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Volumn 39, Issue 1-2, 1996, Pages 68-78

Histone hyperacetylating agents stimulate promoter activity of human choline acetyltransferase gene in transfection experiment

Author keywords

CHP126 cell; Histone deacetylase; Sympathetic neuron; Trapoxin; Trichostatin

Indexed keywords

BUTYRIC ACID; CHOLINE ACETYLTRANSFERASE; ENZYME INHIBITOR; HISTONE; HISTONE DEACETYLASE; MESSENGER RNA; TRICHOSTATIN A;

EID: 0013587241     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0169-328X(96)00006-X     Document Type: Article
Times cited : (12)

References (72)
  • 1
    • 0026057864 scopus 로고
    • Transcription factor access is mediated by accurately positioned nucleosomes on the mouse mammary tumor virus promoter
    • Archer, T.K., Cordingley, M.G., Wolfors, R.G. and Hager, G.L., Transcription factor access is mediated by accurately positioned nucleosomes on the mouse mammary tumor virus promoter. Mol. Cell. Biol., 11 (1991) 688-698.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 688-698
    • Archer, T.K.1    Cordingley, M.G.2    Wolfors, R.G.3    Hager, G.L.4
  • 3
    • 0022640694 scopus 로고
    • Regulation of metallothionein-I gene by sodium butyrate
    • Birren, B.W. and Hershman, H.R., Regulation of metallothionein-I gene by sodium butyrate. Nucl. Acid. Res., 14 (1986) 853-867.
    • (1986) Nucl. Acid. Res. , vol.14 , pp. 853-867
    • Birren, B.W.1    Hershman, H.R.2
  • 4
    • 0023441843 scopus 로고
    • Butyrate-induced changes in nuclease sensitivity of chromatin cannot be correlated with transcriptional activation
    • Birren, B.W., Taplitz, S.J. and Hershman, H.R., Butyrate-induced changes in nuclease sensitivity of chromatin cannot be correlated with transcriptional activation. Mol. Cell. Biol., 7 (1987) 3863-3870.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3863-3870
    • Birren, B.W.1    Taplitz, S.J.2    Hershman, H.R.3
  • 5
    • 0019810119 scopus 로고
    • Manifold effects of sodium butyrate on nuclear function
    • Boffa, L.C., Gruss, R.J. and Allfrey, V.G., Manifold effects of sodium butyrate on nuclear function. J. Biol. Chem., 256 (1981) 9612-9621.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9612-9621
    • Boffa, L.C.1    Gruss, R.J.2    Allfrey, V.G.3
  • 6
    • 0024350147 scopus 로고
    • Mutational analysis of sodium butyrate inducible elements in the human immunodeficiency virus type I long terminal repeat
    • Bohan, C.A., Robinson, R.A., Luciw, P.A. and Srinivasan, A., Mutational analysis of sodium butyrate inducible elements in the human immunodeficiency virus type I long terminal repeat. Virology, 172 (1989) 573-583.
    • (1989) Virology , vol.172 , pp. 573-583
    • Bohan, C.A.1    Robinson, R.A.2    Luciw, P.A.3    Srinivasan, A.4
  • 7
    • 0027771191 scopus 로고
    • Characterization of a pathway for ciliary neurotrophic factor signaling to the nucleus
    • Bonni, A., Frank, D.A., Schindler, C. and Greenberg, M.E., Characterization of a pathway for Ciliary Neurotrophic Factor signaling to the nucleus. Science, 262 (1993) 1575-1579.
    • (1993) Science , vol.262 , pp. 1575-1579
    • Bonni, A.1    Frank, D.A.2    Schindler, C.3    Greenberg, M.E.4
  • 8
    • 0025297904 scopus 로고
    • Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate
    • Bresnick, E.H., John, S., Berard, D.S., Lefebvre, P. and Hager, G.L., Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate. Proc. Natl. Acad. Sci. USA, 87 (1990) 3977-3981.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3977-3981
    • Bresnick, E.H.1    John, S.2    Berard, D.S.3    Lefebvre, P.4    Hager, G.L.5
  • 9
    • 0023709306 scopus 로고
    • Butyrate induces selective transcription activation of a hypomethylated embryonic globin gene in adult erythroid cells
    • Burns, L.J., Glauber, J.G., Ginder, G.D., Butyrate induces selective transcription activation of a hypomethylated embryonic globin gene in adult erythroid cells. Blood, 72 (1988) 1536-1542.
