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Volumn 25, Issue 2, 2008, Pages 183-189

Histone deacetylases: Target enzymes for cancer therapy

Author keywords

Epigenetic regulation; Histone deacetylase; New cancer therapies

Indexed keywords

3 [(3 CHOLAMIDOPROPYL)DIMETHYLAMMONIO] 1 PROPANESULFONIC ACID; 3 CARBOXYCINNAMIC ACID DIHYDROXAMIDE; 3 PHENYLSULFAMOYLCINNAMOHYDROXAMIC ACID; 4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; 4 N ACETYLDINALINE; 6 (1,3 DIOXO 1H,3H BENZO[DE]ISOQUINOLIN 2 YL) N HYDROXYHEXANAMIDE; APICIDIN; ARYLBUTYRIC ACID DERIVATIVE; AZELAIC DIHYDROXAMIC ACID; BUTYRIC ACID; DEPSIPEPTIDE; HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 3; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID DERIVATIVE; KETONE DERIVATIVE; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; OXAMFLATIN; PANOBINOSTAT; PHENYLACETIC ACID; PYROXAMIDE; ROMIDEPSIN; SMALL INTERFERING RNA; SUBEROXYLANILIDE HYDROXAMIC ACID; TRAPOXIN; TRICHOSTATIN A; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALPROIC ACID;

EID: 41149141516     PISSN: 02620898     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10585-007-9131-5     Document Type: Review
Times cited : (150)

References (69)
  • 1
    • 78651162036 scopus 로고
    • Acetylation and Methylation of Histones and Their Possible Role in the Regulation of Rna Synthesis
    • Allfrey VG, Faulkner R, Mirsky AE (1964) Acetylation and Methylation of Histones and Their Possible Role in the Regulation of Rna Synthesis. Proc Natl Acad Sci USA 51:786-794
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 2
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • Glozak MA, Sengupta N, Zhang X, Seto E (2005) Acetylation and deacetylation of non-histone proteins. Gene 363:15-23
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 3
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton J, Hassig CA, Schreiber SL (1996) A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272:408-411
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 6
    • 0035862199 scopus 로고    scopus 로고
    • The human histone deacetylase family
    • Gray SG, Ekstrom TJ (2001) The human histone deacetylase family. Exp Cell Res 262:75-83
    • (2001) Exp Cell Res , vol.262 , pp. 75-83
    • Gray, S.G.1    Ekstrom, T.J.2
  • 7
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylases, transcriptional control, and cancer
    • Cress WD, Seto E (2000) Histone deacetylases, transcriptional control, and cancer. J Cell Physiol 184:1-16
    • (2000) J Cell Physiol , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 9
    • 0034252183 scopus 로고    scopus 로고
    • Histone acetylation modifiers in the pathogenesis of malignant disease
    • Mahlknecht U, Hoelzer D (2000) Histone acetylation modifiers in the pathogenesis of malignant disease. Mol Med 6:623-644
    • (2000) Mol Med , vol.6 , pp. 623-644
    • Mahlknecht, U.1    Hoelzer, D.2
  • 10
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • Lin RJ, Nagy L, Inoue S, Shao W, Miller WH Jr, Evans RM (1998) Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 391:811-814
    • (1998) Nature , vol.391 , pp. 811-814
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3    Shao, W.4    Miller Jr., W.H.5    Evans, R.M.6
  • 13
    • 0029693220 scopus 로고    scopus 로고
    • The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation
    • Van Lint C, Emiliani S, Verdin E (1996) The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expr 5:245-253
    • (1996) Gene Expr , vol.5 , pp. 245-253
