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Volumn 30, Issue 4, 2012, Pages 1715-1724

Synergetic effects of DNA demethylation and histone deacetylase inhibition in primary rat hepatocytes

Author keywords

DNA methyltransferase inhibitors; Epigenetics; Histone deacetylase inhibitors; Primary hepatocytes

Indexed keywords

5 AZA 2' DEOXYCYTIDINE; 6 [(4 PYRROLIDINE 1 YLBENZOYL)AMINO]HEXANOIC ACID HYDROXAMATE; ALBUMIN; CYCLIN DEPENDENT KINASE 1; CYTOCHROME P450 1A1; DNA; DNA METHYLTRANSFERASE INHIBITOR; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 84866734794     PISSN: 01676997     EISSN: 15730646     Source Type: Journal    
DOI: 10.1007/s10637-011-9659-8     Document Type: Article
Times cited : (14)

References (55)
  • 1
    • 65249157050 scopus 로고    scopus 로고
    • Epigenetics, DNA methylation, and chromatin modifying drugs
    • Szyf M (2009) Epigenetics, DNA methylation, and chromatin modifying drugs. Annu Rev Pharmacol Toxicol 49:243-263
    • (2009) Annu Rev Pharmacol Toxicol , vol.49 , pp. 243-263
    • Szyf, M.1
  • 2
    • 0025716314 scopus 로고
    • DNA methylation and epigenetic inheritance
    • Holliday R (1990) DNA methylation and epigenetic inheritance. Philos Trans R Soc Lond B Biol Sci 326:329-338
    • (1990) Philos Trans R Soc Lond B Biol Sci , vol.326 , pp. 329-338
    • Holliday, R.1
  • 3
    • 85047687069 scopus 로고    scopus 로고
    • Therapeutic implications of DNA methylation
    • Szyf M (2005) Therapeutic implications of DNA methylation. Future Oncol 1:125-135
    • (2005) Future Oncol , vol.1 , pp. 125-135
    • Szyf, M.1
  • 4
    • 21544472099 scopus 로고    scopus 로고
    • DNA methylation and demethylation as targets for anticancer therapy
    • Szyf M (2005) DNA methylation and demethylation as targets for anticancer therapy. Biochemistry (Mosc) 70:533-549
    • (2005) Biochemistry (Mosc) , vol.70 , pp. 533-549
    • Szyf, M.1
  • 5
    • 34547792388 scopus 로고    scopus 로고
    • Epigenetic gene silencing in cancer: The DNA hypermethylome
    • Esteller M (2007) Epigenetic gene silencing in cancer: the DNA hypermethylome. Hum Mol Genet 16:R50-R59
    • (2007) Hum Mol Genet , vol.16
    • Esteller, M.1
  • 6
    • 33744906758 scopus 로고    scopus 로고
    • Decitabine in myelodysplastic syndromes: Viewpoints
    • Garcia-Manero G, Saba HI (2008) Decitabine in myelodysplastic syndromes: viewpoints. Drugs 66:959-960
    • (2008) Drugs , vol.66 , pp. 959-960
    • Garcia-Manero, G.1    Saba, H.I.2
  • 7
    • 43949136445 scopus 로고    scopus 로고
    • Modes of action of the DNA methyltransferase inhibitors azacytidine and decitabine
    • Stresemann C, Lyko F (2008) Modes of action of the DNA methyltransferase inhibitors azacytidine and decitabine. Int J Cancer 123:8-13
    • (2008) Int J Cancer , vol.123 , pp. 8-13
    • Stresemann, C.1    Lyko, F.2
  • 9
    • 4644275854 scopus 로고    scopus 로고
    • 5-aza-2'-deoxycytidine upregulates caspase-9 expression cooperating with p53-induced apoptosis in human lung cancer cells
    • Gomyo Y, Sasaki J, Branch C, Roth JA, Mukhopadhyay T (2004) 5-aza-2'-deoxycytidine upregulates caspase-9 expression cooperating with p53-induced apoptosis in human lung cancer cells. Oncogene 23:6779-6787
    • (2004) Oncogene , vol.23 , pp. 6779-6787
    • Gomyo, Y.1    Sasaki, J.2    Branch, C.3    Roth, J.A.4    Mukhopadhyay, T.5
  • 10
    • 0022404250 scopus 로고
    • Induction of differentiation and inhibition of DNA methylation in HL-60 myeloid leukemic cells by 5-AZA-2'-deoxycytidine
