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Volumn 413, Issue 1, 2008, Pages 143-150

Identification of novel small-molecule histone deacetylase inhibitors by medium-throughput screening using a fluorigenic assay

Author keywords

Chromone; Histone deacetylase like amidohydrolase (HDAH); Medium throughput screening; p benzoquinone; Pyran 4 one; Trifluoromethylketone

Indexed keywords

ACETYLATION; BIOACTIVITY; BIOCHEMISTRY; CELLS; CHEMOTHERAPY; ENZYMES; FOOD ADDITIVES; GENE EXPRESSION; LEAD; METABOLISM; MODEL STRUCTURES; ONCOGENIC VIRUSES; STABILIZERS (AGENTS); THROUGHPUT;

EID: 46249130572     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20080536     Document Type: Article
Times cited : (19)

References (53)
  • 1
    • 34248656480 scopus 로고    scopus 로고
    • Histone deacetylases: An important class of cellular regulators with a variety of functions
    • Hildmann, C., Riester, D. and Schwienhorst, A. (2007) Histone deacetylases: an important class of cellular regulators with a variety of functions. Appl. Microbiol. Biotechnol. 75, 487-497
    • (2007) Appl. Microbiol. Biotechnol , vol.75 , pp. 487-497
    • Hildmann, C.1    Riester, D.2    Schwienhorst, A.3
  • 2
    • 35848958631 scopus 로고    scopus 로고
    • Signal transduction pathways and the modification of chromatin structure
    • Davie, J. R. and Spencer, V. A. (2001) Signal transduction pathways and the modification of chromatin structure. Prog. Nucleic Acid Res. Mol. Biol. 65, 299-340
    • (2001) Prog. Nucleic Acid Res. Mol. Biol , vol.65 , pp. 299-340
    • Davie, J.R.1    Spencer, V.A.2
  • 3
    • 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, J. M., Corner, G. A. and Augenlicht, L. H. (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
  • 5
    • 11844278521 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors
    • Monneret, C. (2005) Histone deacetylase inhibitors. Eur. J. Med. Chem. 40, 1-13
    • (2005) Eur. J. Med. Chem , vol.40 , pp. 1-13
    • Monneret, C.1
  • 7
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • 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
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 8
    • 34248644319 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Turning epigenic mechanisms of gene regulation into tools of therapeutic intervention in malignant and other diseases
    • Riester, D., Hildmann, C. and Schwienhorst, A. (2007) Histone deacetylase inhibitors: turning epigenic mechanisms of gene regulation into tools of therapeutic intervention in malignant and other diseases. Appl. Microbiol. Biotechnol. 75, 499-514
    • (2007) Appl. Microbiol. Biotechnol , vol.75 , pp. 499-514
    • Riester, D.1    Hildmann, C.2    Schwienhorst, A.3
  • 11
    • 33846870167 scopus 로고    scopus 로고
    • An active site tyrosine residue is essential for amidohydrolase but not for esterase activity of a class 2 histone deacetylase-like bacterial enzyme
    • Moreth, K., Riester, D., Hildmann, C., Hempel, R., Wegener, D., Schober, A. and Schwienhorst, A. (2007) An active site tyrosine residue is essential for amidohydrolase but not for esterase activity of a class 2 histone deacetylase-like bacterial enzyme. Biochem. J. 401, 659-665
    • (2007) Biochem. J , vol.401 , pp. 659-665
    • Moreth, K.1    Riester, D.2    Hildmann, C.3    Hempel, R.4    Wegener, D.5    Schober, A.6    Schwienhorst, A.7
  • 15
    • 5444254467 scopus 로고    scopus 로고