    • Van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 14
    • 0035577768 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells
    • Munster PN, Troso-Sandoval T, Rosen N, Rifkind R, Marks PA, Richon VM (2001) The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells. Cancer Res 61:8492-8497
    • (2001) Cancer Res , vol.61 , pp. 8492-8497
    • Munster, P.N.1    Troso-Sandoval, T.2    Rosen, N.3    Rifkind, R.4    Marks, P.A.5    Richon, V.M.6
  • 15
    • 0034662614 scopus 로고    scopus 로고
    • Genetic reprogramming in pathways of colonic cell maturation induced by short chain fatty acids: Comparison with trichostatin A, sulindac, and curcumin and implications for chemoprevention of colon cancer
    • Mariadason JM, Corner GA, Augenlicht LH (2000) Genetic reprogramming in pathways of colonic cell maturation induced by short chain fatty acids: comparison with trichostatin A, sulindac, and curcumin and implications for chemoprevention of colon cancer. Cancer Res 60:4561-4572
    • (2000) Cancer Res , vol.60 , pp. 4561-4572
    • Mariadason, J.M.1    Corner, G.A.2    Augenlicht, L.H.3
  • 16
    • 0042905956 scopus 로고    scopus 로고
    • Gene expression profiling of multiple histone deacetylase (HDAC) inhibitors: Defining a common gene set produced by HDAC inhibition in T24 and MDA carcinoma cell lines
    • Glaser KB, Staver MJ, Waring JF, Stender J, Ulrich RG, Davidsen SK (2003) Gene expression profiling of multiple histone deacetylase (HDAC) inhibitors: defining a common gene set produced by HDAC inhibition in T24 and MDA carcinoma cell lines. Mol Cancer Ther 2:151-163
    • (2003) Mol Cancer Ther , vol.2 , pp. 151-163
    • Glaser, K.B.1    Staver, M.J.2    Waring, J.F.3    Stender, J.4    Ulrich, R.G.5    Davidsen, S.K.6
  • 18
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • Johnstone RW (2002) Histone-deacetylase inhibitors: novel drugs for the treatment of cancer. Nat Rev Drug Discov 1:287-299
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 20
    • 0028022785 scopus 로고
    • Induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines
    • Hoshikawa Y, Kwon HJ, Yoshida M, Horinouchi S, Beppu T, Trichostatin A (1994) induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines. Exp Cell Res 214:189-197
    • (1994) Exp Cell Res , vol.214 , pp. 189-197
    • Hoshikawa, Y.1    Kwon, H.J.2    Yoshida, M.3    Horinouchi, S.4    Beppu, T.5    Trichostatin, A.6
  • 23
    • 0034297220 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid as a potential therapeutic agent for human breast cancer treatment
    • Huang L, Pardee AB (2000) Suberoylanilide hydroxamic acid as a potential therapeutic agent for human breast cancer treatment. Mol Med 6:849-866
    • (2000) Mol Med , vol.6 , pp. 849-866
    • Huang, L.1    Pardee, A.B.2
  • 24
    • 33847372445 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor: Effects on gene expression and growth of glioma cells in vitro and in vivo
    • Yin D, Ong JM, Hu J, Desmond JC, Kawamata N, Konda BM, Black KL, Koeffler HP (2007) Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor: effects on gene expression and growth of glioma cells in vitro and in vivo. Clin Cancer Res 13:1045-1052
    • (2007) Clin Cancer Res , vol.13 , pp. 1045-1052
    • Yin, D.1    Ong, J.M.2    Hu, J.3    Desmond, J.C.4    Kawamata, N.5    Konda, B.M.6    Black, K.L.7    Koeffler, H.P.8
  • 25
    • 24044478600 scopus 로고    scopus 로고
    • P21Waf1/Cip1 is a common target induced by short-chain fatty acid HDAC inhibitors (valproic acid, tributyrin and sodium butyrate) in neuroblastoma cells