    • (1988) Blood , vol.72 , pp. 1536-1542
    • Burns, L.J.1    Glauber, J.G.2    Ginder, G.D.3
  • 10
    • 0024552817 scopus 로고
    • Stimulation of choline acetyltransferase activity by retinoic acid and sodium butyrate in a cultured human neuroblastoma
    • Casper D. and Davies P., Stimulation of choline acetyltransferase activity by retinoic acid and sodium butyrate in a cultured human neuroblastoma. Brain Res., 478 (1989) 74-84.
    • (1989) Brain Res. , vol.478 , pp. 74-84
    • Casper, D.1    Davies, P.2
  • 11
    • 0024500154 scopus 로고
    • Mechanism of activation of choline acetyltransferase in a human neuroblastoma cell line
    • Casper D. and Davies P., Mechanism of activation of choline acetyltransferase in a human neuroblastoma cell line. Brain Res., 478 (1989) 85-94.
    • (1989) Brain Res. , vol.478 , pp. 85-94
    • Casper, D.1    Davies, P.2
  • 12
    • 0028917015 scopus 로고
    • Human choline acetyltransferase gene: Localization of alternative first exons
    • Chireux, M., Le Van Thai, A. and Weber, M.J., Human choline acetyltransferase gene: localization of alternative first exons. J. Neurosci. Res., 40 (1994) 427-438.
    • (1994) J. Neurosci. Res. , vol.40 , pp. 427-438
    • Chireux, M.1    Le Van Thai, A.2    Weber, M.J.3
  • 13
    • 0028239096 scopus 로고
    • Performance and limits of the mixed-phase assay for chloramphenicol acetyltransferase at low [3H]acetyl CoA concentration
    • Chireux, M., Raynal, J.-F. and Weber, M.J., Performance and limits of the mixed-phase assay for chloramphenicol acetyltransferase at low [3H]acetyl CoA concentration. Anal. Biochem., 219 (1994) 147-153.
    • (1994) Anal. Biochem. , vol.219 , pp. 147-153
    • Chireux, M.1    Raynal, J.-F.2    Weber, M.J.3
  • 14
    • 0018371969 scopus 로고
    • Different accessibilities in chromatin to histone acetylase
    • Cousens, L.C., Gallwitz, D. and Alberts, B.M., Different accessibilities in chromatin to histone acetylase. J. Biol. Chem., 254 (1979) 1716-1723.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1716-1723
    • Cousens, L.C.1    Gallwitz, D.2    Alberts, B.M.3
  • 15
    • 0019321271 scopus 로고
    • Concentration-dependent effects of sodium butyrate in Chinese hamster cells: Cell-cycle progression, inner-histone acetylation, histone H1 dephosphorylation, and induction of an H1-like protein
    • D'Anna, J.A., Tobey, R.A. and Gurley, L.R., Concentration-dependent effects of sodium butyrate in Chinese hamster cells: cell-cycle progression, inner-histone acetylation, histone H1 dephosphorylation, and induction of an H1-like protein. Biochemistry, 19 (1980) 2656-2671.
    • (1980) Biochemistry , vol.19 , pp. 2656-2671
    • D'Anna, J.A.1    Tobey, R.A.2    Gurley, L.R.3
  • 16
    • 0026710819 scopus 로고
    • Transcriptional regulation of the human placental-like alkaline phosphatase gene and mechanisms involved in its induction by sodium butyrate
    • Deng, G., Liu, G., Hu, L., Gum, J.R. and Kim, Y.S., Transcriptional regulation of the human placental-like alkaline phosphatase gene and mechanisms involved in its induction by sodium butyrate. Cancer Res., 52 (1992) 3378-3383.
    • (1992) Cancer Res. , vol.52 , pp. 3378-3383
    • Deng, G.1    Liu, G.2    Hu, L.3    Gum, J.R.4    Kim, Y.S.5
  • 17
    • 0026517010 scopus 로고
    • Control of the peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptors
    • Dreyer, C., Krey, G., Keller, H., Givel, F., Helftenbein, G. and Wahli, W., Control of the peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptors. Cell, 68 (1992) 879-887.
