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Volumn 31, Issue SUPPL. 1, 2012, Pages

Understanding histone deacetylases in the cancer development and treatment: An epigenetic perspective of cancer chemotherapy

Author keywords

[No Author keywords available]

Indexed keywords

4 PHENYLBUTYRIC ACID; BELINOSTAT; DACINOSTAT; ENTINOSTAT; GIVINOSTAT; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; PANOBINOSTAT; PIVALOYLOXYMETHYL BUTYRATE; ROMIDEPSIN; TRICHOSTATIN A; VALPROIC ACID; VORINOSTAT;

EID: 84866550710     PISSN: 10445498     EISSN: 15577430     Source Type: Journal    
DOI: 10.1089/dna.2011.1575     Document Type: Review
Times cited : (31)

References (49)
  • 1
    • 37349061341 scopus 로고    scopus 로고
    • A natural histone deacetylase inhibitor, Psammaplin A, induces cell cycle arrest and apoptosis in human endometrial cancer cells
    • DOI 10.1016/j.ygyno.2007.08.098, PII S0090825807007135
    • Ahn, M.Y., Jung, J.H., Na, Y.J., and Kim, H.S. (2008). A natural histone deacetylase inhibitor, Psammaplin, A., induces cell cycle arrest and apoptosis in human endometrial cancer cells. Gynecol Oncol 108, 27-33. (Pubitemid 350299431)
    • (2008) Gynecologic Oncology , vol.108 , Issue.1 , pp. 27-33
    • Ahn, M.Y.1    Jung, J.H.2    Na, Y.J.3    Kim, H.S.4
  • 2
    • 79960356610 scopus 로고    scopus 로고
    • Romidepsin: A novel histone deacetylase inhibitor for cancer
    • Bertino, E.M., and Otterson, G.A. (2011). Romidepsin: a novel histone deacetylase inhibitor for cancer. Expert Opin Investig Drugs 20, 1151-1158.
    • (2011) Expert Opin Investig Drugs , vol.20 , pp. 1151-1158
    • Bertino, E.M.1    Otterson, G.A.2
  • 3
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • DOI 10.1038/nrd2133, PII NRD2133
    • Bolden, J.E., Peart, M.J., and Johnstone, R.W. (2006). Anticancer activities of histone deacetylase inhibitors. Nat Rev Drug Discov 5, 769-784. (Pubitemid 44348499)
    • (2006) Nature Reviews Drug Discovery , vol.5 , Issue.9 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 4
    • 77249087051 scopus 로고    scopus 로고
    • Chemical phylogenetics of histone deacetylases
    • Bradner, J.E., West, N., Grachan M.L., et al. (2010). Chemical phylogenetics of histone deacetylases. Nat Chem Biol 6, 238-243.
    • (2010) Nat Chem Biol , vol.6 , pp. 238-243
    • Bradner, J.E.1    West, N.2    Grachan, M.L.3
  • 5
    • 4544358659 scopus 로고    scopus 로고
    • Histone deacetylases 5 and 9 govern responsiveness of the heart to a subset of stress signals and play redundant roles in heart development
    • DOI 10.1128/MCB.24.19.8467-8476.2004
    • Chang, S., McKinsey, T.A., Zhang, C.L., Richardson, J.A., Hill, J.A., and Olson, E.N. (2004). Histone deacetylases 5 and 9 govern responsiveness of the heart to a subset of stress signals and play redundant roles in heart development. Mol Cell Biol 24, 8467-8476. (Pubitemid 39245069)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.19 , pp. 8467-8476
    • Chang, S.1    McKinsey, T.A.2    Zhang, C.L.3    Richardson, J.A.4    Hill, J.A.5    Olson, E.N.6
  • 8
    • 34548456881 scopus 로고    scopus 로고
    • Dietary histone deacetylase inhibitors: From cells to mice to man
    • DOI 10.1016/j.semcancer.2007.04.001, PII S1044579X07000247
    • Dashwood, R.H., and Ho E. (2007). Dietary histone deacetylase inhibitors: from cells to mice to man. Semin Cancer Biol 17, 363-369. (Pubitemid 47369168)
    • (2007) Seminars in Cancer Biology , vol.17 , Issue.5 , pp. 363-369
    • Dashwood, R.H.1    Ho, E.2
  • 9
    • 77953292595 scopus 로고    scopus 로고
    • Post-translational modifications in signal integration
    • Deribe, Y.L., Pawson, T., and Dikic I. (2010). Post-translational modifications in signal integration. Nat Struct Mol Biol 17, 666-672.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 666-672
    • Deribe, Y.L.1    Pawson, T.2    Dikic, I.3
  • 10
    • 36048958965 scopus 로고    scopus 로고
    • HDAC Inhibitors: Overview and perspectives
    • Dokmanovic, M., Clarke, C., and Marks, P.A. (2007). HDAC Inhibitors: Overview and perspectives. Mol Cancer Res 5, 981-989.