    • Rocchi P, Tonelli R, Camerin C, Purgato S, Fronza R, Bianucci F, Guerra F, Pession A, Ferreri AM (2005) p21Waf1/Cip1 is a common target induced by short-chain fatty acid HDAC inhibitors (valproic acid, tributyrin and sodium butyrate) in neuroblastoma cells. Oncol Rep 13:1139-1144
    • (2005) Oncol Rep , vol.13 , pp. 1139-1144
    • Rocchi, P.1    Tonelli, R.2    Camerin, C.3    Purgato, S.4    Fronza, R.5    Bianucci, F.6    Guerra, F.7    Pession, A.8    Ferreri, A.M.9
  • 27
    • 18644367141 scopus 로고    scopus 로고
    • Induction and superinduction of growth arrest and DNA damage gene 45 (GADD45) alpha and beta messenger RNAs by histone deacetylase inhibitors trichostatin a (TSA) and butyrate in SW620 human colon carcinoma cells
    • Chen Z, Clark S, Birkeland M, Sung CM, Lago A, Liu R, Kirkpatrick R, Johanson K, Winkler JD, Hu E (2002) Induction and superinduction of growth arrest and DNA damage gene 45 (GADD45) alpha and beta messenger RNAs by histone deacetylase inhibitors trichostatin A (TSA) and butyrate in SW620 human colon carcinoma cells. Cancer Lett 188:127-140
    • (2002) Cancer Lett , vol.188 , pp. 127-140
    • Chen, Z.1    Clark, S.2    Birkeland, M.3    Sung, C.M.4    Lago, A.5    Liu, R.6    Kirkpatrick, R.7    Johanson, K.8    Winkler, J.D.9    Hu, E.10
  • 28
    • 0344873745 scopus 로고    scopus 로고
    • P53-independent induction of Gadd45 by histone deacetylase inhibitor: Coordinate regulation by transcription factors Oct-1 and NF-Y
    • Hirose T, Sowa Y, Takahashi S, Saito S, Yasuda C, Shindo N, Furuichi K, Sakai T (2003) p53-independent induction of Gadd45 by histone deacetylase inhibitor: coordinate regulation by transcription factors Oct-1 and NF-Y. Oncogene 22:7762-7773
    • (2003) Oncogene , vol.22 , pp. 7762-7773
    • Hirose, T.1    Sowa, Y.2    Takahashi, S.3    Saito, S.4    Yasuda, C.5    Shindo, N.6    Furuichi, K.7    Sakai, T.8
  • 29
    • 0035837658 scopus 로고    scopus 로고
    • Paradoxical effects of trichostatin A: Inhibition of NF-Y-associated histone acetyltransferase activity, phosphorylation of hGCN5 and downregulation of cyclin a and B1 mRNA
    • Nair AR, Boersma LJ, Schiltz L, Chaudhry MA, Muschel RJ (2001) Paradoxical effects of trichostatin A: inhibition of NF-Y-associated histone acetyltransferase activity, phosphorylation of hGCN5 and downregulation of cyclin A and B1 mRNA. Cancer Lett 166:55-64
    • (2001) Cancer Lett , vol.166 , pp. 55-64
    • Nair, A.R.1    Boersma, L.J.2    Schiltz, L.3    Chaudhry, M.A.4    Muschel, R.J.5
  • 30
    • 0035023260 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors promote apoptosis and differential cell cycle arrest in anaplastic thyroid cancer cells
    • Greenberg VL, Williams JM, Cogswell JP, Mendenhall M, Zimmer SG (2001) Histone deacetylase inhibitors promote apoptosis and differential cell cycle arrest in anaplastic thyroid cancer cells. Thyroid 11:315-325
    • (2001) Thyroid , vol.11 , pp. 315-325
    • Greenberg, V.L.1    Williams, J.M.2    Cogswell, J.P.3    Mendenhall, M.4    Zimmer, S.G.5
  • 31
    • 0141570734 scopus 로고    scopus 로고
    • Functional interplay between modulation of histone deacetylase activity and its regulatory role in G2-M transition
    • Noh EJ, Lee JS (2003) Functional interplay between modulation of histone deacetylase activity and its regulatory role in G2-M transition. Biochem Biophys Res Commun 310:267-273
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 267-273
    • Noh, E.J.1    Lee, J.S.2
  • 32
    • 0033561497 scopus 로고    scopus 로고
    • Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase
    • Kim YB, Lee KH, Sugita K, Yoshida M, Horinouchi S (1999) Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase. Oncogene 18:2461-2470
    • (1999) Oncogene , vol.18 , pp. 2461-2470
    • Kim, Y.B.1    Lee, K.H.2    Sugita, K.3    Yoshida, M.4    Horinouchi, S.5
  • 34
    • 33644688961 scopus 로고    scopus 로고
    • Induction of apoptosis by trichostatin A, a histone deacetylase inhibitor, is associated with inhibition of cyclooxygenase-2 activity in human non-small cell lung cancer cells
    • Choi YH (2005) Induction of apoptosis by trichostatin A, a histone deacetylase inhibitor, is associated with inhibition of cyclooxygenase-2 activity in human non-small cell lung cancer cells. Int J Oncol 27:473-479
    • (2005) Int J Oncol , vol.27 , pp. 473-479
    • Choi, Y.H.1
  • 35
    • 33845352223 scopus 로고    scopus 로고
    • Bim plays a crucial role in synergistic induction of apoptosis by the histone deacetylase inhibitor SBHA and TRAIL in melanoma cells
    • Gillespie S, Borrow J, Zhang XD, Hersey P (2006) Bim plays a crucial role in synergistic induction of apoptosis by the histone deacetylase inhibitor SBHA and TRAIL in melanoma cells. Apoptosis 11:2251-2265
    • (2006) Apoptosis , vol.11 , pp. 2251-2265
    • Gillespie, S.1    Borrow, J.2    Zhang, X.D.3    Hersey, P.4
  • 36
    • 4444239987 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberic bishydroxamate regulates the expression of multiple apoptotic mediators and induces mitochondria-dependent apoptosis of melanoma cells
    • Zhang XD, Gillespie SK, Borrow JM, Hersey P (2004) The histone deacetylase inhibitor suberic bishydroxamate regulates the expression of multiple apoptotic mediators and induces mitochondria-dependent apoptosis of melanoma cells. Mol Cancer Ther 3:425-435
    • (2004) Mol Cancer Ther , vol.3 , pp. 425-435
    • Zhang, X.D.1    Gillespie, S.K.2    Borrow, J.M.3    Hersey, P.4
  • 39
    • 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, Payne SG, Atadja P, Spiegel S, Dent P, Grant S (2006) 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 69:216-225
    • (2006) Mol Pharmacol , vol.69 , pp. 216-225
    • Rosato, R.R.1    Maggio, S.C.2    Almenara, J.A.3    Payne, S.G.4    Atadja, P.5    Spiegel, S.6    Dent, P.7    Grant, S.8
  • 40
    • 0035184066 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor downregulation of bcl-xl gene expression leads to apoptotic cell death in mesothelioma
    • Cao XX, Mohuiddin I, Ece F, McConkey DJ, Smythe WR (2001) Histone deacetylase inhibitor downregulation of bcl-xl gene expression leads to apoptotic cell death in mesothelioma. Am J Respir Cell Mol Biol 25:562-568
    • (2001) Am J Respir Cell Mol Biol , vol.25 , pp. 562-568
    • Cao, X.X.1    Mohuiddin, I.2    Ece, F.3    McConkey, D.J.4    Smythe, W.R.5
  • 41
    • 4344716951 scopus 로고    scopus 로고
    • Modulation of pro- and anti-apoptotic factors in human melanoma cells exposed to histone deacetylase inhibitors
    • Facchetti F, Previdi S, Ballarini M, Minucci S, Perego P, La Porta CA (2004) Modulation of pro- and anti-apoptotic factors in human melanoma cells exposed to histone deacetylase inhibitors. Apoptosis 9:573-582
    • (2004) Apoptosis , vol.9 , pp. 573-582
    • Facchetti, F.1    Previdi, S.2    Ballarini, M.3    Minucci, S.4    Perego, P.5    La Porta, C.A.6
  • 42
    • 0038408486 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor up-regulates RECK to inhibit MMP-2 activation and cancer cell invasion.