    • Members of the histone deacetylase superfamily differ in substrate specificity towards small synthetic substrates
    • Riester, D., Wegener, D., Hildmann, C. and Schwienhorst, A. (2004) Members of the histone deacetylase superfamily differ in substrate specificity towards small synthetic substrates. Biochem. Biophys. Res. Commun. 324, 1116-1123
    • (2004) Biochem. Biophys. Res. Commun , vol.324 , pp. 1116-1123
    • Riester, D.1    Wegener, D.2    Hildmann, C.3    Schwienhorst, A.4
  • 16
    • 0141849191 scopus 로고    scopus 로고
    • Improved fluorogenic histone deacetylase assay for high-throughput-screening applications
    • Wegener, D., Hildmann, C., Riester, D. and Schwienhorst, A. (2003) Improved fluorogenic histone deacetylase assay for high-throughput-screening applications. Anal. Biochem. 321, 202-208
    • (2003) Anal. Biochem , vol.321 , pp. 202-208
    • Wegener, D.1    Hildmann, C.2    Riester, D.3    Schwienhorst, A.4
  • 17
    • 0037253808 scopus 로고    scopus 로고
    • A fluorogenic histone deacetylase assay well suited for high-throughput activity screening
    • Wegener, D., Wirsching, F., Riester, D. and Schwienhorst, A. (2003) A fluorogenic histone deacetylase assay well suited for high-throughput activity screening. Chem. Biol. 10, 61-68
    • (2003) Chem. Biol , vol.10 , pp. 61-68
    • Wegener, D.1    Wirsching, F.2    Riester, D.3    Schwienhorst, A.4
  • 18
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang, J. H., Chung, T. D. and Oldenburg, K. R. (1999) A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J. Biomol. Screen. 4, 67-73
    • (1999) J. Biomol. Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 19
    • 40349098104 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor Helminthosporium carbonum (HC)-toxin suppresses the malignant phenotype of neuroblastoma cells
    • Deubzer, H. E., Ehemann, V., Westermann, F., Heinrich, R., Mechtersheimer, G., Kulozik, A. E., Schwab, M. and Witt, O. (2008) Histone deacetylase inhibitor Helminthosporium carbonum (HC)-toxin suppresses the malignant phenotype of neuroblastoma cells. Int. J. Cancer 122, 1891-1900
    • (2008) Int. J. Cancer , vol.122 , pp. 1891-1900
    • Deubzer, H.E.1    Ehemann, V.2    Westermann, F.3    Heinrich, R.4    Mechtersheimer, G.5    Kulozik, A.E.6    Schwab, M.7    Witt, O.8
  • 20
    • 0024315565 scopus 로고
    • Viability measurements in mammalian cell systems
    • Cook, J. A. and Mitchell, J. B. (1989) Viability measurements in mammalian cell systems. Anal. Biochem. 179, 1-7
    • (1989) Anal. Biochem , vol.179 , pp. 1-7
    • Cook, J.A.1    Mitchell, J.B.2
  • 21
    • 0037369256 scopus 로고    scopus 로고
    • Induction of fetal hemoglobin expression by the histone deacetylase inhibitor apicidin
    • Witt, O., Monkemeyer, S., Ronndahl, G., Erdlenbruch, B., Reinhardt, D., Kanbach, K. and Pekrun, A. (2003) Induction of fetal hemoglobin expression by the histone deacetylase inhibitor apicidin. Blood 101, 2001-2007
    • (2003) Blood , vol.101 , pp. 2001-2007
    • Witt, O.1    Monkemeyer, S.2    Ronndahl, G.3    Erdlenbruch, B.4    Reinhardt, D.5    Kanbach, K.6    Pekrun, A.7
  • 22
    • 33846695065 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor assay based on fluorescence resonance energy transfer
    • Riester, D., Hildmann, C., Schwienhorst, A. and Meyer-Almes, F. J. (2007) Histone deacetylase inhibitor assay based on fluorescence resonance energy transfer. Anal. Biochem. 362, 136-141