    • (1992) Cell , vol.68 , pp. 879-887
    • Dreyer, C.1    Krey, G.2    Keller, H.3    Givel, F.4    Helftenbein, G.5    Wahli, W.6
  • 19
    • 0026710374 scopus 로고
    • Two cytosolic cell proteinase genes are differentially sensitive to sodium butyrate
    • Fregeau, C.J., Helgason, C.D. and Bleackley, R.C., Two cytosolic cell proteinase genes are differentially sensitive to sodium butyrate. Nucl. Acid Res., 20 (1992) 3113-3119.
    • (1992) Nucl. Acid Res. , vol.20 , pp. 3113-3119
    • Fregeau, C.J.1    Helgason, C.D.2    Bleackley, R.C.3
  • 20
    • 0027394241 scopus 로고
    • Identification of sequence elements in mouse calbindin-D28k gene that confer 1,25-dihydroxyvitamin D3-and butyrate-inducible responses
    • Gill, R.K. and Christakos, S., Identification of sequence elements in mouse calbindin-D28k gene that confer 1,25-dihydroxyvitamin D3-and butyrate-inducible responses. Proc. Natl. Acad. Sci. USA, 90 (1993) 2984-2988.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2984-2988
    • Gill, R.K.1    Christakos, S.2
  • 21
    • 0021203873 scopus 로고
    • Activation of a chicken embryonic globin gene in adult erythroid cells by 5-azacytidine and sodium butyrate
    • Ginder, G.D., Whitters, M.J., Pohlman, J.K., Activation of a chicken embryonic globin gene in adult erythroid cells by 5-azacytidine and sodium butyrate. Proc. Natl. Acad. Sci. USA, 81 (1984) 3954-3958.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3954-3958
    • Ginder, G.D.1    Whitters, M.J.2    Pohlman, J.K.3
  • 23
    • 0025912341 scopus 로고
    • 5′-flanking sequence mediate butyrate stimulation of embryonic globin gene expression in adult erythroid cells
    • Glauber J.G., Wandersee N.J., Little J.A. and Ginder G.D., 5′-flanking sequence mediate butyrate stimulation of embryonic globin gene expression in adult erythroid cells. Mol. Cell. Biol., 11 (1991) 4690-4697.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4690-4697
    • Glauber, J.G.1    Wandersee, N.J.2    Little, J.A.3    Ginder, G.D.4
  • 24
    • 0021101284 scopus 로고
    • Expression of recombinant plasmids in mammalian cells is enhanced by sodium butyrate
    • German, C.M. and Howard, B.H., Expression of recombinant plasmids in mammalian cells is enhanced by sodium butyrate. Nucl. Acid Res., 11 (1983) 7631-7648.
    • (1983) Nucl. Acid Res. , vol.11 , pp. 7631-7648
    • German, C.M.1    Howard, B.H.2
  • 25
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes, T.R., Thorne, A.W. and Crane-Robinson, C., A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J., 7 (1988) 1395-1402.
    • (1988) EMBO J. , vol.7 , pp. 1395-1402
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 26
    • 0027172737 scopus 로고
    • Comparison of the promoter region of the human and porcine choline acetyltransferase genes: Localization of an important enhancer region
    • Hersh, L.B., Kong, C.F., Sampson, C., Mues, G., Li, Y.-P., Fisher, A., Hilt, D. and Baetge, E.E., Comparison of the promoter region of the human and porcine choline acetyltransferase genes: localization of an important enhancer region. J. Neurochem., 61 (1993) 306-314.
    • (1993) J. Neurochem. , vol.61 , pp. 306-314
    • Hersh, L.B.1    Kong, C.F.2    Sampson, C.3    Mues, G.4    Li, Y.-P.5    Fisher, A.6    Hilt, D.7    Baetge, E.E.8
  • 27
    • 0028022785 scopus 로고
    • Trichostatin A induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines
    • Hoshikawa, Y., Kwon, H.J., Yoshida, M., Horinouchi, S. and Beppu, T., Trichostatin A induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines. Exp. Cell Res., 214 (1994) 189-197.