    • Liu LT, Chang HC, Chiang LC, Hung WC (2003) Histone deacetylase inhibitor up-regulates RECK to inhibit MMP-2 activation and cancer cell invasion. Cancer Res 63:3069-3072
    • (2003) Cancer Res , vol.63 , pp. 3069-3072
    • Liu, L.T.1    Chang, H.C.2    Chiang, L.C.3    Hung, W.C.4
  • 43
    • 33846861339 scopus 로고    scopus 로고
    • Depsipeptide a histone deacetlyase inhibitor down regulates levels of matrix metalloproteinases 2 and 9 mRNA and protein expressions in lung cancer cells (A549)
    • Vinodhkumar R, Song YS, Ravikumar V, Ramakrishnan G, Devaki T (2007) Depsipeptide a histone deacetlyase inhibitor down regulates levels of matrix metalloproteinases 2 and 9 mRNA and protein expressions in lung cancer cells (A549). Chem Biol Interact 165:220-229
    • (2007) Chem Biol Interact , vol.165 , pp. 220-229
    • Vinodhkumar, R.1    Song, Y.S.2    Ravikumar, V.3    Ramakrishnan, G.4    Devaki, T.5
  • 44
    • 20544473454 scopus 로고    scopus 로고
    • Depsipeptide inhibits migration of primary and metastatic uveal melanoma cell lines in vitro: A potential strategy for uveal melanoma
    • Klisovic DD, Klisovic MI, Effron D, Liu S, Marcucci G, Katz SE (2005) Depsipeptide inhibits migration of primary and metastatic uveal melanoma cell lines in vitro: a potential strategy for uveal melanoma. Melanoma Res 15:147-153
    • (2005) Melanoma Res , vol.15 , pp. 147-153
    • Klisovic, D.D.1    Klisovic, M.I.2    Effron, D.3    Liu, S.4    Marcucci, G.5    Katz, S.E.6
  • 45
    • 4344685827 scopus 로고    scopus 로고
    • Expression profiling of sodium butyrate (NaB)-treated cells: Identification of regulation of genes related to cytokine signaling and cancer metastasis by NaB
    • Joseph J, Mudduluru G, Antony S, Vashistha S, Ajitkumar P, Somasundaram K (2004) Expression profiling of sodium butyrate (NaB)-treated cells: identification of regulation of genes related to cytokine signaling and cancer metastasis by NaB. Oncogene 23:6304-6315
    • (2004) Oncogene , vol.23 , pp. 6304-6315
    • Joseph, J.1    Mudduluru, G.2    Antony, S.3    Vashistha, S.4    Ajitkumar, P.5    Somasundaram, K.6
  • 46
    • 1842850710 scopus 로고    scopus 로고
    • Involvement of histone deacetylation in ras-induced down-regulation of the metastasis suppressor RECK
    • Chang HC, Liu LT, Hung WC (2004) Involvement of histone deacetylation in ras-induced down-regulation of the metastasis suppressor RECK. Cell Signal 16:675-679
    • (2004) Cell Signal , vol.16 , pp. 675-679
    • Chang, H.C.1    Liu, L.T.2    Hung, W.C.3
  • 49
    • 0037137896 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor FK228 inhibits tumor angiogenesis
    • Kwon HJ, Kim MS, Kim MJ, Nakajima H, Kim KW (2002) Histone deacetylase inhibitor FK228 inhibits tumor angiogenesis. Int J Cancer 97:290-296
    • (2002) Int J Cancer , vol.97 , pp. 290-296
    • Kwon, H.J.1    Kim, M.S.2    Kim, M.J.3    Nakajima, H.4    Kim, K.W.5
  • 51
    • 0037225763 scopus 로고    scopus 로고
    • Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1alpha activity
    • Mie Lee Y, Kim SH, Kim HS, Jin Son M, Nakajima H, Jeong Kwon H, Kim KW (2003) Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1alpha activity. Biochem Biophys Res Commun 300:241-246