    • (2007) Anal. Biochem , vol.362 , pp. 136-141
    • Riester, D.1    Hildmann, C.2    Schwienhorst, A.3    Meyer-Almes, F.J.4
  • 23
    • 0034837064 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylase as new anticancer agents
    • Jung, M. (2001) Inhibitors of histone deacetylase as new anticancer agents. Curr. Med. Chem. 8, 1505-1511
    • (2001) Curr. Med. Chem , vol.8 , pp. 1505-1511
    • Jung, M.1
  • 25
    • 0033244380 scopus 로고    scopus 로고
    • Reactions of 2-polyfluoroacylcyclohexanones with 1,2-diaminoarenes
    • Pashkevich, K. I., Sevenard, D. V. and Khomutov, O. G. (1999) Reactions of 2-polyfluoroacylcyclohexanones with 1,2-diaminoarenes. Russ. Chem. Bull. 48, 557-560
    • (1999) Russ. Chem. Bull , vol.48 , pp. 557-560
    • Pashkevich, K.I.1    Sevenard, D.V.2    Khomutov, O.G.3
  • 26
    • 0000926454 scopus 로고
    • Microbial production, structure elucidation and bioconversion of sophorose lipids
    • Asmer, H.-J., Lang, S., Wagner, F. and Wray, V. (1988) Microbial production, structure elucidation and bioconversion of sophorose lipids. J. Am. Oil Chem. Soc. 65, 1460-1466
    • (1988) J. Am. Oil Chem. Soc , vol.65 , pp. 1460-1466
    • Asmer, H.-J.1    Lang, S.2    Wagner, F.3    Wray, V.4
  • 27
    • 0026755646 scopus 로고
    • Depudecin: A novel compound inducing the flat phenotype of NIH3T3 cells doubly transformed by ras- and src-oncogene, produced by Alternaria brassicicola
    • Matsumoto, M., Matsutani, S., Sugita, K., Yoshida, H., Hayashi, F., Terui, Y., Nakai, H., Uotani, N., Kawamura, Y., Matsumoto, K. et al. (1992) Depudecin: a novel compound inducing the flat phenotype of NIH3T3 cells doubly transformed by ras- and src-oncogene, produced by Alternaria brassicicola. J. Antibiot. 45, 879-885
    • (1992) J. Antibiot , vol.45 , pp. 879-885
    • Matsumoto, M.1    Matsutani, S.2    Sugita, K.3    Yoshida, H.4    Hayashi, F.5    Terui, Y.6    Nakai, H.7    Uotani, N.8    Kawamura, Y.9    Matsumoto, K.10
  • 30
    • 34250401396 scopus 로고
    • The structure of pilopleurin: A new chromone from Pilopleura kozo-poljanskii
    • Avramenko, L. G., Sklyar, Y. E., Perel'son, M. E. and Pimenov, M. G. (1975) The structure of pilopleurin: a new chromone from Pilopleura kozo-poljanskii. Chem. Nat. Compd. 9, 15-16
    • (1975) Chem. Nat. Compd , vol.9 , pp. 15-16
    • Avramenko, L.G.1    Sklyar, Y.E.2    Perel'son, M.E.3    Pimenov, M.G.4
  • 31
    • 0003183636 scopus 로고
    • The effect of actinomycin D on cancer in childhood
    • Tan, C. T., Dargeon, H. W. and Burchenal, J. H. (1959) The effect of actinomycin D on cancer in childhood. Pediatrics 24, 544-561
    • (1959) Pediatrics , vol.24 , pp. 544-561
    • Tan, C.T.1    Dargeon, H.W.2    Burchenal, J.H.3
  • 32
    • 46749102501 scopus 로고
    • Studies on the therapy of reticulosarcoma(-tosis) with actinomycin
    • Shiba, S. (1959) Studies on the therapy of reticulosarcoma(-tosis) with actinomycin. Acta Unio Int. Cancrum 15, 264-266
    • (1959) Acta Unio Int. Cancrum , vol.15 , pp. 264-266
    • Shiba, S.1
  • 35
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: Development of this histone deacetylase inhibitor as an anticancer drug
    • Marks, P. A. and Breslow, R. (2007) Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug. Nat. Biotechnol. 25, 84-90
    • (2007) Nat. Biotechnol , vol.25 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 38