    • (2007) Mol Cancer Res , vol.5 , pp. 981-989
    • Dokmanovic, M.1    Clarke, C.2    Marks, P.A.3
  • 11
    • 33845209109 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and paclitaxel cause synergistic effects on apoptosis and microtubule stabilization in papillary serous endometrial cancer cells
    • DOI 10.1158/1535-7163.MCT-06-0209
    • Dowdy, S.C., Jiang, S., Zhou, X.C., Hou, X., Jin, F., Podratz, K.C., and Jiang, S.W. (2006). Histone deacetylase inhibitors and paclitaxel cause synergistic effects on apoptosis and microtubule stabilization in papillary serous endometrial cancer cells. Mol Cancer Ther 5, 2767-2776. (Pubitemid 44849003)
    • (2006) Molecular Cancer Therapeutics , vol.5 , Issue.11 , pp. 2767-2776
    • Dowdy, S.C.1    Jiang, S.2    Zhou, X.C.3    Hou, X.4    Jin, F.5    Podratz, K.C.6    Jiang, S.-W.7
  • 13
    • 40849139208 scopus 로고    scopus 로고
    • Epigenetics in cancer
    • Esteller, M. (2008). Epigenetics in cancer. N Eng J Med 358, 1148-1159.
    • (2008) N Eng J Med , vol.358 , pp. 1148-1159
    • Esteller, M.1
  • 14
    • 0037067696 scopus 로고    scopus 로고
    • Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family
    • DOI 10.1074/jbc.M111871200
    • Gao, L., Cueto, M.A., Asselbergs, F., and Atadja, P. (2002). Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J Biol Chem 277, 25748-25755. (Pubitemid 34951896)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25748-25755
    • Gao, L.1    Cueto, M.A.2    Asselbergs, F.3    Atadja, P.4
  • 15
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • DOI 10.1016/j.gene.2005.09.010, PII S037811190500572X
    • Glozak, M.A., Sengupta, N., Zhang, X., and Seto E. (2005). Acetylation and deacetylation of non-histone proteins. Gene 363, 15-23. (Pubitemid 41691888)
    • (2005) Gene , vol.363 , Issue.1-2 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 16
    • 0033571273 scopus 로고    scopus 로고
    • Chromatin remodelling at the PHO8 promoter requires SWI-SNF and SAGA at a step subsequent to activator binding
    • DOI 10.1093/emboj/18.22.6407
    • Gregory, P.D., Schmid, A., Zavari, M., Munsterkotter, M., and Horz W. (1999). Chromatin remodelling at the PHO8 promoter requires SWI-SNF and SAGA at a step subsequent to activator binding. EMBO J 18, 6407-6414. (Pubitemid 29533244)
    • (1999) EMBO Journal , vol.18 , Issue.22 , pp. 6407-6414
    • Gregory, P.D.1    Schmid, A.2    Zavari, M.3    Munsterkotter, M.4    Horz, W.5
  • 17
    • 0036479127 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel histone deacetylase HDAC10
    • DOI 10.1074/jbc.M109861200
    • Guardiola, A.R., and Yao, T.P. (2002). Molecular cloning and characterization of a novel histone deacetylase HDAC10. J Biol Chem 277, 3350-3356. (Pubitemid 34953202)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3350-3356
    • Guardiola, A.R.1    Yao, T.-P.2
  • 18
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
    • Haberland, M., Montgomery, R.L., and Olson, E.N. (2009). The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat Rev Genet 10, 32-42.