    • (1994) Exp. Cell Res. , vol.214 , pp. 189-197
    • Hoshikawa, Y.1    Kwon, H.J.2    Yoshida, M.3    Horinouchi, S.4    Beppu, T.5
  • 28
    • 0342674635 scopus 로고
    • A model for differentiation: Modification of chromatin proteins in differentiating erythroid and nonerythroid cells
    • A.W. Nienhuis and G. Stomatoyannopoulos (Eds.), Grune and Stratton, New-York
    • Ingram, V.M., Hagopian, H.K., Riggs, M.G., Neumann, J.R., Dobson, M.E., Owens, B.B. and Maniatis, G.M., A model for differentiation: modification of chromatin proteins in differentiating erythroid and nonerythroid cells. In: A.W. Nienhuis and G. Stomatoyannopoulos (Eds.), Cellular and Molecular Regulation of Hemoglobin Switching, Grune and Stratton, New-York, 1979, pp. 471-489.
    • (1979) Cellular and Molecular Regulation of Hemoglobin Switching , pp. 471-489
    • Ingram, V.M.1    Hagopian, H.K.2    Riggs, M.G.3    Neumann, J.R.4    Dobson, M.E.5    Owens, B.B.6    Maniatis, G.M.7
  • 30
    • 0027466842 scopus 로고
    • Multiple mRNA species of choline acetyltransferase from rat spinal cord
    • Kengaku, M., Misawa, H. and Deguchi, T., Multiple mRNA species of choline acetyltransferase from rat spinal cord. Mol. Brain Res., 18 (1993) 71-76.
    • (1993) Mol. Brain Res. , vol.18 , pp. 71-76
    • Kengaku, M.1    Misawa, H.2    Deguchi, T.3
  • 31
    • 0027378351 scopus 로고
    • Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase
    • Kijima, M., Yoshida, M., Sugita, K., Horinouchi, S. and Beppu, T., Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase. J. Biol. Chem., 268 (1993) 22429-22435.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22429-22435
    • Kijima, M.1    Yoshida, M.2    Sugita, K.3    Horinouchi, S.4    Beppu, T.5
  • 32
    • 0022639635 scopus 로고
    • Effects of cell division, cell density, and cyclic nucleotides on choline acetyltransferase activity in a cholinergic neuroblastoma cell line (S-20Y)
    • Kirshner, J.A., Markelonis, G.J. and Max, S.R., Effects of cell division, cell density, and cyclic nucleotides on choline acetyltransferase activity in a cholinergic neuroblastoma cell line (S-20Y). J. Neurochem., 46 (1986) 817-821.
    • (1986) J. Neurochem. , vol.46 , pp. 817-821
    • Kirshner, J.A.1    Markelonis, G.J.2    Max, S.R.3
  • 33
    • 0026697332 scopus 로고
    • Scaffold-attached regions (SAR elements) mediate transcriptional effects due to butyrate
    • Klehr, D., Schlake, T., Maass, K. and Bode J., Scaffold-attached regions (SAR elements) mediate transcriptional effects due to butyrate. Biochemistry, 31 (1992) 3222-3229.
    • (1992) Biochemistry , vol.31 , pp. 3222-3229
    • Klehr, D.1    Schlake, T.2    Maass, K.3    Bode, J.4
  • 34
    • 0020025385 scopus 로고
    • Effects of sodium butyrate, a new pharmacologic agent, on cells in culture
    • Kruh, J., Effects of sodium butyrate, a new pharmacologic agent, on cells in culture. Mol. Cell. Biol., 42 (1982) 65-82.
    • (1982) Mol. Cell. Biol. , vol.42 , pp. 65-82
    • Kruh, J.1
  • 35
    • 0027474156 scopus 로고
    • Identification of a neuron-specific promoter of human aromatic L-amino acid decarboxylase gene
    • Le Van Thai, A., Coste, E., Allen, M.J., Palmiter, R.D. and Weber, M.J., Identification of a neuron-specific promoter of human aromatic L-amino acid decarboxylase gene. Mol. Brain Res., 17 (1993) 227-238.