    • Momparler RL, Bouchard J, Samson J (1985) Induction of differentiation and inhibition of DNA methylation in HL-60 myeloid leukemic cells by 5-AZA-2'-deoxycytidine. Leuk Res 9:1361-1366
    • (1985) Leuk Res , vol.9 , pp. 1361-1366
    • Momparler, R.L.1    Bouchard, J.2    Samson, J.3
  • 11
    • 34547911052 scopus 로고    scopus 로고
    • Chemistry of acetyl transfer by histone modifying enzymes: Structure, mechanism and implications for effector design
    • Hodawadekar SC, Marmorstein R (2007) Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design. Oncogene 26:5528-5540
    • (2007) Oncogene , vol.26 , pp. 5528-5540
    • Hodawadekar, S.C.1    Marmorstein, R.2
  • 12
    • 34547924046 scopus 로고    scopus 로고
    • HATs and HDACs: From structure, function and regulation to novel strategies for therapy and prevention
    • Yang XJ, Seto EY (2007) HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention. Oncogene 26:5310-5318
    • (2007) Oncogene , vol.26 , pp. 5310-5318
    • Yang, X.J.1    Seto, E.Y.2
  • 14
    • 78649905409 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: A chemical genetics approach to understanding cellular functions
    • Marks PA (2010) Histone deacetylase inhibitors: a chemical genetics approach to understanding cellular functions. Biochim Biophys Acta 1799(10-12):717-725
    • (2010) Biochim Biophys Acta , vol.1799 , Issue.10-12 , pp. 717-725
    • Marks, P.A.1
  • 15
    • 34547122494 scopus 로고    scopus 로고
    • HDAC inhibitors: Clinical update and mechanism-based potential
    • Glaser KB (2007) HDAC inhibitors: clinical update and mechanism-based potential. Biochem Pharmacol 74:659-671
    • (2007) Biochem Pharmacol , vol.74 , pp. 659-671
    • Glaser, K.B.1
  • 16
    • 67449127082 scopus 로고    scopus 로고
    • Clinical studies of histone deacetylase inhibitors
    • Prince HM, Bishton MJ, Harrison SJ (2009) Clinical studies of histone deacetylase inhibitors. Clin Cancer Res 15:3958-3969
    • (2009) Clin Cancer Res , vol.15 , pp. 3958-3969
    • Prince, H.M.1    Bishton, M.J.2    Harrison, S.J.3
  • 17
    • 67349222049 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as anti-neoplastic agents
    • Batty N, Malouf GG, Issa JP (2009) Histone deacetylase inhibitors as anti-neoplastic agents. Cancer Lett 280:192-200
    • (2009) Cancer Lett , vol.280 , pp. 192-200
    • Batty, N.1    Malouf, G.G.2    Issa, J.P.3
  • 18
    • 59649092334 scopus 로고    scopus 로고
    • Zn(II)-dependent histone deacetylase inhibitors: Suberoylanilide hydroxamic acid and trichostatin A
    • Codd R, Braich N, Liu J, Soe CZ, Pakchung AA (2009) Zn(II)-dependent histone deacetylase inhibitors: suberoylanilide hydroxamic acid and trichostatin A. Int J Biochem Cell Biol 41:736-739
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 736-739
    • Codd, R.1    Braich, N.2    Liu, J.3    Soe, C.Z.4    Pakchung, A.A.5
  • 19
    • 33750688857 scopus 로고    scopus 로고
    • Epigenetic tete-A-tete: The bilateral relationship between chromatin modifications and DNA methylation
    • D'Alessio AC, Szyf M (2006) Epigenetic tete-a-tete: the bilateral relationship between chromatin modifications and DNA methylation. Biochem Cell Biol 84:463-476
    • (2006) Biochem Cell Biol , vol.84 , pp. 463-476
    • D'Alessio, A.C.1    Szyf, M.2
  • 21
    • 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, Herman JG, Baylin SB (1999) Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nat Genet 21:103-107
    • (1999) Nat Genet , vol.21 , pp. 103-107
    • Cameron, E.E.1    Bachman, K.E.2    Myohanen, S.3    Herman, J.G.4    Baylin, S.B.5
