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Volumn 13, Issue 4, 2013, Pages 640-647

Immunomodulatory effects of histone deacetylase inhibitors

Author keywords

Chromatin modifications; HDAC11; Histone acetylation; Histone deacetylase inhibitor; Immune system; Immunomodulation; Trichostatin a

Indexed keywords

4 PHENYLBUTYRIC ACID; BUTYRIC ACID; DACINOSTAT; DEPSIPEPTIDE; DOXORUBICIN; ENTINOSTAT; GIVINOSTAT; HISTONE DEACETYLASE INHIBITOR; LIXIVAPTAN; MOCETINOSTAT; PANOBINOSTAT; ROMIDEPSIN; TACEDINALINE; TRICHOSTATIN A; VALPROIC ACID; VORINOSTAT;

EID: 84876719154     PISSN: 15665240     EISSN: 18755666     Source Type: Journal    
DOI: 10.2174/1566524011313040013     Document Type: Review
Times cited : (39)

References (97)
  • 1
    • 79959521749 scopus 로고    scopus 로고
    • The redox basis of epigenetic modifications: From mechanisms to functional consequences
    • Cyr AR, Domann FE. The redox basis of epigenetic modifications: from mechanisms to functional consequences. Antioxid Redox Signal 2011; 15: 551-589.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 551-589
    • Cyr, A.R.1    Domann, F.E.2
  • 2
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo MH, Allis CD. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 1998; 20: 615-626.
    • (1998) Bioessays , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 5
    • 59349115177 scopus 로고    scopus 로고
    • Chemical mechanisms of histone lysine and arginine modifications
    • Smith BC, Denu JM. Chemical mechanisms of histone lysine and arginine modifications. Biochim Biophys Acta 2009; 1789: 45-57.
    • (2009) Biochim Biophys Acta , vol.1789 , pp. 45-57
    • Smith, B.C.1    Denu, J.M.2
  • 6
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 2007; 128: 693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 8
    • 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
  • 9
    • 78649905409 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: A chemical genetics approach to understanding cellular functions
    • Marks PA. Histone deacetylase inhibitors: a chemical genetics approach to understanding cellular functions. Biochim Biophys Acta 2010; 1799: 717-725.
    • (2010) Biochim Biophys Acta , vol.1799 , pp. 717-725
    • Marks, P.A.1
  • 10
    • 67650090545 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Potential in cancer therapy
    • Marks PA, Xu WS. Histone deacetylase inhibitors: Potential in cancer therapy. J Cell Biochem 2009; 107: 600-608.
    • (2009) J Cell Biochem , vol.107 , pp. 600-608
    • Marks, P.A.1    Xu, W.S.2
  • 11
    • 0034687694 scopus 로고    scopus 로고
    • Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP- ribose
    • Tanner KG, Landry J, Sternglanz R, Denu JM. Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP- ribose. Proc Natl Acad Sci USA 2000; 97: 14178-14182.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14178-14182
    • Tanner, K.G.1    Landry, J.2    Sternglanz, R.3    Denu, J.M.4
  • 12
    • 33646548638 scopus 로고    scopus 로고
    • Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion
    • Gantt SL, Gattis SG, Fierke CA. Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion. Biochemistry 2006; 45: 6170-6178.
    • (2006) Biochemistry , vol.45 , pp. 6170-6178
    • Gantt, S.L.1    Gattis, S.G.2    Fierke, C.A.3
  • 13
    • 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
  • 14
  • 15
    • 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
  • 16
    • 34547919621 scopus 로고    scopus 로고
    • Class IIa histone deacetylases: Regulating the regulators
    • Martin M, Kettmann R, Dequiedt F. Class IIa histone deacetylases: regulating the regulators. Oncogene 2007; 26: 5450-5467.
    • (2007) Oncogene , vol.26 , pp. 5450-5467
    • Martin, M.1    Kettmann, R.2    Dequiedt, F.3
  • 17
    • 61849144810 scopus 로고    scopus 로고
    • HDAC family: What are the cancer relevant targets?
    • Witt O, Deubzer HE, Milde T, Oehme I. HDAC family: What are the cancer relevant targets? Cancer Lett 2009; 277: 8-21.
    • (2009) Cancer Lett , vol.277 , pp. 8-21
    • Witt, O.1    Deubzer, H.E.2    Milde, T.3    Oehme, I.4
  • 18
    • 70649108817 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and neurodegenerative disorders: Holding the promise
    • Mai A, Rotili D, Valente S, Kazantsev AG. Histone deacetylase inhibitors and neurodegenerative disorders: holding the promise. Curr Pharm Des 2009; 15: 3940-3957.
    • (2009) Curr Pharm Des , vol.15 , pp. 3940-3957
    • Mai, A.1    Rotili, D.2    Valente, S.3    Kazantsev, A.G.4
  • 19
    • 26444439216 scopus 로고    scopus 로고
    • Prospects: Histone deacetylase inhibitors
    • Dokmanovic M, Marks PA. Prospects: histone deacetylase inhibitors. J Cell Biochem 2005; 96: 293-304.
    • (2005) J Cell Biochem , vol.96 , pp. 293-304
    • Dokmanovic, M.1    Marks, P.A.2
  • 20
    • 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, Beppu T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem 1990; 265: 17174-17179.