    • 0029929724 scopus 로고    scopus 로고
    • Novel human DNA alkyltransferases obtained by random substitution and genetic selection in bacteria
    • Christians, F. C. and Loeb, L. A. (1996) Novel human DNA alkyltransferases obtained by random substitution and genetic selection in bacteria. Proc. Natl. Acad. Sci. U.S.A. 93, 6124-6128
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 6124-6128
    • Christians, F.C.1    Loeb, L.A.2
  • 39
    • 2942560687 scopus 로고    scopus 로고
    • Recent applications of biosurfactants as biological and immunological molecules
    • Cameotra, S. S. and Makkar, R. S. (2004) Recent applications of biosurfactants as biological and immunological molecules. Curr. Opin. Microbiol. 7, 262-266
    • (2004) Curr. Opin. Microbiol , vol.7 , pp. 262-266
    • Cameotra, S.S.1    Makkar, R.S.2
  • 40
    • 0030997231 scopus 로고    scopus 로고
    • Differentiation of human promyelocytic leukemia cell line HL60 by microbial extracellular glycolipids
    • Isoda, H., Shinmoto, H., Kitamoto, D., Matsumura, M. and Nakahara, T. (1997) Differentiation of human promyelocytic leukemia cell line HL60 by microbial extracellular glycolipids. Lipids 32, 263-271
    • (1997) Lipids , vol.32 , pp. 263-271
    • Isoda, H.1    Shinmoto, H.2    Kitamoto, D.3    Matsumura, M.4    Nakahara, T.5
  • 41
    • 0031126610 scopus 로고    scopus 로고
    • Microbial extracellular glycolipid induction of differentiation and inhibition of the protein kinase C activity of human promyelocytic leukemia cell line HL60
    • Isoda, H., Kitamoto, D., Shinmoto, H., Matsumura, M. and Nakahara, T. (1997) Microbial extracellular glycolipid induction of differentiation and inhibition of the protein kinase C activity of human promyelocytic leukemia cell line HL60. Biosci. Biotechnol. Biochem. 61, 609-614
    • (1997) Biosci. Biotechnol. Biochem , vol.61 , pp. 609-614
    • Isoda, H.1    Kitamoto, D.2    Shinmoto, H.3    Matsumura, M.4    Nakahara, T.5
  • 42
    • 0032139053 scopus 로고    scopus 로고
    • Bioactivity of extracellular glycolipids: Investigation of potential anti-cancer activity of sophorolipids and sophorolipid-derivatives
    • Scholz, C., Mehta, S., Bisht, K., Guilmanov, V., Kaplan, D., Nicolosi, R. and Gross, R. (1998) Bioactivity of extracellular glycolipids: investigation of potential anti-cancer activity of sophorolipids and sophorolipid-derivatives. Proc. Am. Chem. Soc. Polym. Prepr. 39, 168-169
    • (1998) Proc. Am. Chem. Soc. Polym. Prepr , vol.39 , pp. 168-169
    • Scholz, C.1    Mehta, S.2    Bisht, K.3    Guilmanov, V.4    Kaplan, D.5    Nicolosi, R.6    Gross, R.7
  • 43
    • 46749097906 scopus 로고    scopus 로고
    • Treatment of cancer with chemically-modified sophorolipids,
    • U.S. Pat. Application 60/092,446
    • Gross, R. A., Bisht, K. S., Scholz, C., Mehta, S., Guilmanov, V. and Nicolosi, R. (1998) Treatment of cancer with chemically-modified sophorolipids, U.S. Pat. Application 60/092,446
    • (1998)
    • Gross, R.A.1    Bisht, K.S.2    Scholz, C.3    Mehta, S.4    Guilmanov, V.5    Nicolosi, R.6
  • 45
    • 0029548583 scopus 로고
    • Succinoyl trehalose lipid induced differentiation of human monocytoid leukemic cell line U937 into monocyte-macrophages
    • Isoda, H., Shinmoto, H., Matsumura, M. and Nakahara, T. (1995) Succinoyl trehalose lipid induced differentiation of human monocytoid leukemic cell line U937 into monocyte-macrophages. Cytotechnology 19, 79-88