  • 23
    • 61749093379 scopus 로고    scopus 로고
    • Combined inhibition of DNA methylation and histone acetylation enhances gene reexpression and drug sensitivity in vivo
    • Steele N, Finn P, Brown R, Plumb JA (2009) Combined inhibition of DNA methylation and histone acetylation enhances gene reexpression and drug sensitivity in vivo. Br J Cancer 100:758-763
    • (2009) Br J Cancer , vol.100 , pp. 758-763
    • Steele, N.1    Finn, P.2    Brown, R.3    Plumb, J.A.4
  • 24
    • 0035866353 scopus 로고    scopus 로고
    • DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors
    • Zhu WG, Lakshmanan RR, Beal MD, Otterson GA (2001) DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors. Cancer Res 61:1327-1333
    • (2001) Cancer Res , vol.61 , pp. 1327-1333
    • Zhu, W.G.1    Lakshmanan, R.R.2    Beal, M.D.3    Otterson, G.A.4
  • 25
    • 0037276902 scopus 로고    scopus 로고
    • The interaction of histone deacetylase inhibitors and DNA methyltransferase inhibitors in the treatment of human cancer cells
    • Zhu WG, Otterson GA (2003) The interaction of histone deacetylase inhibitors and DNA methyltransferase inhibitors in the treatment of human cancer cells. Curr Med Chem Anticancer Agents 3:187-199
    • (2003) Curr Med Chem Anticancer Agents , vol.3 , pp. 187-199
    • Zhu, W.G.1    Otterson, G.A.2
  • 30
    • 18844407076 scopus 로고    scopus 로고
    • Differential effects of histone deacetylase inhibitors in tumor and normal cells-what is the toxicological relevance?
    • Papeleu P, Vanhaecke T, Elaut G, Vinken M, Henkens T, Snykers S, Rogiers V (2005) Differential effects of histone deacetylase inhibitors in tumor and normal cells-what is the toxicological relevance? Crit Rev Toxicol 35:363-378
    • (2005) Crit Rev Toxicol , vol.35 , pp. 363-378
    • Papeleu, P.1    Vanhaecke, T.2    Elaut, G.3    Vinken, M.4    Henkens, T.5    Snykers, S.6    Rogiers, V.7
  • 31
    • 34247510665 scopus 로고    scopus 로고
    • Hepatocytes-The choice to investigate drug metabolism and toxicity in man: In vitro variability as a reflection of in vivo
    • Gomez-Lechon MJ, Castell JV, Donato MT (2007) Hepatocytes-the choice to investigate drug metabolism and toxicity in man: in vitro variability as a reflection of in vivo. Chem Biol Interact 168:30-50
    • (2007) Chem Biol Interact , vol.168 , pp. 30-50
    • Gomez-Lechon, M.J.1    Castell, J.V.2    Donato, M.T.3
  • 33
    • 0033523895 scopus 로고    scopus 로고
    • Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation
    • Jung M, Brosch G, Kolle D, Scherf H, Gerhauser C, Loidl P (1999) Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation. J Med Chem 42:4669-4679
    • (1999) J Med Chem , vol.42 , pp. 4669-4679
    • Jung, M.1    Brosch, G.2    Kolle, D.3    Scherf, H.4    Gerhauser, C.5    Loidl, P.6
  • 34
    • 0030744926 scopus 로고    scopus 로고
    • Analogues of trichostatin A and trapoxin B as histone deacetylase inhibitors
    • Jung M, Hoffmann K, Brosch G, Loidl P (1997) Analogues of trichostatin A and trapoxin B as histone deacetylase inhibitors. Bioorg Med Chem Lett 7:1655-1658
    • (1997) Bioorg Med Chem Lett , vol.7 , pp. 1655-1658
    • Jung, M.1    Hoffmann, K.2    Brosch, G.3    Loidl, P.4
  • 36
    • 3042521360 scopus 로고    scopus 로고
    • Proliferation of Epidermal Growth Factor-stimulated Hepatocytes in a Hormonally Defined Serumfree Medium
    • Papeleu P, Loyer P, Vanhaecke T, Henkens T, Elaut G, Guguen-Guillouzo C, Rogiers V (2004) Proliferation of Epidermal Growth Factor-stimulated Hepatocytes in a Hormonally Defined Serumfree Medium. ATLA 32:57-64