    • (1993) Mol. Brain Res. , vol.17 , pp. 227-238
    • Le Van Thai, A.1    Coste, E.2    Allen, M.J.3    Palmiter, R.D.4    Weber, M.J.5
  • 36
    • 0026017987 scopus 로고
    • Inhibition of promoter activity by methylation: Possible involvement of protein mediators
    • Levine, A., Cantoni, G.L. and Razin, A., Inhibition of promoter activity by methylation: possible involvement of protein mediators. Proc. Natl. Acad. Sci. USA, 88 (1991) 6515-6518.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6515-6518
    • Levine, A.1    Cantoni, G.L.2    Razin, A.3
  • 37
    • 0027411076 scopus 로고
    • Cyclic AMP regulation of human choline acetyltransferase gene
    • Li, Y.P., Beatge, E.E. and Hersh, L.B., Cyclic AMP regulation of human choline acetyltransferase gene. Neurosci. Res., 18 (1993) 271-275.
    • (1993) Neurosci. Res. , vol.18 , pp. 271-275
    • Li, Y.P.1    Beatge, E.E.2    Hersh, L.B.3
  • 38
    • 0028911160 scopus 로고
    • A cell type-specific silencer in the human choline acetyltransferase gene requiring two distinct and interactive E boxes
    • Li, Y.-P., Baskin, F., Davis, R., Wu, D. and Hersh, L.B., A cell type-specific silencer in the human choline acetyltransferase gene requiring two distinct and interactive E boxes. Mol. Brain Res., 30 (1995) 106-114.
    • (1995) Mol. Brain Res. , vol.30 , pp. 106-114
    • Li, Y.-P.1    Baskin, F.2    Davis, R.3    Wu, D.4    Hersh, L.B.5
  • 39
    • 0019132555 scopus 로고
    • Butyrate and related inhibitors of histone deacetylation block the induction of egg white genes by steroid hormones
    • McKnight, S., Hager, L. and Palmiter, R.D., Butyrate and related inhibitors of histone deacetylation block the induction of egg white genes by steroid hormones. Cell, 22 (1980) 469-477.
    • (1980) Cell , vol.22 , pp. 469-477
    • McKnight, S.1    Hager, L.2    Palmiter, R.D.3
  • 40
    • 0026713577 scopus 로고
    • Gene expression of mouse choline acetyltransferase. Alternative splicing and identification of a highly active promoter region
    • Misawa, H., Ishii, K. and Deguchi, T., Gene expression of mouse choline acetyltransferase. Alternative splicing and identification of a highly active promoter region. J. Biol. Chem., 267 (1992) 20392-20399.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20392-20399
    • Misawa, H.1    Ishii, K.2    Deguchi, T.3
  • 41
    • 0027537452 scopus 로고
    • Transcriptional regulation of choline acetyltransferase gene by cyclic AMP
    • Misawa, H., Takahashi, R. and Deguchi, T., Transcriptional regulation of choline acetyltransferase gene by cyclic AMP. J. Neurochem., 60 (1993) 1383-1387.
    • (1993) J. Neurochem. , vol.60 , pp. 1383-1387
    • Misawa, H.1    Takahashi, R.2    Deguchi, T.3
  • 42
    • 0028007336 scopus 로고
    • Activation of the mouse cytokeratin A (endoA) gene in teratocarcinoma F9 cells by the histone deacetylase inhibitor Trichostatin A
    • Miyashita, T., Yamamoto, H., Nishimune, Y., Nozaki, M., Morita, T. and Matsushiro, A., Activation of the mouse cytokeratin A (endoA) gene in teratocarcinoma F9 cells by the histone deacetylase inhibitor Trichostatin A. FEBS Lett., 353 (1994) 225-229.
    • (1994) FEBS Lett. , vol.353 , pp. 225-229
    • Miyashita, T.1    Yamamoto, H.2    Nishimune, Y.3    Nozaki, M.4    Morita, T.5    Matsushiro, A.6
  • 44
    • 0026641056 scopus 로고
    • Transcriptional regulation of prolactin receptor gene expression by sodium butyrate in MCF-7 human breast cancer cells
    • Ormandy, C.J., De Fazio, A., Kelly, P.A. and Sutherland, R.L., Transcriptional regulation of prolactin receptor gene expression by sodium butyrate in MCF-7 human breast cancer cells. Endocrinology, 131 (1992) 982-984.