    • (1995) Cytotechnology , vol.19 , pp. 79-88
    • Isoda, H.1    Shinmoto, H.2    Matsumura, M.3    Nakahara, T.4
  • 46
    • 46749105922 scopus 로고
    • Chromone derivatives useful as antitumor agents,
    • U.S. Pat. 4,904,690
    • Aono, T. and Mizuno, K. (1988) Chromone derivatives useful as antitumor agents, U.S. Pat. 4,904,690
    • (1988)
    • Aono, T.1    Mizuno, K.2
  • 47
    • 28544452258 scopus 로고    scopus 로고
    • Piperazinobenzopyranones and phenalkylaminobenzopyranones: Potent inhibitors of breast cancer resistance protein (ABCG2)
    • Boumendjel, A., Nicolle, E., Moraux, T., Gerby, B., Blanc, M., Ronot, X. and Boutonnat, J. (2005) Piperazinobenzopyranones and phenalkylaminobenzopyranones: potent inhibitors of breast cancer resistance protein (ABCG2). J. Med. Chem. 48, 7275-7281
    • (2005) J. Med. Chem , vol.48 , pp. 7275-7281
    • Boumendjel, A.1    Nicolle, E.2    Moraux, T.3    Gerby, B.4    Blanc, M.5    Ronot, X.6    Boutonnat, J.7
  • 48
    • 0036898614 scopus 로고    scopus 로고
    • Down-regulation of PIK3CG, a catalytic subunit of phosphatidylinositol 3-OH kinase, by CpG hypermethylation in human colorectal carcinoma
    • Semba, S., Itoh, N., Ito, M., Youssef, E. M., Harada, M., Moriya, T., Kimura, W. and Yamakawa, M. (2002) Down-regulation of PIK3CG, a catalytic subunit of phosphatidylinositol 3-OH kinase, by CpG hypermethylation in human colorectal carcinoma. Clin. Cancer Res. 8, 3824-3831
    • (2002) Clin. Cancer Res , vol.8 , pp. 3824-3831
    • Semba, S.1    Itoh, N.2    Ito, M.3    Youssef, E.M.4    Harada, M.5    Moriya, T.6    Kimura, W.7    Yamakawa, M.8
  • 49
    • 0026260045 scopus 로고
    • Solution structure of actinomycin-DNA complexes: Drug intercalation at isolated G-C sites
    • Liu, X. Y., Chen, H. and Patel, D. V. (1991) Solution structure of actinomycin-DNA complexes: drug intercalation at isolated G-C sites. J. Biomol. NMR 1, 323-347
    • (1991) J. Biomol. NMR , vol.1 , pp. 323-347
    • Liu, X.Y.1    Chen, H.2    Patel, D.V.3
  • 50
    • 0026660866 scopus 로고
    • NMR study of the solution conformation of actinomycin D
    • Yu, C. and Tseng, Y. Y. (1992) NMR study of the solution conformation of actinomycin D. Eur. J. Biochem. 209, 181-187
    • (1992) Eur. J. Biochem , vol.209 , pp. 181-187
    • Yu, C.1    Tseng, Y.Y.2
  • 51
    • 0019288968 scopus 로고
    • Selective inhibition of rat liver nuclear RNA polymerase II by actinomycin D in vivo
    • Yu, F. L. (1980) Selective inhibition of rat liver nuclear RNA polymerase II by actinomycin D in vivo. Carcinogenesis 1, 577-581
    • (1980) Carcinogenesis , vol.1 , pp. 577-581
    • Yu, F.L.1
  • 52
    • 0019390734 scopus 로고
    • DNA double-stranded breaks in mammalian cells after exposure to intercalating agents
    • Ross, W. E. and Bradley, M. O. (1981) DNA double-stranded breaks in mammalian cells after exposure to intercalating agents. Biochim. Biophys. Acta 654, 129-134
    • (1981) Biochim. Biophys. Acta , vol.654 , pp. 129-134
    • Ross, W.E.1    Bradley, M.O.2
  • 53
    • 0028180032 scopus 로고
    • Cell cycle phase-dependent cytotoxicity of actinomycin D in HeLa cells
    • Wu, M. H. and Yung, B. Y. (1994) Cell cycle phase-dependent cytotoxicity of actinomycin D in HeLa cells. Eur. J. Pharmacol. 270, 203-212
    • (1994) Eur. J. Pharmacol , vol.270 , pp. 203-212
    • Wu, M.H.1    Yung, B.Y.2


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