    • (1990) J Biol Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 22
    • 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
  • 23
    • 34547094822 scopus 로고    scopus 로고
    • Distinct pharmacological properties of second generation HDAC inhibitors with the benzamide or hydroxamate head group
    • Beckers T, Burkhardt C, Wieland H, et al. Distinct pharmacological properties of second generation HDAC inhibitors with the benzamide or hydroxamate head group. Int J Cancer 2007; 121: 1138-1148.
    • (2007) Int J Cancer , vol.121 , pp. 1138-1148
    • Beckers, T.1    Burkhardt, C.2    Wieland, H.3
  • 24
    • 14844353574 scopus 로고    scopus 로고
    • Identification and functional significance of genes regulated by structurally different histone deacetylase inhibitors
    • Peart MJ, Smyth GK, van Laar RK, et al. Identification and functional significance of genes regulated by structurally different histone deacetylase inhibitors. Proc Natl Acad Sci USA 2005; 102: 3697-3702.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3697-3702
    • Peart, M.J.1    Smyth, G.K.2    van Laar, R.K.3
  • 25
    • 77749309291 scopus 로고    scopus 로고
    • Romidepsin for the treatment of cutaneous T-cell lymphoma
    • Campas-Moya C. Romidepsin for the treatment of cutaneous T-cell lymphoma. Drugs Today (Barc) 2009; 45: 787-795.
    • (2009) Drugs Today (Barc) , vol.45 , pp. 787-795
    • Campas-Moya, C.1
  • 26
    • 34447509697 scopus 로고    scopus 로고
    • Vorinostat: A new oral histone deacetylase inhibitor approved for cutaneous T-cell lymphoma
    • Duvic M, Vu J. Vorinostat: a new oral histone deacetylase inhibitor approved for cutaneous T-cell lymphoma. Expert Opin Investig Drugs 2007; 16: 1111-1120.
    • (2007) Expert Opin Investig Drugs , vol.16 , pp. 1111-1120
    • Duvic, M.1    Vu, J.2
  • 27
    • 77954884940 scopus 로고    scopus 로고
    • Romidepsin: A new therapy for cutaneous T-cell lymphoma and a potential therapy for solid tumors
    • Grant C, Rahman F, Piekarz R, et al. Romidepsin: a new therapy for cutaneous T-cell lymphoma and a potential therapy for solid tumors. Expert Rev Anticancer Ther 2010; 10: 997-1008.
    • (2010) Expert Rev Anticancer Ther , vol.10 , pp. 997-1008
    • Grant, C.1    Rahman, F.2    Piekarz, R.3
  • 28
    • 79954596318 scopus 로고    scopus 로고
    • Photosensitization by iodinated DNA minor groove binding ligands: Evaluation of DNA double-strand break induction and repair
    • Briggs B, Ververis K, Rodd AL, Foong LJ, Silva FM, Karagiannis TC. Photosensitization by iodinated DNA minor groove binding ligands: Evaluation of DNA double-strand break induction and repair. J Photochem Photobiol B 2011; 103: 145-152.
    • (2011) J Photochem Photobiol B , vol.103 , pp. 145-152
    • Briggs, B.1    Ververis, K.2    Rodd, A.L.3    Foong, L.J.4    Silva, F.M.5    Karagiannis, T.C.6
  • 29
    • 40549126605 scopus 로고    scopus 로고
    • Effect of valproic acid on radiation-induced DNA damage in euchromatic and heterochromatic compartments
    • Harikrishnan KN, Karagiannis TC, Chow MZ, El-Osta A. Effect of valproic acid on radiation-induced DNA damage in euchromatic and heterochromatic compartments. Cell Cycle 2008; 7: 468-476.
    • (2008) Cell Cycle , vol.7 , pp. 468-476
    • Harikrishnan, K.N.1    Karagiannis, T.C.2    Chow, M.Z.3    El-Osta, A.4
  • 30
    • 25144451310 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor, Trichostatin A, enhances radiation sensitivity and accumulation of gammaH2A.X
    • Karagiannis TC, Harikrishnan KN, El-Osta A. The histone deacetylase inhibitor, Trichostatin A, enhances radiation sensitivity and accumulation of gammaH2A.X. Cancer Biol Ther 2005; 4: 787-793.
    • (2005) Cancer Biol Ther , vol.4 , pp. 787-793
    • Karagiannis, T.C.1    Harikrishnan, K.N.2    El-Osta, A.3
  • 31
    • 34250015533 scopus 로고    scopus 로고
    • Disparity of histone deacetylase inhibition on repair of radiation-induced DNA damage on euchromatin and constitutive heterochromatin compartments
    • Karagiannis TC, Harikrishnan KN, El-Osta A. Disparity of histone deacetylase inhibition on repair of radiation-induced DNA damage on euchromatin and constitutive heterochromatin compartments. Oncogene 2007; 26: 3963-3971.
    • (2007) Oncogene , vol.26 , pp. 3963-3971
    • Karagiannis, T.C.1    Harikrishnan, K.N.2    El-Osta, A.3
  • 33
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • Kazantsev AG, Thompson LM. Therapeutic application of histone deacetylase inhibitors for central nervous system disorders. Nat Rev Drug Discov 2008; 7: 854-868.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 854-868
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 34
    • 79957954734 scopus 로고    scopus 로고
    • The therapeutic potential of HDAC inhibitors in the treatment of multiple sclerosis
    • Faraco G, Cavone L, Chiarugi A. The therapeutic potential of HDAC inhibitors in the treatment of multiple sclerosis. Mol Med 2011; 17: 442-447.
