroblastoma
    • Glick RD, Swendeman SL, Coffey DC, et al. Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/CD95 ligand expression in human neuroblastoma. Cancer Res 1999;59:4392-9.
    • (1999) Cancer Res , vol.59 , pp. 4392-4399
    • Glick, R.D.1    Swendeman, S.L.2    Coffey, D.C.3
  • 46
    • 0032729215 scopus 로고    scopus 로고
    • Apoptosis induced by the histone deacetylase inhibitor sodium butyrate in human leukemic lymphoblasts
    • Bernhard D, Ausserlechner MJ, Tonko M, et al. Apoptosis induced by the histone deacetylase inhibitor sodium butyrate in human leukemic lymphoblasts. FASEB J 1999;13:1991-2001.
    • (1999) FASEB J , vol.13 , pp. 1991-2001
    • Bernhard, D.1    Ausserlechner, M.J.2    Tonko, M.3
  • 47
    • 0034665124 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, an inhibitor of histone deacetylase, suppresses the growth of prostate cancer cells in vitro and in vivo
    • Butler LM, Agus DB, Scher HI, et al. Suberoylanilide hydroxamic acid, an inhibitor of histone deacetylase, suppresses the growth of prostate cancer cells in vitro and in vivo. Cancer Res 2000;60:5165-70.
    • (2000) Cancer Res , vol.60 , pp. 5165-5170
    • Butler, L.M.1    Agus, D.B.2    Scher, H.I.3
  • 48
    • 0042090495 scopus 로고    scopus 로고
    • Novel mechanisms of apoptosis induced by histone deacetylase inhibitors
    • Peart MJ, Tainton KM, Ruefli AA, et al. Novel mechanisms of apoptosis induced by histone deacetylase inhibitors. Cancer Res 2003;63:4460-71.
    • (2003) Cancer Res , vol.63 , pp. 4460-4471
    • Peart, M.J.1    Tainton, K.M.2    Ruefli, A.A.3
  • 49
    • 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;101:4055-62.
    • (2003) Blood , vol.101 , pp. 4055-4062
    • Mitsiades, N.1    Mitsiades, C.S.2    Richardson, P.G.3
  • 50
    • 12444296582 scopus 로고    scopus 로고
    • Apoptosis on hepatoma cells but not on primary hepatocytes by histone deacetylase inhibitors valproate and ITF2357
    • Armeanu S, Pathil A, Venturelli S, et al. Apoptosis on hepatoma cells but not on primary hepatocytes by histone deacetylase inhibitors valproate and ITF2357. J Hepatol 2005;42:210-7.
    • (2005) J Hepatol , vol.42 , pp. 210-217
    • Armeanu, S.1    Pathil, A.2    Venturelli, S.3
  • 51
    • 33745258655 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor LBH589 is a potent antimyeloma agent that overcomes drug resistance
    • Maiso P, Carvajal-Vergara X, Ocio EM, et al. The histone deacetylase inhibitor LBH589 is a potent antimyeloma agent that overcomes drug resistance. Cancer Res 2006;66:5781-9.
    • (2006) Cancer Res , vol.66 , pp. 5781-5789
    • Maiso, P.1    Carvajal-Vergara, X.2    Ocio, E.M.3
  • 52
    • 34249941680 scopus 로고    scopus 로고
    • Analysis of the apoptotic and therapeutic activities of histone deacetylase inhibitors by using a mouse model of B cell lymphoma
    • Lindemann RK, Newbold A, Whitecross KF, et al. Analysis of the apoptotic and therapeutic activities of histone deacetylase inhibitors by using a mouse model of B cell lymphoma. Proc Natl Acad Sci U S A 2007;104:8071-6.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 8071-8076
    • Lindemann, R.K.1    Newbold, A.2    Whitecross, K.F.3
  • 53
    • 0038819943 scopus 로고    scopus 로고
    • Ineffectiveness of histone deacetylase inhibitors to induce apoptosis involves the transcriptional activation of NF-κB through the Akt pathway
    • Mayo MW, Denlinger CE, Broad RM, et al. Ineffectiveness of histone deacetylase inhibitors to induce apoptosis involves the transcriptional activation of NF-κB through the Akt pathway. J Biol Chem 2003;278:18980-9.