    • (2004) ATLA , vol.32 , pp. 57-64
    • Papeleu, P.1    Loyer, P.2    Vanhaecke, T.3    Henkens, T.4    Elaut, G.5    Guguen-Guillouzo, C.6    Rogiers, V.7
  • 37
    • 0029973363 scopus 로고    scopus 로고
    • Growth factor dependence of progression through G1 and S phases of adult rat hepatocytes in vitro. Evidence of a mitogen restriction point in mid-late G1
    • Loyer P, Cariou S, Glaise D, Bilodeau M, Baffet G, Guguen-Guillouzo C (1996) Growth factor dependence of progression through G1 and S phases of adult rat hepatocytes in vitro. Evidence of a mitogen restriction point in mid-late G1. J Biol Chem 271:11484-11492
    • (1996) J Biol Chem , vol.271 , pp. 11484-11492
    • Loyer, P.1    Cariou, S.2    Glaise, D.3    Bilodeau, M.4    Baffet, G.5    Guguen-Guillouzo, C.6
  • 38
    • 0032795940 scopus 로고    scopus 로고
    • The mitogenactivated protein kinase kinase/extracellular signal-regulated kinase cascade activation is a key signalling pathway involved in the regulation of G(1) phase progression in proliferating hepatocytes
    • Talarmin H, Rescan C, Cariou S, Glaise D, Zanninelli G, Bilodeau M, Loyer P, Guguen-Guillouzo C, Baffet G (1999) The mitogenactivated protein kinase kinase/extracellular signal-regulated kinase cascade activation is a key signalling pathway involved in the regulation of G(1) phase progression in proliferating hepatocytes. Mol Cell Biol 19:6003-6011
    • (1999) Mol Cell Biol , vol.19 , pp. 6003-6011
    • Talarmin, H.1    Rescan, C.2    Cariou, S.3    Glaise, D.4    Zanninelli, G.5    Bilodeau, M.6    Loyer, P.7    Guguen-Guillouzo, C.8    Baffet, G.9
  • 39
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 41
    • 0026158432 scopus 로고
    • Long-term in vitro function of adult hepatocytes in a collagen sandwich configuration
    • Dunn JC, Tompkins RG, Yarmush ML (1991) Long-term in vitro function of adult hepatocytes in a collagen sandwich configuration. Biotechnol Prog 7:237-245
    • (1991) Biotechnol Prog , vol.7 , pp. 237-245
    • Dunn, J.C.1    Tompkins, R.G.2    Yarmush, M.L.3
  • 42
    • 0042830316 scopus 로고    scopus 로고
    • Trichostatin A induces differential cell cycle arrests but does not induce apoptosis in primary cultures of mitogen-stimulated rat hepatocytes
    • Papeleu P, Loyer P, Vanhaecke T, Elaut G, Geerts A, Guguen-Guillouzo C, Rogiers V (2003) Trichostatin A induces differential cell cycle arrests but does not induce apoptosis in primary cultures of mitogen-stimulated rat hepatocytes. J Hepatol 39:374-382
    • (2003) J Hepatol , vol.39 , pp. 374-382
    • Papeleu, P.1    Loyer, P.2    Vanhaecke, T.3    Elaut, G.4    Geerts, A.5    Guguen-Guillouzo, C.6    Rogiers, V.7
  • 43
  • 44
    • 33845902230 scopus 로고    scopus 로고
    • Trichostatin A, a critical factor in maintaining the functional differentiation of primary cultured rat hepatocytes
    • Henkens T, Papeleu P, Elaut G, Vinken M, Rogiers V, Vanhaecke T (2007) Trichostatin A, a critical factor in maintaining the functional differentiation of primary cultured rat hepatocytes. Toxicol Appl Pharmacol 218:64-71
    • (2007) Toxicol Appl Pharmacol , vol.218 , pp. 64-71
    • Henkens, T.1    Papeleu, P.2    Elaut, G.3    Vinken, M.4    Rogiers, V.5    Vanhaecke, T.6
  • 46
    • 71149106051 scopus 로고    scopus 로고
    • In vitro basis for treatment with hypomethylating agents and histone deacetylase inhibitors: Can epigenetic changes be used to monitor treatment?