    • (2011) Mol Med , vol.17 , pp. 442-447
    • Faraco, G.1    Cavone, L.2    Chiarugi, A.3
  • 35
    • 0347296187 scopus 로고    scopus 로고
    • Sodium phenylacetate inhibits adoptive transfer of experimental allergic encephalomyelitis in SJL/J mice at multiple steps
    • Dasgupta S, Zhou Y, Jana M, Banik NL, Pahan K. Sodium phenylacetate inhibits adoptive transfer of experimental allergic encephalomyelitis in SJL/J mice at multiple steps. J Immunol 2003; 170: 3874-3882.
    • (2003) J Immunol , vol.170 , pp. 3874-3882
    • Dasgupta, S.1    Zhou, Y.2    Jana, M.3    Banik, N.L.4    Pahan, K.5
  • 36
    • 20444446595 scopus 로고    scopus 로고
    • Transcriptional therapy with the histone deacetylase inhibitor trichostatin A ameliorates experimental autoimmune encephalomyelitis
    • Camelo S, Iglesias AH, Hwang D, et al. Transcriptional therapy with the histone deacetylase inhibitor trichostatin A ameliorates experimental autoimmune encephalomyelitis. J Neuroimmunol 2005; 164: 10-21.
    • (2005) J Neuroimmunol , vol.164 , pp. 10-21
    • Camelo, S.1    Iglesias, A.H.2    Hwang, D.3
  • 37
    • 0037452775 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease
    • Hockly E, Richon VM, Woodman B, et al. Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease. Proc Natl Acad Sci USA 2003; 100: 2041-2046.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2041-2046
    • Hockly, E.1    Richon, V.M.2    Woodman, B.3
  • 38
    • 34047210698 scopus 로고    scopus 로고
    • Anti-rheumatic activities of histone deacetylase (HDAC) inhibitors in vivo in collagen-induced arthritis in rodents
    • Lin HS, Hu CY, Chan HY, et al. Anti-rheumatic activities of histone deacetylase (HDAC) inhibitors in vivo in collagen-induced arthritis in rodents. Br J Pharmacol 2007; 150: 862-872.
    • (2007) Br J Pharmacol , vol.150 , pp. 862-872
    • Lin, H.S.1    Hu, C.Y.2    Chan, H.Y.3
  • 39
    • 0035931503 scopus 로고    scopus 로고
    • Broad spectrum antiprotozoal agents that inhibit histone deacetylase: Structure-activity relationships of apicidin. Part 2
    • Colletti SL, Myers RW, Darkin-Rattray SJ, et al. Broad spectrum antiprotozoal agents that inhibit histone deacetylase: structure-activity relationships of apicidin. Part 2. Bioorg Med Chem Lett 2001; 11: 113-117.
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 113-117
    • Colletti, S.L.1    Myers, R.W.2    Darkin-Rattray, S.J.3
  • 40
    • 0035931503 scopus 로고    scopus 로고
    • Broad spectrum antiprotozoal agents that inhibit histone deacetylase: Structure-activity relationships of apicidin. Part 1
    • Colletti SL, Myers RW, Darkin-Rattray SJ, et al. Broad spectrum antiprotozoal agents that inhibit histone deacetylase: structure-activity relationships of apicidin. Part 1. Bioorg Med Chem Lett 2001; 11: 107-111.
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 107-111
    • Colletti, S.L.1    Myers, R.W.2    Darkin-Rattray, S.J.3
  • 41
    • 10544250252 scopus 로고    scopus 로고
    • Apicidin: A novel antiprotozoal agent that inhibits parasite histone deacetylase
    • Darkin-Rattray SJ, Gurnett AM, Myers RW, et al. Apicidin: a novel antiprotozoal agent that inhibits parasite histone deacetylase. Proc Natl Acad Sci USA 1996; 93: 13143-13147.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13143-13147
    • Darkin-Rattray, S.J.1    Gurnett, A.M.2    Myers, R.W.3
  • 42
    • 0034192770 scopus 로고    scopus 로고
    • Anti-malarial effect of histone deacetylation inhibitors and mammalian tumour cytodifferentiating agents
    • Andrews KT, Walduck A, Kelso MJ, Fairlie DP, Saul A, Parsons PG. Anti-malarial effect of histone deacetylation inhibitors and mammalian tumour cytodifferentiating agents. Int J Parasitol 2000; 30: 761-768.
    • (2000) Int J Parasitol , vol.30 , pp. 761-768
    • Andrews, K.T.1    Walduck, A.2    Kelso, M.J.3    Fairlie, D.P.4    Saul, A.5    Parsons, P.G.6
  • 43
    • 42049106596 scopus 로고    scopus 로고
    • Potent antimalarial activity of histone deacetylase inhibitor analogues
    • Andrews KT, Tran TN, Lucke AJ, et al. Potent antimalarial activity of histone deacetylase inhibitor analogues. Antimicrob Agents Chemother 2008; 52: 1454-1461.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 1454-1461
    • Andrews, K.T.1    Tran, T.N.2    Lucke, A.J.3
  • 44
    • 13944252903 scopus 로고    scopus 로고
    • Concurrent opposite effects of trichostatin A, an inhibitor of histone deacetylases, on expression of alpha-MHC and cardiac tubulins: Implication for gain in cardiac muscle contractility
    • Davis FJ, Pillai JB, Gupta M, Gupta MP. Concurrent opposite effects of trichostatin A, an inhibitor of histone deacetylases, on expression of alpha-MHC and cardiac tubulins: implication for gain in cardiac muscle contractility. Am J Physiol Heart Circ Physiol 2005; 288: H1477-H1490.