    • (2003) J Biol Chem , vol.278 , pp. 18980-18989
    • Mayo, M.W.1    Denlinger, C.E.2    Broad, R.M.3
  • 54
    • 3843103805 scopus 로고    scopus 로고
    • Combined histone deacetylase and NF-κB inhibition sensitizes non-small cell lung cancer to cell death
    • Rundall BK, Denlinger CE, Jones DR. Combined histone deacetylase and NF-κB inhibition sensitizes non-small cell lung cancer to cell death. Surgery 2004;136:416-25.
    • (2004) Surgery , vol.136 , pp. 416-425
    • Rundall, B.K.1    Denlinger, C.E.2    Jones, D.R.3
  • 55
    • 20744449274 scopus 로고    scopus 로고
    • Blockade of histone deacetylase inhibitor-induced RelA/p65 acetylation and NF-κB activation potentiates apoptosis in leukemia cells through a process mediated by oxidative damage, XIAP down-regulation, and c-Jun N-terminal kinase 1 activation
    • Dai Y, Rahmani M, Dent P, et al. Blockade of histone deacetylase inhibitor-induced RelA/p65 acetylation and NF-κB activation potentiates apoptosis in leukemia cells through a process mediated by oxidative damage, XIAP down-regulation, and c-Jun N-terminal kinase 1 activation. Mol Cell Biol 2005;25:5429-44.
    • (2005) Mol Cell Biol , vol.25 , pp. 5429-5444
    • Dai, Y.1    Rahmani, M.2    Dent, P.3
  • 56
    • 24744454815 scopus 로고    scopus 로고
    • The conflicting roles of the cdk inhibitor p21 (CIP1/WAF1) in apoptosis
    • Gartel AL. The conflicting roles of the cdk inhibitor p21 (CIP1/WAF1) in apoptosis. Leuk Res 2005;29:1237-8.
    • (2005) Leuk Res , vol.29 , pp. 1237-1238
    • Gartel, A.L.1
  • 57
    • 0038243113 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors activate p21 (WAF1) expression via ATM
    • Ju R, Muller MT. Histone deacetylase inhibitors activate p21 (WAF1) expression via ATM. Cancer Res 2003;63:2891-7.
    • (2003) Cancer Res , vol.63 , pp. 2891-2897
    • Ju, R.1    Muller, M.T.2
  • 58
    • 0033604457 scopus 로고    scopus 로고
    • Induction of apoptosis in U937 human leukemia cells by suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-XL, c -Jun, and p21CIP1, but independent of p53
    • Vrana JA, Decker RH, Johnson CR, et al. Induction of apoptosis in U937 human leukemia cells by suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-XL, c -Jun, and p21CIP1, but independent of p53. Oncogene 1999;18:7016-25.
    • (1999) Oncogene , vol.18 , pp. 7016-7025
    • Vrana, J.A.1    Decker, R.H.2    Johnson, C.R.3
  • 59
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon VM, Sandhoff TW, Rifkind RA, et al. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc Natl Acad Sci U S A 2000;97:10014-9.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3
  • 60
    • 25444440875 scopus 로고    scopus 로고
    • The role of autophagy in cancer development and response to therapy
    • Kondo Y, Kanzawa T, Sawaya R, et al. The role of autophagy in cancer development and response to therapy. Nat Rev Cancer 2005;5:726-34.
    • (2005) Nat Rev Cancer , vol.5 , pp. 726-734
    • Kondo, Y.1    Kanzawa, T.2    Sawaya, R.3
  • 61
    • 33645944960 scopus 로고    scopus 로고
    • Autophagy and cancer therapy
    • Kondo Y, Kondo S. Autophagy and cancer therapy. Autophagy 2006;2:85-90.
    • (2006) Autophagy , vol.2 , pp. 85-90
    • Kondo, Y.1    Kondo, S.2
  • 62
    • 33846794896 scopus 로고    scopus 로고
    • Autophagy inhibition enhances therapy-induced apoptosis in a Myc-induced model of lymphoma
    • Amaravadi RK, Yu D, Lum JJ, et al. Autophagy inhibition enhances therapy-induced apoptosis in a Myc-induced model of lymphoma. J Clin Invest 2007;117:326-36.