    • (1992) Endocrinology , vol.131 , pp. 982-984
    • Ormandy, C.J.1    De Fazio, A.2    Kelly, P.A.3    Sutherland, R.L.4
  • 47
    • 0021016117 scopus 로고
    • Inhibition by sodium butyrate of enzyme induction by glucocorticoids and dibutyryl cyclic AMP
    • Plesko, M.M., Hargrove, J.L., Granner, D.K. and Chalkley, R. Inhibition by sodium butyrate of enzyme induction by glucocorticoids and dibutyryl cyclic AMP. J. Biol. Chem., 258 (1983) 13738-13744.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13738-13744
    • Plesko, M.M.1    Hargrove, J.L.2    Granner, D.K.3    Chalkley, R.4
  • 48
    • 0017291238 scopus 로고
    • Effect of sodium butyrate on mammalian cells in culture: A review
    • Prasad, K.N. and Shina, P.K., Effect of sodium butyrate on mammalian cells in culture: a review. In Vitro, 12 (1976) 125-132.
    • (1976) In Vitro , vol.12 , pp. 125-132
    • Prasad, K.N.1    Shina, P.K.2
  • 49
    • 0028323383 scopus 로고
    • Trans-activation by thyroid hormone receptors of the 5′ flanking region of the human ChAT gene
    • Quirin-Stricker, C., Nappey, V., Simoni, P., Toussaint, J.L. and Schmitt, M., Trans-activation by thyroid hormone receptors of the 5′ flanking region of the human ChAT gene. Mol. Brain Res., 23 (1994) 253-265.
    • (1994) Mol. Brain Res. , vol.23 , pp. 253-265
    • Quirin-Stricker, C.1    Nappey, V.2    Simoni, P.3    Toussaint, J.L.4    Schmitt, M.5
  • 50
    • 0023188027 scopus 로고
    • Comparison of the effects of elevated K ions and muscle-conditioned medium on the neurotransmitter phenotype of cultured sympathetic neurons
    • Raynaud, B., Clarous, D., Vidal, S., Ferrand, C. and Weber, M.J., Comparison of the effects of elevated K ions and muscle-conditioned medium on the neurotransmitter phenotype of cultured sympathetic neurons. Dev. Biol., 121 (1987) 548-558.
    • (1987) Dev. Biol. , vol.121 , pp. 548-558
    • Raynaud, B.1    Clarous, D.2    Vidal, S.3    Ferrand, C.4    Weber, M.J.5
  • 51
    • 0023117207 scopus 로고
    • The use of a tyrosine hydroxylase cDNA probe to study the neurotransmitter plasticity of rat sympathetic neurons in culture
    • Raynaud, B., Faucon-Biguet, N., Vidal, S., Mallet, J. and Weber, M.J., The use of a tyrosine hydroxylase cDNA probe to study the neurotransmitter plasticity of rat sympathetic neurons in culture. Dev. Biol., 119 (1987) 305-312.
    • (1987) Dev. Biol. , vol.119 , pp. 305-312
    • Raynaud, B.1    Faucon-Biguet, N.2    Vidal, S.3    Mallet, J.4    Weber, M.J.5
  • 52
    • 0025265458 scopus 로고
    • The induction of vimentin gene expression by sodium butyrate in human promonocytic leukemia U937 cells
    • Rius, C., Cabañas, C. and Aller, P., The induction of vimentin gene expression by sodium butyrate in human promonocytic leukemia U937 cells. Exp. Cell Res., 188 (1990) 129-134.
    • (1990) Exp. Cell Res. , vol.188 , pp. 129-134
    • Rius, C.1    Cabañas, C.2    Aller, P.3
  • 53
    • 0024521819 scopus 로고
    • Ciliary neurotrophic factor induces cholinergic differentiation of rat sympathetic neurons in culture
    • Saadat, S., Sendtner, M. and Rohrer, H., Ciliary neurotrophic factor induces cholinergic differentiation of rat sympathetic neurons in culture. J. Cell Biol., 108 (1989) 1807-1815.