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Davis, F.J.1    Pillai, J.B.2    Gupta, M.3    Gupta, M.P.4
  • 45
    • 1842579393 scopus 로고    scopus 로고
    • Hypertrophy of the heart: A new therapeutic target?
    • Frey N, Katus HA, Olson EN, Hill JA. Hypertrophy of the heart: a new therapeutic target? Circulation 2004; 109: 1580-1589.
    • (2004) Circulation , vol.109 , pp. 1580-1589
    • Frey, N.1    Katus, H.A.2    Olson, E.N.3    Hill, J.A.4
  • 46
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
    • Haberland M, Montgomery RL, Olson EN. The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat Rev Genet 2009; 10: 32-42.
    • (2009) Nat Rev Genet , vol.10 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 47
    • 58149345103 scopus 로고    scopus 로고
    • A new (heat) shocking player in cardiac hypertrophy
    • Vondriska TM, Wang Y. A new (heat) shocking player in cardiac hypertrophy. Circ Res 2008; 103: 1194-1196.
    • (2008) Circ Res , vol.103 , pp. 1194-1196
    • Vondriska, T.M.1    Wang, Y.2
  • 48
    • 79956200230 scopus 로고    scopus 로고
    • Suppression of histone deacetylases worsens right ventricular dysfunction after pulmonary artery banding in rats
    • Bogaard HJ, Mizuno S, Hussaini AA, et al. Suppression of histone deacetylases worsens right ventricular dysfunction after pulmonary artery banding in rats. Am J Respir Crit Care Med 2011; 183: 1402-1410.
    • (2011) Am J Respir Crit Care Med , vol.183 , pp. 1402-1410
    • Bogaard, H.J.1    Mizuno, S.2    Hussaini, A.A.3
  • 49
    • 33644837326 scopus 로고    scopus 로고
    • Control of cardiac growth by histone acetylation/deacetylation
    • Backs J, Olson EN. Control of cardiac growth by histone acetylation/deacetylation. Circ Res 2006; 98: 15-24.
    • (2006) Circ Res , vol.98 , pp. 15-24
    • Backs, J.1    Olson, E.N.2
  • 50
    • 0037162697 scopus 로고    scopus 로고
    • Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy
    • Zhang CL, McKinsey TA, Chang S, Antos CL, Hill JA, Olson EN. Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy. Cell 2002; 110: 479-488.
    • (2002) Cell , vol.110 , pp. 479-488
    • Zhang, C.L.1    McKinsey, T.A.2    Chang, S.3    Antos, C.L.4    Hill, J.A.5    Olson, E.N.6
  • 51
    • 69449096138 scopus 로고    scopus 로고
    • Transcriptional regulation of Foxp3 gene: Multiple signal pathways on the road
    • Shen Z, Chen L, Hao F, Wu J. Transcriptional regulation of Foxp3 gene: multiple signal pathways on the road. Med Res Rev 2009; 29: 742-766.
    • (2009) Med Res Rev , vol.29 , pp. 742-766
    • Shen, Z.1    Chen, L.2    Hao, F.3    Wu, J.4
  • 52
    • 65449158768 scopus 로고    scopus 로고
    • Genetic and epigenetic networks controlling T helper 1 cell differentiation
    • Placek K, Coffre M, Maiella S, Bianchi E, Rogge L. Genetic and epigenetic networks controlling T helper 1 cell differentiation. Immunology 2009; 127: 155-162.
    • (2009) Immunology , vol.127 , pp. 155-162
    • Placek, K.1    Coffre, M.2    Maiella, S.3    Bianchi, E.4    Rogge, L.5
  • 53
    • 3042566927 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor Trichostatin A modulates CD4+ T cell responses
    • Moreira JM, Scheipers P, Sorensen P. The histone deacetylase inhibitor Trichostatin A modulates CD4+ T cell responses. BMC Cancer 2003; 3: 30.
    • (2003) BMC Cancer , vol.3 , pp. 30
    • Moreira, J.M.1    Scheipers, P.2    Sorensen, P.3
  • 54
    • 46749144173 scopus 로고    scopus 로고
    • Histone deacetylase inhibition modulates indoleamine 2,3-dioxygenase-dependent DC functions and regulates experimental graft-versus-host disease in mice
    • Reddy P, Sun Y, Toubai T, et al. Histone deacetylase inhibition modulates indoleamine 2,3-dioxygenase-dependent DC functions and regulates experimental graft-versus-host disease in mice. J Clin Invest 2008; 118: 2562-2573.
    • (2008) J Clin Invest , vol.118 , pp. 2562-2573
    • Reddy, P.1    Sun, Y.2    Toubai, T.3
  • 55
    • 0032577868 scopus 로고    scopus 로고
    • Differential expression of human histone deacetylase mRNAs in response to immune cell apoptosis induction by trichostatin A and butyrate
    • Dangond F, Gullans SR. Differential expression of human histone deacetylase mRNAs in response to immune cell apoptosis induction by trichostatin A and butyrate. Biochem Biophys Res Commun 1998; 247: 833-837.
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 833-837
    • Dangond, F.1    Gullans, S.R.2
  • 56
    • 67449163837 scopus 로고    scopus 로고
    • Use of epigenetic modification to induce FOXP3 expression in naive T cells
    • Moon C, Kim SH, Park KS, et al. Use of epigenetic modification to induce FOXP3 expression in naive T cells. Transplant Proc 2009; 41: 1848-1854.