    • (2009) Nat Rev Genet , vol.10 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 19
    • 28544449926 scopus 로고    scopus 로고
    • Nucleosome stability at the yeast PHO5 and PHO8 promoters correlates with differential cofactor requirements for chromatin opening
    • DOI 10.1128/MCB.25.24.10755-10767.2005
    • Hertel, C.B., Langst, G., Hö rz, W., and Korber P. (2005). Nucleosome stability at the yeast PHO5 and PHO8 promoters correlates with differential cofactor requirements for chromatin opening. Mol Cell Biol 25, 10755-10767. (Pubitemid 41747121)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.24 , pp. 10755-10767
    • Hertel, C.B.1    Langst, G.2    Horz, W.3    Korber, P.4
  • 20
    • 0034717183 scopus 로고    scopus 로고
    • Tandem bromodomains in the chromatin remodeler RSC recognize acetylated histone H3 Lys14
    • Jacobson, R.H., Ladurner, A.G., King, D.S., and Tjian R. (2000). Tandem bromodomains in the chromatin remodeler RSC recognize acetylated histone H3 Lys14. Science 288, 1422-1425.
    • (2000) Science , vol.288 , pp. 1422-1425
    • Jacobson, R.H.1    Ladurner, A.G.2    King, D.S.3    Tjian, R.4
  • 21
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • DOI 10.1016/j.cell.2007.01.029, PII S0092867407001274
    • Jones, P.A., and Baylin, S.B. (2007). The epigenomics of cancer. Cell 128, 683-692. (Pubitemid 46273572)
    • (2007) Cell , vol.128 , Issue.4 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 24
    • 0033561497 scopus 로고    scopus 로고
    • Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase
    • DOI 10.1038/sj.onc.1202564
    • Kim, Y.B., Lee, K.H., Sugita, K., and Yoshida, M., Horinouchi S. (1999). Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase. Oncogene 18, 2461-2470. (Pubitemid 29206159)
    • (1999) Oncogene , vol.18 , Issue.15 , pp. 2461-2470
    • Kim, Y.B.1    Lee, K.-H.2    Sugita, K.3    Yoshida, M.4    Horinouchi, S.5
  • 25
    • 0141996376 scopus 로고    scopus 로고
    • Modulation of histone acetylation by [4-(acetylamino)-N-(2-amino-phenyl) benzamide] in HCT-8 colon carcinoma
    • Kraker, A.J., Mizzen, C.A., Hartl, B.G., Miin, J., Allis, C.D., and Merriman R.L. (2003). Modulation of histone acetylation by [4-(acetylamino)-N- (2-amino-phenyl) benzamide] in HCT-8 colon carcinoma. Mol Cancer Ther 2, 401-408.
    • (2003) Mol Cancer Ther , vol.2 , pp. 401-408
    • Kraker, A.J.1    Mizzen, C.A.2    Hartl, B.G.3    Miin, J.4    Allis, C.D.5    Merriman, R.L.6
  • 26
    • 4444309863 scopus 로고    scopus 로고
    • Treatment of myelodysplastic syndromes with valproic acid alone or in combination with all-trans retinoic acid
    • DOI 10.1182/blood-2003-12-4333
    • Kuendgen, A., Strupp, C., Aivado, M., et al. (2004). Treatment of myelodysplastic syndromes with valproic acid alone or in combination with all-trans retinoic acid. Blood 104, 1266-1269. (Pubitemid 39166498)
    • (2004) Blood , vol.104 , Issue.5 , pp. 1266-1269
    • Kuendgen, A.1    Strupp, C.2    Aivado, M.3    Bernhardt, A.4    Hildebrandt, B.5    Haas, R.6    Germing, U.7    Gattermann, N.8
  • 27
  • 29
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • DOI 10.1038/38444
    • Luger, K., Mader, A.W., Richmond, R.K., Sargent, D.F., and Richmond, T.J. (1997). Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389, 251-260. (Pubitemid 27406632)
    • (1997) Nature , vol.389 , Issue.6648 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 30
    • 64249135764 scopus 로고    scopus 로고
    • Novel agents on the horizon for cancer therapy
    • Ma, W.W., and Adjei, A.A. (2010). Novel agents on the horizon for cancer therapy. CA Cancer J Clin 59, 111-137.