    • (1989) J. Cell Biol. , vol.108 , pp. 1807-1815
    • Saadat, S.1    Sendtner, M.2    Rohrer, H.3
  • 54
    • 0018939305 scopus 로고
    • Thyroid hormone nuclear receptor levels are influenced by the acetylation of chromatin-associated proteins
    • Samuels, H.H., Stanley, F., Casanova, J. and Shao, T.C., Thyroid hormone nuclear receptor levels are influenced by the acetylation of chromatin-associated proteins. J. Biol. Chem., 255 (1980) 2499-2508.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2499-2508
    • Samuels, H.H.1    Stanley, F.2    Casanova, J.3    Shao, T.C.4
  • 55
    • 0028201770 scopus 로고
    • Gene expression within chromatin domain: The role of core histone hyperacetylation
    • Schlake, T., Klehr-Wirth, D., Yoshida, M., Beppu, T. and Bode, J., Gene expression within chromatin domain: the role of core histone hyperacetylation. Biochemistry, 33 (1994) 4197-4206.
    • (1994) Biochemistry , vol.33 , pp. 4197-4206
    • Schlake, T.1    Klehr-Wirth, D.2    Yoshida, M.3    Beppu, T.4    Bode, J.5
  • 56
    • 0027990579 scopus 로고
    • A previously unidentified choline acetyltransferase transcript in the human foetal brain
    • Schmitt, M., Garnier, J.M., Simoni, P. and Quirin-Stricker, C., A previously unidentified choline acetyltransferase transcript in the human foetal brain. Neurosci. Lett., 178 (1994) 225-226.
    • (1994) Neurosci. Lett. , vol.178 , pp. 225-226
    • Schmitt, M.1    Garnier, J.M.2    Simoni, P.3    Quirin-Stricker, C.4
  • 57
    • 0017864644 scopus 로고
    • The effect of sodium butyrate on histone modification
    • Sealy, L. and Chalkley, R., The effect of sodium butyrate on histone modification. Cell, 14 (1978) 115-121.
    • (1978) Cell , vol.14 , pp. 115-121
    • Sealy, L.1    Chalkley, R.2
  • 58
    • 0027263905 scopus 로고
    • Regulation of c-fos expression by sodium butyrate in the human colon carcinoma cell line Caco-2
    • Souleimani, A. and Asselin, C., Regulation of c-fos expression by sodium butyrate in the human colon carcinoma cell line Caco-2. Biochem. Biophys. Res. Comm., 193 (1993) 330-336.
    • (1993) Biochem. Biophys. Res. Comm. , vol.193 , pp. 330-336
    • Souleimani, A.1    Asselin, C.2
  • 59
    • 0027157441 scopus 로고
    • Regulation of c-myc expression by sodium butyrate in the colon carcinoma cell line Caco-2
    • Souleimani, A. and Asselin, C., Regulation of c-myc expression by sodium butyrate in the colon carcinoma cell line Caco-2. FEBS Lett., 326 (1993) 45-50.
    • (1993) FEBS Lett. , vol.326 , pp. 45-50
    • Souleimani, A.1    Asselin, C.2
  • 61
    • 0018801554 scopus 로고
    • Studies of the acetylation and deacetylation in high mobility group proteins: Identification of the sites of acetylation in HMG-1
    • Sterner, R., Vidali, G. and Allfrey, V.G., Studies of the acetylation and deacetylation in high mobility group proteins: identification of the sites of acetylation in HMG-1. J. Biol. Chem., 254 (1979) 11577-11583.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11577-11583
    • Sterner, R.1    Vidali, G.2    Allfrey, V.G.3
  • 62
    • 0026548820 scopus 로고
    • Morphological reversion of sis-transformed NIH3T3 cells by Trichostatin A
    • Sugita, K., Koizumi, K. and Yoshida, H., Morphological reversion of sis-transformed NIH3T3 cells by Trichostatin A. Cancer Res., 52 (1992) 168-172.
    • (1992) Cancer Res. , vol.52 , pp. 168-172
    • Sugita, K.1    Koizumi, K.2    Yoshida, H.3
  • 63
    • 0021736205 scopus 로고
    • Regulation of enzymes responsible for neurotransmitter synthesis and degradation in cultured rat sympathetic neurons. III. Effects of sodium butyrate
    • Swerts, J.P. and Weber, M.J., Regulation of enzymes responsible for neurotransmitter synthesis and degradation in cultured rat sympathetic neurons. III. Effects of sodium butyrate. Dev. Biol., 106 (1984) 282-288.