    • (2009) Transplant Proc , vol.41 , pp. 1848-1854
    • Moon, C.1    Kim, S.H.2    Park, K.S.3
  • 57
    • 35948980739 scopus 로고    scopus 로고
    • Deacetylase inhibition promotes the generation and function of regulatory T cells
    • Tao R, de Zoeten EF, Ozkaynak E, et al. Deacetylase inhibition promotes the generation and function of regulatory T cells. Nat Med 2007; 13: 1299-1307.
    • (2007) Nat Med , vol.13 , pp. 1299-1307
    • Tao, R.1    de Zoeten, E.F.2    Ozkaynak, E.3
  • 58
    • 37149018400 scopus 로고    scopus 로고
    • FOXP3 actively represses transcription by recruiting the HAT/HDAC complex
    • Li B, Greene MI. FOXP3 actively represses transcription by recruiting the HAT/HDAC complex. Cell Cycle 2007; 6: 1432-1436.
    • (2007) Cell Cycle , vol.6 , pp. 1432-1436
    • Li, B.1    Greene, M.I.2
  • 59
    • 33846876336 scopus 로고    scopus 로고
    • Histone deacetylase activities are required for innate immune cell control of Th1 but not Th2 effector cell function
    • Brogdon JL, Xu Y, Szabo SJ, et al. Histone deacetylase activities are required for innate immune cell control of Th1 but not Th2 effector cell function. Blood 2007; 109: 1123-1130.
    • (2007) Blood , vol.109 , pp. 1123-1130
    • Brogdon, J.L.1    Xu, Y.2    Szabo, S.J.3
  • 60
    • 51449089427 scopus 로고    scopus 로고
    • Butyrate inhibits functional differentiation of human monocyte-derived dendritic cells
    • Wang B, Morinobu A, Horiuchi M, Liu J, Kumagai S. Butyrate inhibits functional differentiation of human monocyte-derived dendritic cells. Cell Immunol 2008; 253: 54-58.
    • (2008) Cell Immunol , vol.253 , pp. 54-58
    • Wang, B.1    Morinobu, A.2    Horiuchi, M.3    Liu, J.4    Kumagai, S.5
  • 61
    • 34447119505 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors affect dendritic cell differentiation and immunogenicity
    • Nencioni A, Beck J, Werth D, et al. Histone deacetylase inhibitors affect dendritic cell differentiation and immunogenicity. Clin Cancer Res 2007; 13: 3933-3941.
    • (2007) Clin Cancer Res , vol.13 , pp. 3933-3941
    • Nencioni, A.1    Beck, J.2    Werth, D.3
  • 62
    • 62149139389 scopus 로고    scopus 로고
    • Valproic acid (VPA), a histone deacetylase (HDAC) inhibitor, diminishes lymphoproliferation in the Fas -deficient MRL/lpr(-/-) murine model of autoimmune lymphoproliferative syndrome (ALPS)
    • Dowdell KC, Pesnicak L, Hoffmann V, et al. Valproic acid (VPA), a histone deacetylase (HDAC) inhibitor, diminishes lymphoproliferation in the Fas -deficient MRL/lpr(-/-) murine model of autoimmune lymphoproliferative syndrome (ALPS). Exp Hematol 2009; 37: 487-494.
    • (2009) Exp Hematol , vol.37 , pp. 487-494
    • Dowdell, K.C.1    Pesnicak, L.2    Hoffmann, V.3
  • 63
    • 0035874537 scopus 로고    scopus 로고
    • Increases in circulating and lymphoid tissue interleukin-10 in autoimmune lymphoproliferative syndrome are associated with disease expression
    • Lopatin U, Yao X, Williams RK, et al. Increases in circulating and lymphoid tissue interleukin-10 in autoimmune lymphoproliferative syndrome are associated with disease expression. Blood 2001; 97: 3161-3170.
    • (2001) Blood , vol.97 , pp. 3161-3170
    • Lopatin, U.1    Yao, X.2    Williams, R.K.3
  • 64
    • 0030614415 scopus 로고    scopus 로고
    • Clincal, immunologic, and genetic features of an autoimmune lymphoproliferative syndrome associated with abnormal lymphocyte apoptosis
    • Sneller MC, Wang J, Dale JK, et al. Clincal, immunologic, and genetic features of an autoimmune lymphoproliferative syndrome associated with abnormal lymphocyte apoptosis. Blood 1997; 89: 1341-1348.
    • (1997) Blood , vol.89 , pp. 1341-1348
    • Sneller, M.C.1    Wang, J.2    Dale, J.K.3
  • 65
    • 38349172125 scopus 로고    scopus 로고
    • Taking ALPS down a Notch
    • Rao V. Taking ALPS down a Notch. Blood 2008; 111: 477.
    • (2008) Blood , vol.111 , pp. 477
    • Rao, V.1
  • 66
    • 0026568919 scopus 로고
    • Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis
    • Watanabe-Fukunaga R, Brannan CI, Copeland NG, Jenkins NA, Nagata S. Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis. Nature 1992; 356: 314-317.
    • (1992) Nature , vol.356 , pp. 314-317
    • Watanabe-Fukunaga, R.1    Brannan, C.I.2    Copeland, N.G.3    Jenkins, N.A.4    Nagata, S.5
  • 67
    • 29144491494 scopus 로고    scopus 로고
    • Resetting the epigenetic histone code in the MRL-lpr/lpr mouse model of lupus by histone deacetylase inhibition
    • Garcia BA, Busby SA, Shabanowitz J, Hunt DF, Mishra N. Resetting the epigenetic histone code in the MRL-lpr/lpr mouse model of lupus by histone deacetylase inhibition. J Proteome Res 2005; 4: 2032-2042.