    • (2010) CA Cancer J Clin , vol.59 , pp. 111-137
    • Ma, W.W.1    Adjei, A.A.2
  • 31
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • DOI 10.1038/nrc1779
    • Minucci, S., and Pelicci, P.G. (2006). Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 6, 38-51. (Pubitemid 43054973)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.1 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 32
    • 33645825587 scopus 로고    scopus 로고
    • min mice
    • DOI 10.1096/fj.05-4785fje
    • Myzak, M.C., Dashwood, W.M., Orner, G.A., Ho, E., and Dashwood, R.H. (2006). Sulforaphane inhibits histone deacetylase in vivo and suppresses tumorigenesis in Apcmin mice. FASEB J 20, 506-508. (Pubitemid 46671231)
    • (2006) FASEB Journal , vol.20 , Issue.3 , pp. 506-508
    • Myzak, M.C.1    Dashwood, W.M.2    Orner, G.A.3    Ho, E.4    Dashwood, R.H.5
  • 33
    • 4143130097 scopus 로고    scopus 로고
    • A novel mechanism of chemoprotection by sulforaphane: Inhibition of histone deacetylase
    • DOI 10.1158/0008-5472.CAN-04-1326
    • Myzak, M.C., Karplus, P.A., Chung, F.L., and Dashwood, R.H. (2004). A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. Cancer Res 64, 5767-5774. (Pubitemid 39095576)
    • (2004) Cancer Research , vol.64 , Issue.16 , pp. 5767-5774
    • Myzak, M.C.1    Karplus, P.A.2    Chung, F.-L.3    Dashwood, R.H.4
  • 34
    • 63049105405 scopus 로고    scopus 로고
    • Modulation of histone deacetylase activity by dietary isothiocynates and allyl sulfides: Studies with sulforaphane and garlic organosulfur compounds
    • Nian, H., Delage, B., Ho, E., and Dashwood, R.H. (2009). Modulation of histone deacetylase activity by dietary isothiocynates and allyl sulfides: studies with sulforaphane and garlic organosulfur compounds. Environ Mol Mutagen 50, 213-221.
    • (2009) Environ Mol Mutagen , vol.50 , pp. 213-221
    • Nian, H.1    Delage, B.2    Ho, E.3    Dashwood, R.H.4
  • 35
    • 4544322261 scopus 로고    scopus 로고
    • Reduced expression of class II histone deacetylase genes is associated with poor prognosis in lung cancer patients
    • DOI 10.1002/ijc.20395
    • Osada, H., Tatematsu, Y., Saito, H., Yatabe, Y., Mitsudomi, T., and Takahash, T. (2004). Reduced expression of class II histone deacetylase genes is associated with poor prognosis in lung cancer patients. Int J Cancer 112, 26-32. (Pubitemid 39249488)
    • (2004) International Journal of Cancer , vol.112 , Issue.1 , pp. 26-32
    • Osada, H.1    Tatematsu, Y.2    Saito, H.3    Yatabe, Y.4    Mitsudomi, T.5    Takahashi, T.6
  • 37
    • 1542297718 scopus 로고    scopus 로고
    • In vitro acetylation of hmgb-1 and -2 proteins by CBP: The role of the acidic tail
    • DOI 10.1021/bi035615y
    • Pasheva, E., Sarov, M., Bidjekov K, et al. (2004). In vitro acetylation of HMGB-1 and-2 proteins by CBP: the role of the acidic tail. Biochemistry 43, 2935-2940. (Pubitemid 38327825)
    • (2004) Biochemistry , vol.43 , Issue.10 , pp. 2935-2940
    • Pasheva, E.1    Sarov, M.2    Bidjekov, K.3    Ugrinova, I.4    Sarg, B.5    Lindner, H.6    Pashev, I.G.7
  • 39
    • 3042785975 scopus 로고    scopus 로고