    • Gore SD (2009) In vitro basis for treatment with hypomethylating agents and histone deacetylase inhibitors: can epigenetic changes be used to monitor treatment? Leuk Res 33(Suppl 2):S2-S6
    • (2009) Leuk Res , vol.33 , Issue.SUPPL. 2
    • Gore, S.D.1
  • 47
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon VM, Sandhoff TW, Rifkind RA, Marks PA (2000) Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc Natl Acad Sci USA 97:10014-10019
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 48
    • 34948830177 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SAHA; Vorinostat) suppresses translation of cyclin D1 in mantle cell lymphoma cells
    • Kawamata N, Chen J, Koeffler HP (2007) Suberoylanilide hydroxamic acid (SAHA; vorinostat) suppresses translation of cyclin D1 in mantle cell lymphoma cells. Blood 110:2667-2673
    • (2007) Blood , vol.110 , pp. 2667-2673
    • Kawamata, N.1    Chen, J.2    Koeffler, H.P.3
  • 49
    • 2642531973 scopus 로고    scopus 로고
    • Epigenetics in human disease and prospects for epigenetic therapy
    • Egger G, Liang G, Aparicio A, Jones PA (2004) Epigenetics in human disease and prospects for epigenetic therapy. Nature 429:457-463
    • (2004) Nature , vol.429 , pp. 457-463
    • Egger, G.1    Liang, G.2    Aparicio, A.3    Jones, P.A.4
  • 51
    • 33747312640 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the dedifferentiation process of isolated hepatocytes and their cultures
    • Elaut G, Henkens T, Papeleu P, Snykers S, Vinken M, Vanhaecke T, Rogiers V (2006) Molecular mechanisms underlying the dedifferentiation process of isolated hepatocytes and their cultures. Curr Drug Metab 7:629-660
    • (2006) Curr Drug Metab , vol.7 , pp. 629-660
    • Elaut, G.1    Henkens, T.2    Papeleu, P.3    Snykers, S.4    Vinken, M.5    Vanhaecke, T.6    Rogiers, V.7
  • 52
    • 0042065286 scopus 로고    scopus 로고
    • Influence of culture time on the expression of drug-metabolizing enzymes in primary human hepatocytes and hepatoma cell line HepG2
    • Wilkening S, Bader A (2003) Influence of culture time on the expression of drug-metabolizing enzymes in primary human hepatocytes and hepatoma cell line HepG2. J Biochem Mol Toxicol 17:207-213
    • (2003) J Biochem Mol Toxicol , vol.17 , pp. 207-213
    • Wilkening, S.1    Bader, A.2
  • 53
    • 0036301269 scopus 로고    scopus 로고
    • Cytochrome P450 expression in human hepatocytes and hepatoma cell lines: Molecular mechanisms that determine lower expression in cultured cells
    • Rodriguez-Antona C, Donato MT, Boobis A, Edwards RJ, Watts PS, Castell JV, Gomez-Lechon MJ (2002) Cytochrome P450 expression in human hepatocytes and hepatoma cell lines: molecular mechanisms that determine lower expression in cultured cells. Xenobiotica 32:505-520
    • (2002) Xenobiotica , vol.32 , pp. 505-520
    • Rodriguez-Antona, C.1    Donato, M.T.2    Boobis, A.3    Edwards, R.J.4    Watts, P.S.5    Castell, J.V.6    Gomez-Lechon, M.J.7
  • 54
    • 0038172423 scopus 로고    scopus 로고
    • Gene expression in two hepatic cell lines, cultured primary hepatocytes, and liver slices compared to the in vivo liver gene expression in rats: Possible implications for toxicogenomics use of in vitro systems
    • Boess F, Kamber M, Romer S, Gasser R, Muller D, Albertini S, Suter L (2003) Gene expression in two hepatic cell lines, cultured primary hepatocytes, and liver slices compared to the in vivo liver gene expression in rats: possible implications for toxicogenomics use of in vitro systems. Toxicol Sci 73:386-402
    • (2003) Toxicol Sci , vol.73 , pp. 386-402
    • Boess, F.1    Kamber, M.2    Romer, S.3    Gasser, R.4    Muller, D.5    Albertini, S.6    Suter, L.7


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