    • (2005) J Proteome Res , vol.4 , pp. 2032-2042
    • Garcia, B.A.1    Busby, S.A.2    Shabanowitz, J.3    Hunt, D.F.4    Mishra, N.5
  • 68
    • 80051693245 scopus 로고    scopus 로고
    • Histone deacetylase 9 deficiency protects against effector T cell-mediated systemic autoimmunity
    • Yan K, Cao Q, Reilly CM, Young NL, Garcia BA, Mishra N. Histone deacetylase 9 deficiency protects against effector T cell-mediated systemic autoimmunity. J Biol Chem 2011; 286: 28833-28843.
    • (2011) J Biol Chem , vol.286 , pp. 28833-28843
    • Yan, K.1    Cao, Q.2    Reilly, C.M.3    Young, N.L.4    Garcia, B.A.5    Mishra, N.6
  • 69
    • 77957033927 scopus 로고    scopus 로고
    • Histone Deacetylase inhibitors: New promise in the treatment of immune and inflammatory diseases
    • Shuttleworth SJ, Bailey SG, Townsend PA. Histone Deacetylase inhibitors: new promise in the treatment of immune and inflammatory diseases. Curr Drug Targets 2010; 11: 1430-1438.
    • (2010) Curr Drug Targets , vol.11 , pp. 1430-1438
    • Shuttleworth, S.J.1    Bailey, S.G.2    Townsend, P.A.3
  • 70
    • 79957954734 scopus 로고    scopus 로고
    • The therapeutic potential of HDAC inhibitors in the treatment of multiple sclerosis
    • Faraco G, Cavone L, Chiarugi A. The therapeutic potential of HDAC inhibitors in the treatment of multiple sclerosis. Mol Med 2011; 17: 442-447.
    • (2011) Mol Med , vol.17 , pp. 442-447
    • Faraco, G.1    Cavone, L.2    Chiarugi, A.3
  • 71
    • 20444446595 scopus 로고    scopus 로고
    • Transcriptional therapy with the histone deacetylase inhibitor trichostatin A ameliorates experimental autoimmune encephalomyelitis
    • Camelo S, Iglesias AH, Hwang D, et al. Transcriptional therapy with the histone deacetylase inhibitor trichostatin A ameliorates experimental autoimmune encephalomyelitis. J Neuroimmunol 2005; 164: 10-21.
    • (2005) J Neuroimmunol , vol.164 , pp. 10-21
    • Camelo, S.1    Iglesias, A.H.2    Hwang, D.3
  • 72
    • 0030882260 scopus 로고    scopus 로고
    • Zlabinger GJ. n-butyrate downregulates the stimulatory function of peripheral blood-derived antigen-presenting cells: A potential mechanism for modulating T-cell responses by short-chain fatty acids
    • Bohmig GA, Krieger PM, Saemann MD, Wenhardt C, Pohanka E, Zlabinger GJ. n-butyrate downregulates the stimulatory function of peripheral blood-derived antigen-presenting cells: a potential mechanism for modulating T-cell responses by short-chain fatty acids. Immunology 1997; 92: 234-243.
    • (1997) Immunology , vol.92 , pp. 234-243
    • Bohmig, G.A.1    Krieger, P.M.2    Saemann, M.D.3    Wenhardt, C.4    Pohanka, E.5
  • 73
    • 0034739319 scopus 로고    scopus 로고
    • Apicidin, an inhibitor of histone deacetylase, prevents H-ras-induced invasive phenotype
    • Kim MS, Son MW, Kim WB, In Park Y, Moon A. Apicidin, an inhibitor of histone deacetylase, prevents H-ras-induced invasive phenotype. Cancer Lett 2000; 157: 23-30.
    • (2000) Cancer Lett , vol.157 , pp. 23-30
    • Kim, M.S.1    Son, M.W.2    Kim, W.B.3    Park, Y.4    Moon, A.5
  • 74
    • 0030198650 scopus 로고    scopus 로고
    • Disruption of cell-cell adhesion in the presence of sodium butyrate activates expression of the 92 kDa type IV collagenase in MDCK cells
    • Fiorino AS, Zvibel I. Disruption of cell-cell adhesion in the presence of sodium butyrate activates expression of the 92 kDa type IV collagenase in MDCK cells. Cell Biol Int 1996; 20: 489-499.
    • (1996) Cell Biol Int , vol.20 , pp. 489-499
    • Fiorino, A.S.1    Zvibel, I.2
  • 75
    • 79961028733 scopus 로고    scopus 로고
    • Treatment with trichostatin A initiated after disease onset delays disease progression and increases survival in a mouse model of amyotrophic lateral sclerosis
    • Yoo YE, Ko CP. Treatment with trichostatin A initiated after disease onset delays disease progression and increases survival in a mouse model of amyotrophic lateral sclerosis. Exp Neurol 2011; 231: 147-159.
    • (2011) Exp Neurol , vol.231 , pp. 147-159
    • Yoo, Y.E.1    Ko, C.P.2
  • 76
    • 33847676166 scopus 로고    scopus 로고
    • Inhibition of histone deacetylases prevents cytokine-induced toxicity in beta cells
    • Larsen L, Tonnesen M, Ronn SG, et al. Inhibition of histone deacetylases prevents cytokine-induced toxicity in beta cells. Diabetologia 2007; 50: 779-789.