    • A review of depsipeptide and other histone deacetylase inhibitors in clinical trials
    • DOI 10.2174/1381612043383980
    • Piekarz, R., and Bates S. (2004). A review of depsipeptide and other histone deacetylase inhibitors in clinical trials. Curr Pharm Design 10, 2289-2298. (Pubitemid 38855037)
    • (2004) Current Pharmaceutical Design , vol.10 , Issue.19 , pp. 2289-2298
    • Piekarz, R.1    Bates, S.2
  • 40
    • 0035866341 scopus 로고    scopus 로고
    • Combination of phenylbutyrate and 13-cis retinoic acid inhibits prostate tumor growth and angiogenesis
    • Pili, R., Kruszewski, M.P., Hager, B.W., Lantz, J., and Carducci MA. (2001). Combination of phenylbutyrate and 13-cis retinoic acid inhibits prostate tumor growth and angiogenesis. Cancer Res 61, 1477-1485. (Pubitemid 34292576)
    • (2001) Cancer Research , vol.61 , Issue.4 , pp. 1477-1485
    • Pili, R.1    Kruszewski, M.P.2    Hager, B.W.3    Lantz, J.4    Carducci, M.A.5
  • 42
    • 0033945861 scopus 로고    scopus 로고
    • DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci
    • DOI 10.1038/77023
    • Rountree, M.R., Bachman, K.E., and Baylin, S.B. (2000). DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. Nat Genet 25, 269-277. (Pubitemid 30437311)
    • (2000) Nature Genetics , vol.25 , Issue.3 , pp. 269-277
    • Rountree, M.R.1    Bachman, K.E.2    Baylin, S.B.3
  • 43
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C.A., and Schreiber, S.L. (1996). A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272, 408-411. (Pubitemid 26138177)
    • (1996) Science , vol.272 , Issue.5260 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 45
    • 38949086502 scopus 로고    scopus 로고
    • Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy
    • DOI 10.1038/sj.bjc.6604199, PII 6604199
    • Weichert, W., Roske1, A., Gekeler, V., Beckers, T., Stephan, C., Jung, K., Fritzsche, F.R., Niesporek, S., Denkert, C., Dietel, M., and Kristiansen, G. (2008). Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy. Br J Cancer 98, 604-610. (Pubitemid 351214528)
    • (2008) British Journal of Cancer , vol.98 , Issue.3 , pp. 604-610
    • Weichert, W.1    Roske, A.2    Gekeler, V.3    Beckers, T.4    Stephan, C.5    Jung, K.6    Fritzsche, F.R.7    Niesporek, S.8    Denkert, C.9    Dietel, M.10    Kristiansen, G.11
  • 47
    • 61849144810 scopus 로고    scopus 로고
    • HDAC family: What are the cancer relevant targets?
    • Witt, O., Deubzer, H.E., Milde, T., and Oehme, I. (2009). HDAC family: what are the cancer relevant targets? Cancer Lett 277, 8-21.
    • (2009) Cancer Lett , vol.277 , pp. 8-21
    • Witt, O.1    Deubzer, H.E.2    Milde, T.3    Oehme, I.4
  • 48
    • 77749246186 scopus 로고    scopus 로고
    • Biochemical Profiling of Histone Binding Selectivity of the Yeast Bromodomain family
    • Zhang, Q., Chakravarty, S., Ghersi, D., Zeng, L., Plotnikov, A.N., and Sanchez, R. (2010). Biochemical Profiling of Histone Binding Selectivity of the Yeast Bromodomain family. PLoS One 5, 1.
    • (2010) PLoS One , vol.5 , pp. 1
    • Zhang, Q.1    Chakravarty, S.2    Ghersi, D.3    Zeng, L.4    Plotnikov, A.N.5    Sanchez, R.6


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