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 241-246
    • Mie Lee, Y.1    Kim, S.H.2    Kim, H.S.3    Jin Son, M.4    Nakajima, H.5    Jeong Kwon, H.6    Kim, K.W.7
  • 53
    • 4644364508 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584
    • Qian DZ, Wang X, Kachhap SK, Kato Y, Wei Y, Zhang L, Atadja P, Pili R (2004) The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584. Cancer Res 64:6626-6634
    • (2004) Cancer Res , vol.64 , pp. 6626-6634
    • Qian, D.Z.1    Wang, X.2    Kachhap, S.K.3    Kato, Y.4    Wei, Y.5    Zhang, L.6    Atadja, P.7    Pili, R.8
  • 54
    • 0042261694 scopus 로고    scopus 로고
    • Antitumor efficacy of FK228, a novel histone deacetylase inhibitor, depends on the effect on expression of angiogenesis factors
    • Sasakawa Y, Naoe Y, Noto T, Inoue T, Sasakawa T, Matsuo M, Manda T, Mutoh S (2003) Antitumor efficacy of FK228, a novel histone deacetylase inhibitor, depends on the effect on expression of angiogenesis factors. Biochem Pharmacol 66:897-906
    • (2003) Biochem Pharmacol , vol.66 , pp. 897-906
    • Sasakawa, Y.1    Naoe, Y.2    Noto, T.3    Inoue, T.4    Sasakawa, T.5    Matsuo, M.6    Manda, T.7    Mutoh, S.8
  • 56
    • 21644485961 scopus 로고    scopus 로고
    • The expression of endothelial nitric-oxide synthase is controlled by a cell-specific histone code
    • Fish JE, Matouk CC, Rachlis A, Lin S, Tai SC, D'Abreo C, Marsden PA (2005) The expression of endothelial nitric-oxide synthase is controlled by a cell-specific histone code. J Biol Chem 280:24824-24838
    • (2005) J Biol Chem , vol.280 , pp. 24824-24838
    • Fish, J.E.1    Matouk, C.C.2    Rachlis, A.3    Lin, S.4    Tai, S.C.5    D'Abreo, C.6    Marsden, P.A.7
  • 58
    • 0036842460 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis
    • Rossig L, Li H, Fisslthaler B, Urbich C, Fleming I, Forstermann U, Zeiher AM, Dimmeler S (2002) Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis. Circ Res 91:837-844
    • (2002) Circ Res , vol.91 , pp. 837-844
    • Rossig, L.1    Li, H.2    Fisslthaler, B.3    Urbich, C.4    Fleming, I.5    Forstermann, U.6    Zeiher, A.M.7    Dimmeler, S.8
  • 59
    • 2942724589 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Development as cancer therapy
    • discussion 281-268
    • Marks PA, Richon VM, Kelly WK, Chiao JH, Miller T (2004) Histone deacetylase inhibitors: development as cancer therapy. Novartis Found Symp 259:269-281 discussion 281-268
    • (2004) Novartis Found Symp , vol.259 , pp. 269-281
    • Marks, P.A.1    Richon, V.M.2    Kelly, W.K.3    Chiao, J.H.4    Miller, T.5
  • 60
    • 20444479514 scopus 로고    scopus 로고
    • Drug insight: Histone deacetylase inhibitors-development of the new targeted anticancer agent suberoylanilide hydroxamic acid
    • Kelly WK, Marks PA (2005) Drug insight: Histone deacetylase inhibitors-development of the new targeted anticancer agent suberoylanilide hydroxamic acid. Nat Clin Pract Oncol 2:150-157
    • (2005) Nat Clin Pract Oncol , vol.2 , pp. 150-157
    • Kelly, W.K.1    Marks, P.A.2