    • (2007) Diabetologia , vol.50 , pp. 779-789
    • Larsen, L.1    Tonnesen, M.2    Ronn, S.G.3
  • 77
    • 79957949655 scopus 로고    scopus 로고
    • The oral histone deacetylase inhibitor ITF2357 reduces cytokines and protects islet beta cells in vivo and in vitro
    • Lewis EC, Blaabjerg L, Storling J, et al. The oral histone deacetylase inhibitor ITF2357 reduces cytokines and protects islet beta cells in vivo and in vitro. Mol Med 2011; 17: 369-377.
    • (2011) Mol Med , vol.17 , pp. 369-377
    • Lewis, E.C.1    Blaabjerg, L.2    Storling, J.3
  • 78
    • 70349152864 scopus 로고    scopus 로고
    • A novel histone deacetylase inhibitor prevents IL-1beta induced metabolic dysfunction in pancreatic beta-cells
    • Susick L, Senanayake T, Veluthakal R, Woster PM, Kowluru A. A novel histone deacetylase inhibitor prevents IL-1beta induced metabolic dysfunction in pancreatic beta-cells. J Cell Mol Med 2009; 13: 1877-1885.
    • (2009) J Cell Mol Med , vol.13 , pp. 1877-1885
    • Susick, L.1    Senanayake, T.2    Veluthakal, R.3    Woster, P.M.4    Kowluru, A.5
  • 79
    • 79959994999 scopus 로고    scopus 로고
    • Chromatin remodeling resets the immune system to protect against autoimmune diabetes in mice
    • Patel T, Patel V, Singh R, Jayaraman S. Chromatin remodeling resets the immune system to protect against autoimmune diabetes in mice. Immunol Cell Biol 2011; 89: 640-649.
    • (2011) Immunol Cell Biol , vol.89 , pp. 640-649
    • Patel, T.1    Patel, V.2    Singh, R.3    Jayaraman, S.4
  • 80
    • 84856634405 scopus 로고    scopus 로고
    • Trichostatin A abrogates airway constriction, but not inflammation, in murine and human asthma models
    • Banerjee A, Trivedi CM, Damera G, et al. Trichostatin A abrogates airway constriction, but not inflammation, in murine and human asthma models. Am J Respir Cell Mol Biol 2012; 46(2): 132-138.
    • (2012) Am J Respir Cell Mol Biol , vol.46 , Issue.2 , pp. 132-138
    • Banerjee, A.1    Trivedi, C.M.2    Damera, G.3
  • 82
    • 67650550767 scopus 로고    scopus 로고
    • Synergistic activation of HIV-1 expression by deacetylase inhibitors and prostratin: Implications for treatment of latent infection
    • Reuse S, Calao M, Kabeya K, et al. Synergistic activation of HIV-1 expression by deacetylase inhibitors and prostratin: implications for treatment of latent infection. PLoS One 2009; 4: e6093.
    • (2009) PLoS One , vol.4
    • Reuse, S.1    Calao, M.2    Kabeya, K.3
  • 83
    • 0036839054 scopus 로고    scopus 로고
    • Synergistic activation of human immunodeficiency virus type 1 promoter activity by NF-kappaB and inhibitors of deacetylases: Potential perspectives for the development of therapeutic strategies
    • Quivy V, Adam E, Collette Y, et al. Synergistic activation of human immunodeficiency virus type 1 promoter activity by NF-kappaB and inhibitors of deacetylases: potential perspectives for the development of therapeutic strategies. J Virol 2002; 76: 11091-11103.
    • (2002) J Virol , vol.76 , pp. 11091-11103
    • Quivy, V.1    Adam, E.2    Collette, Y.3
  • 84
    • 4143089463 scopus 로고    scopus 로고
    • Administration of HDAC inhibitors to reactivate HIV-1 expression in latent cellular reservoirs: Implications for the development of therapeutic strategies
    • Demonte D, Quivy V, Colette Y, Van Lint C. Administration of HDAC inhibitors to reactivate HIV-1 expression in latent cellular reservoirs: implications for the development of therapeutic strategies. Biochem Pharmacol 2004; 68: 1231123-8.
    • (2004) Biochem Pharmacol , vol.68 , pp. 1231123-1231128
    • Demonte, D.1    Quivy, V.2    Colette, Y.3    van Lint, C.4
  • 85
    • 33644540503 scopus 로고    scopus 로고
    • Latency: The hidden HIV-1 challenge
    • Marcello A. Latency: the hidden HIV-1 challenge. Retrovirology 2006; 3: 7.
    • (2006) Retrovirology , vol.3 , pp. 7
    • Marcello, A.1
  • 86
    • 46149125241 scopus 로고    scopus 로고
    • A pervasive role of histone acetyltransferases and deacetylases in an NF-kappaB-signaling code
    • Calao M, Burny A, Quivy V, Dekoninck A, Van Lint C. A pervasive role of histone acetyltransferases and deacetylases in an NF-kappaB-signaling code. Trends Biochem Sci 2008; 33: 339-349.
    • (2008) Trends Biochem Sci , vol.33 , pp. 339-349
    • Calao, M.1    Burny, A.2    Quivy, V.3    Dekoninck, A.4    van Lint, C.5
  • 87
    • 0029919356 scopus 로고    scopus 로고
    • Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation
    • Van Lint C, Emiliani S, Ott M, Verdin E. Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation. EMBO J 1996; 15: 1112-1120.