    • (1984) Dev. Biol. , vol.106 , pp. 282-288
    • Swerts, J.P.1    Weber, M.J.2
  • 64
    • 0021435705 scopus 로고
    • Regulation of enzymes responsible for neurotransmitter synthesis and degradation in cultured rat sympathetic neurons. II. Regulation of 16S acetylcholinesterase by conditioned medium
    • Swerts, J.P., Le Van Thai, A. and Weber, M.J., Regulation of enzymes responsible for neurotransmitter synthesis and degradation in cultured rat sympathetic neurons. II. Regulation of 16S acetylcholinesterase by conditioned medium. Dev. Biol., 103 (1984) 230-234.
    • (1984) Dev. Biol. , vol.103 , pp. 230-234
    • Swerts, J.P.1    Le Van Thai, A.2    Weber, M.J.3
  • 65
    • 0020858934 scopus 로고
    • Regulation of enzymes responsible for neurotransmitter synthesis and degradation in cultured rat sympathetic neurons. I. Effects of muscle conditioned medium
    • Swerts, J.P., Le Van Thai, A., Vigny, A. and Weber, M.J., Regulation of enzymes responsible for neurotransmitter synthesis and degradation in cultured rat sympathetic neurons. I. Effects of muscle conditioned medium. Dev. Biol., 100 (1983) 1-11.
    • (1983) Dev. Biol. , vol.100 , pp. 1-11
    • Swerts, J.P.1    Le Van Thai, A.2    Vigny, A.3    Weber, M.J.4
  • 66
    • 0019805374 scopus 로고
    • Selective inhibition by sodium butyrate of glucocorticoid-induced tyrosine aminotransferase synthesis in hepatoma tissue-cultured cells
    • Tichonicky, L. Santana-Calderon, M.A., Defer, N., Giesen, E.M., Beck, G. and Kruh, J., Selective inhibition by sodium butyrate of glucocorticoid-induced tyrosine aminotransferase synthesis in hepatoma tissue-cultured cells. Eur. J. Biochem., 120 (1981) 427-433.
    • (1981) Eur. J. Biochem. , vol.120 , pp. 427-433
    • Tichonicky, L.1    Santana-Calderon, M.A.2    Defer, N.3    Giesen, E.M.4    Beck, G.5    Kruh, J.6
  • 68
    • 0025779831 scopus 로고
    • Histone acetylation and control of gene expression
    • Turner, B.M., Histone acetylation and control of gene expression. J. Cell Sci., 99 (1991) 13-20.
    • (1991) J. Cell Sci. , vol.99 , pp. 13-20
    • Turner, B.M.1
  • 69
    • 0024790913 scopus 로고
    • The cholinergic neuronal differentiation factor from heart cells is identical to leukemia inhibitory factor
    • Yamamori, T., Fukada, K., Korsching, S. and Patterson, P.H., The cholinergic neuronal differentiation factor from heart cells is identical to Leukemia Inhibitory Factor. Science, 246 (1989) 1412-1416.
    • (1989) Science , vol.246 , pp. 1412-1416
    • Yamamori, T.1    Fukada, K.2    Korsching, S.3    Patterson, P.H.4
  • 70
    • 0023689244 scopus 로고
    • Reversible arrest of proliferation of rat 3Y1 fibroblasts in both the G1 and G2 phases by Trichostatin A
    • Yoshida, M. and Beppu, T., Reversible arrest of proliferation of rat 3Y1 fibroblasts in both the G1 and G2 phases by Trichostatin A. Exp. Cell Res., 177 (1988) 122-131.
    • (1988) Exp. Cell Res. , vol.177 , pp. 122-131
    • Yoshida, M.1    Beppu, T.2
  • 71
    • 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. and Beppu, T., Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by Trichostatin A. J. Biol. Chem., 265 (1990) 17174-17179.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 72
    • 0023195737 scopus 로고
    • Effects of Trichostatins on differentiation of murine erythroleukemia cells
    • Yoshida, M., Nomura, S. and Beppu, T., Effects of Trichostatins on differentiation of murine erythroleukemia cells. Cancer Res., 47 (1987) 3688-3691
    • (1987) Cancer Res. , vol.47 , pp. 3688-3691
    • Yoshida, M.1    Nomura, S.2    Beppu, T.3


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