  • 61
    • 0036906832 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: From target to clinical trials
    • Kelly WK, O'Connor OA, Marks PA (2002) Histone deacetylase inhibitors: from target to clinical trials. Expert Opin Investig Drugs 11:1695-1713
    • (2002) Expert Opin Investig Drugs , vol.11 , pp. 1695-1713
    • Kelly, W.K.1    O'Connor, O.A.2    Marks, P.A.3
  • 63
    • 33644696512 scopus 로고    scopus 로고
    • Chemical ablation of androgen receptor in prostate cancer cells by the histone deacetylase inhibitor LAQ824
    • Chen L, Meng S, Wang H, Bali P, Bai W, Li B, Atadja P, Bhalla KN, Wu J (2005) Chemical ablation of androgen receptor in prostate cancer cells by the histone deacetylase inhibitor LAQ824. Mol Cancer Ther 4:1311-1319
    • (2005) Mol Cancer Ther , vol.4 , pp. 1311-1319
    • Chen, L.1    Meng, S.2    Wang, H.3    Bali, P.4    Bai, W.5    Li, B.6    Atadja, P.7    Bhalla, K.N.8    Wu, J.9
  • 64
    • 34548075217 scopus 로고    scopus 로고
    • Hydroxamic acid analogue histone deacetylase inhibitors attenuate estrogen receptor-alpha levels and transcriptional activity: A result of hyperacetylation and inhibition of chaperone function of heat shock protein 90
    • Fiskus W, Ren Y, Mohapatra A, Bali P, Mandawat A, Rao R, Herger B, Yang Y, Atadja P, Wu J, Bhalla K (2007) Hydroxamic acid analogue histone deacetylase inhibitors attenuate estrogen receptor-alpha levels and transcriptional activity: a result of hyperacetylation and inhibition of chaperone function of heat shock protein 90. Clin Cancer Res 13:4882-4890
    • (2007) Clin Cancer Res , vol.13 , pp. 4882-4890
    • Fiskus, W.1    Ren, Y.2    Mohapatra, A.3    Bali, P.4    Mandawat, A.5    Rao, R.6    Herger, B.7    Yang, Y.8    Atadja, P.9    Wu, J.10    Bhalla, K.11
  • 65
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P, Pranpat M, Bradner J, Balasis M, Fiskus W, Guo F, Rocha K, Kumaraswamy S, Boyapalle S, Atadja P, Seto E, Bhalla K (2005) Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J Biol Chem 280:26729-26734
    • (2005) J Biol Chem , vol.280 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3    Balasis, M.4    Fiskus, W.5    Guo, F.6    Rocha, K.7    Kumaraswamy, S.8    Boyapalle, S.9    Atadja, P.10    Seto, E.11    Bhalla, K.12
  • 67
    • 0036161439 scopus 로고    scopus 로고
    • Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR
    • Fischle W, Dequiedt F, Hendzel MJ, Guenther MG, Lazar MA, Voelter W, Verdin E (2002) Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR. Mol Cell 9:45-57
    • (2002) Mol Cell , vol.9 , pp. 45-57
    • Fischle, W.1    Dequiedt, F.2    Hendzel, M.J.3    Guenther, M.G.4    Lazar, M.A.5    Voelter, W.6    Verdin, E.7
  • 69
    • 33746228132 scopus 로고    scopus 로고
    • Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10
    • Chang S, Young BD, Li S, Qi X, Richardson JA, Olson EN (2006) Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10. Cell 126:321-334
    • (2006) Cell , vol.126 , pp. 321-334
    • Chang, S.1    Young, B.D.2    Li, S.3    Qi, X.4    Richardson, J.A.5    Olson, E.N.6


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