    • (1996) EMBO J , vol.15 , pp. 1112-1120
    • van Lint, C.1    Emiliani, S.2    Ott, M.3    Verdin, E.4
  • 88
    • 79959337704 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylases: Correlation between isoform specificity and reactivation of HIV type 1 (HIV-1) from latently infected cells
    • Huber K, Doyon G, Plaks J, Fyne E, Mellors JW, Sluis-Cremer N. Inhibitors of histone deacetylases: correlation between isoform specificity and reactivation of HIV type 1 (HIV-1) from latently infected cells. J Biol Chem 2011; 286: 22211-22218.
    • (2011) J Biol Chem , vol.286 , pp. 22211-22218
    • Huber, K.1    Doyon, G.2    Plaks, J.3    Fyne, E.4    Mellors, J.W.5    Sluis-Cremer, N.6
  • 89
    • 79251554670 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors impair innate immune responses to Toll-like receptor agonists and to infection
    • Roger T, Lugrin J, Le Roy D, et al. Histone deacetylase inhibitors impair innate immune responses to Toll-like receptor agonists and to infection. Blood 2011; 117: 1205-1217.
    • (2011) Blood , vol.117 , pp. 1205-1217
    • Roger, T.1    Lugrin, J.2    Le, R.D.3
  • 90
    • 35948983828 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors decrease Toll-like receptor-mediated activation of proinflammatory gene expression by impairing transcription factor recruitment
    • Bode KA, Schroder K, Hume DA, et al. Histone deacetylase inhibitors decrease Toll-like receptor-mediated activation of proinflammatory gene expression by impairing transcription factor recruitment. Immunology 2007; 122: 596-606.
    • (2007) Immunology , vol.122 , pp. 596-606
    • Bode, K.A.1    Schroder, K.2    Hume, D.A.3
  • 91
    • 77954013043 scopus 로고    scopus 로고
    • Differential effects of selective HDAC inhibitors on macrophage inflammatory responses to the Toll-like receptor 4 agonist LPS
    • Halili MA, Andrews MR, Labzin LI, et al. Differential effects of selective HDAC inhibitors on macrophage inflammatory responses to the Toll-like receptor 4 agonist LPS. J Leukoc Biol 2010; 87: 1103-1114.
    • (2010) J Leukoc Biol , vol.87 , pp. 1103-1114
    • Halili, M.A.1    Andrews, M.R.2    Labzin, L.I.3
  • 92
    • 80053428068 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors impair antibacterial defenses of macrophages
    • Mombelli M, Lugrin J, Rubino I, et al. Histone deacetylase inhibitors impair antibacterial defenses of macrophages. J Infect Dis 2011; 204: 1367-1374.
    • (2011) J Infect Dis , vol.204 , pp. 1367-1374
    • Mombelli, M.1    Lugrin, J.2    Rubino, I.3
  • 93
    • 57849154398 scopus 로고    scopus 로고
    • From immunity to tolerance through HDAC
    • Georgopoulos K. From immunity to tolerance through HDAC. Nat Immunol 2009; 10: 13-14.
    • (2009) Nat Immunol , vol.10 , pp. 13-14
    • Georgopoulos, K.1
  • 94
    • 57849096553 scopus 로고    scopus 로고
    • The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance
    • Villagra A, Cheng F, Wang HW, et al. The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance. Nat Immunol 2009; 10: 92-100.
    • (2009) Nat Immunol , vol.10 , pp. 92-100
    • Villagra, A.1    Cheng, F.2    Wang, H.W.3
  • 95
    • 80052735701 scopus 로고    scopus 로고
    • Advantages of promoting interleukin-10 by silence of histone deacetylase 11 in inducing tolerance in orthotopic liver transplantation in rats
    • Lai X, Li JZ, Lian ZR, et al. Advantages of promoting interleukin-10 by silence of histone deacetylase 11 in inducing tolerance in orthotopic liver transplantation in rats. Transplant Proc 2011; 43: 2728-2732.
    • (2011) Transplant Proc , vol.43 , pp. 2728-2732
    • Lai, X.1    Li, J.Z.2    Lian, Z.R.3
  • 96
    • 84859541677 scopus 로고    scopus 로고
    • Suppression of Histone Deacetylase 11 Promotes Expression of IL-10 in Kupffer Cells and Induces Tolerance Following Orthotopic Liver Transplantation in Rats
    • Lian ZR, Xu YF, Wang XB, Gong JP, Liu ZJ. Suppression of Histone Deacetylase 11 Promotes Expression of IL-10 in Kupffer Cells and Induces Tolerance Following Orthotopic Liver Transplantation in Rats. J Surg Res 2012; 174(2): 359-368.
    • (2012) J Surg Res , vol.174 , Issue.2 , pp. 359-368
    • Lian, Z.R.1    Xu, Y.F.2    Wang, X.B.3    Gong, J.P.4    Liu, Z.J.5
  • 97
    • 79953084657 scopus 로고    scopus 로고
    • HDAC11 plays an essential role in regulating OX40 ligand expression in Hodgkin lymphoma
    • Buglio D, Khaskhely NM, Voo KS, Martinez-Valdez H, Liu YJ, Younes A. HDAC11 plays an essential role in regulating OX40 ligand expression in Hodgkin lymphoma. Blood 2011; 117: 2910-2917.
    • (2011) Blood , vol.117 , pp. 2910-2917
    • Buglio, D.1    Khaskhely, N.M.2    Voo, K.S.3    Martinez-Valdez, H.4    Liu, Y.J.5    Younes, A.6


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