    • (2007) J Clin Invest , vol.117 , pp. 326-336
    • Amaravadi, R.K.1    Yu, D.2    Lum, J.J.3
  • 63
    • 11144221007 scopus 로고    scopus 로고
    • Apoptotic and autophagic cell death induced by histone deacetylase inhibitors
    • Shao Y, Gao Z, Marks PA, et al. Apoptotic and autophagic cell death induced by histone deacetylase inhibitors. Proc Natl Acad Sci U S A 2004;101:18030-5.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 18030-18035
    • Shao, Y.1    Gao, Z.2    Marks, P.A.3
  • 64
    • 34347394714 scopus 로고    scopus 로고
    • Targeting autophagy augments the anticancer activity of the 0histone deacetylase inhibitor SAHA to overcome Bcr-Abl-mediated drug resistance
    • Carew JS, Nawrocki ST, Kahue CN, et al. Targeting autophagy augments the anticancer activity of the 0histone deacetylase inhibitor SAHA to overcome Bcr-Abl-mediated drug resistance. Blood 2007;110:313-22.
    • (2007) Blood , vol.110 , pp. 313-322
    • Carew, J.S.1    Nawrocki, S.T.2    Kahue, C.N.3
  • 65
    • 30344433284 scopus 로고    scopus 로고
    • Synergistic antileukemic interactions between 2-medroxyestradiol (2-ME) and histone deacetylase inhibitors involve Akt down-regulation and oxidative stress
    • Gao N, Rahmani M, Shi X, et al. Synergistic antileukemic interactions between 2-medroxyestradiol (2-ME) and histone deacetylase inhibitors involve Akt down-regulation and oxidative stress. Blood 2006;107:241-9.
    • (2006) Blood , vol.107 , pp. 241-249
    • Gao, N.1    Rahmani, M.2    Shi, X.3
  • 66
    • 22344444291 scopus 로고    scopus 로고
    • Modulation of sensitivity to doxorubicin by the histone deacetylase inhibitor sodium butyrate in breast cancer cells
    • Louis M, Rosato RR, Battaglia E, et al. Modulation of sensitivity to doxorubicin by the histone deacetylase inhibitor sodium butyrate in breast cancer cells. Int J Oncol 2005;26:1569-74.
    • (2005) Int J Oncol , vol.26 , pp. 1569-1574
    • Louis, M.1    Rosato, R.R.2    Battaglia, E.3
  • 67
    • 2542523228 scopus 로고    scopus 로고
    • Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors
    • Pei XY, Dai Y, Grant S. Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors. Clin Cancer Res 2004;10:3839-52.
    • (2004) Clin Cancer Res , vol.10 , pp. 3839-3852
    • Pei, X.Y.1    Dai, Y.2    Grant, S.3
  • 68
    • 33750530675 scopus 로고    scopus 로고
    • Phase 1/2 study of the combination of 5-aza-2′-deoxycytidine with valproic acid in patients with leukemia
    • Garcia-Manero G, Kantarjian HM, Sanchez-Gonzalez B, et al. Phase 1/2 study of the combination of 5-aza-2′-deoxycytidine with valproic acid in patients with leukemia. Blood 2006;108:3271-9.
    • (2006) Blood , vol.108 , pp. 3271-3279
    • Garcia-Manero, G.1    Kantarjian, H.M.2    Sanchez-Gonzalez, B.3
  • 69
    • 33745714230 scopus 로고    scopus 로고
    • Combined DNA methyltransferase and histone deacetylase inhibition in the treatment of myeloid neoplasms
    • Gore SD, Baylin S, Sugar E, et al. Combined DNA methyltransferase and histone deacetylase inhibition in the treatment of myeloid neoplasms. Cancer Res 2006;66:6361-9.
    • (2006) Cancer Res , vol.66 , pp. 6361-6369
    • Gore, S.D.1    Baylin, S.2    Sugar, E.3


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