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Volumn 188, Issue 1-2, 2002, Pages 127-140

Induction and superinduction of growth arrest and DNA damage gene 45 (GADD45) α and β messenger RNAs by histone deacetylase inhibitors trichostatin A (TSA) and butyrate in SW620 human colon carcinoma cells

Author keywords

Apoptosis; Butyrate; Growth arrest and DNA damage gene 45 (GADD45); Histone deacetylase (HDAC); p21(cip waf); Trichostatin (TSA)

Indexed keywords

1 (5 ISOQUINOLINESULFONYL) 2 METHYLPIPERAZINE; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; BUTYRIC ACID; CURCUMIN; ETICYCLIDINE; HISTONE DEACETYLASE INHIBITOR; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; N (2 METHYLAMINOETHYL) 5 ISOQUINOLINESULFONAMIDE; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN P21; SB 242235; TRICHOSTATIN A; UNCLASSIFIED DRUG;

EID: 18644367141     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-3835(02)00322-1     Document Type: Article
Times cited : (82)

References (75)
  • 1
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo J., Su F., Chen D., Shiloh A., Gu W. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature. 408:2000;377-381.
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 2
    • 0032506542 scopus 로고    scopus 로고
    • Regulation of activity of the transcription factor GATA-1 by acetylation
    • Boyes J., Byfield P., Nakatani Y., Ogryzko V. Regulation of activity of the transcription factor GATA-1 by acetylation. Nature. 396:1998;594-598.
    • (1998) Nature , vol.396 , pp. 594-598
    • Boyes, J.1    Byfield, P.2    Nakatani, Y.3    Ogryzko, V.4
  • 3
    • 0031444009 scopus 로고    scopus 로고
    • Protein acetylation: More than chromatin modification to regulate transcription
    • Bayle J.H., Crabtree G.R. Protein acetylation: more than chromatin modification to regulate transcription. Chem. Biol. 4:1997;885-888.
    • (1997) Chem. Biol. , vol.4 , pp. 885-888
    • Bayle, J.H.1    Crabtree, G.R.2
  • 5
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression
    • Laherty C.D., Yang W.M., Sun J.M., Davie J.R., Seto E., Eisenman R.N. Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell. 89:1997;349-356.
    • (1997) Cell , vol.89 , pp. 349-356
    • Laherty, C.D.1    Yang, W.M.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5    Eisenman, R.N.6
  • 6
    • 0032142918 scopus 로고    scopus 로고
    • Role of histone acetylases and deacetylases in gene regulation
    • Kuo M.H., Allis C.D. Role of histone acetylases and deacetylases in gene regulation. Bioessay. 20:1998;615-626.
    • (1998) Bioessay , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 7
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylases, transcriptional control, and cancer
    • Cress W.D., Seto E. Histone deacetylases, transcriptional control, and cancer. J. Cell. Physiol. 184:2000;1-16.
    • (2000) J. Cell. Physiol. , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 8
    • 0035862199 scopus 로고    scopus 로고
    • The human histone deacetylase family
    • Gray S.G., Ekstrom T.J. The human histone deacetylase family. Exp. Cell Res. 262:2001;75-83.
    • (2001) Exp. Cell Res. , vol.262 , pp. 75-83
    • Gray, S.G.1    Ekstrom, T.J.2
  • 9
    • 0034596309 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Inducers of differentiation or apoptosis of transformed cells
    • Marks P.A., Richon V.M., Rifkind R.A. Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells. J. Natl. Cancer Inst. 92:2000;1210-1216.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1210-1216
    • Marks, P.A.1    Richon, V.M.2    Rifkind, R.A.3
  • 10
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton J., Hassig C.A., Schreiber S.L. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science. 272:1996;408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 11
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylase related to yeast Hda1p
    • Grozinger C.M., Hassig C.A., Schreiber S.L. Three proteins define a class of human histone deacetylase related to yeast Hda1p. Proc. Natl. Acad. Sci. USA. 96:1999;4868-4873.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 12
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family
    • Yang W.M., Yao Y.L., Sun J.M., Davie J.R., Seto E. Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J. Biol. Chem. 272:1997;28001-28007.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28001-28007
    • Yang, W.M.1    Yao, Y.L.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5
  • 17
    • 0036493156 scopus 로고    scopus 로고
    • Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain
    • Tong J.J., Liu J., Bertos N.R., Yang X.J. Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain. Nucleic Acids Res. 30:2002;1114-1123.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1114-1123
    • Tong, J.J.1    Liu, J.2    Bertos, N.R.3    Yang, X.J.4
  • 19
    • 0036479127 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel histone deacetylase HDAC10
    • Guardiola A.R., Yao T.P. Molecular cloning and characterization of a novel histone deacetylase HDAC10. J Biol. Chem. 277:2002;3350-3356.
    • (2002) J Biol. Chem. , vol.277 , pp. 3350-3356
    • Guardiola, A.R.1    Yao, T.P.2
  • 20
    • 0037016696 scopus 로고    scopus 로고
    • Isolation and chacterization of mammalian HDAC10, a novel histone deacetylase
    • Kao H.Y., Lee C.H., Komarov A., Han C.C., Evans R.M. Isolation and chacterization of mammalian HDAC10, a novel histone deacetylase. J. Biol. Chem. 277:2002;187-193.
    • (2002) J. Biol. Chem. , vol.277 , pp. 187-193
    • Kao, H.Y.1    Lee, C.H.2    Komarov, A.3    Han, C.C.4    Evans, R.M.5
  • 21
    • 0034597816 scopus 로고    scopus 로고
    • Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation
    • McKinsey T.A., Zhang C.L., Lu J., Olson E.N. Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation. Nature. 408:2000;46-47.
    • (2000) Nature , vol.408 , pp. 46-47
    • McKinsey, T.A.1    Zhang, C.L.2    Lu, J.3    Olson, E.N.4
  • 22
  • 23
    • 0034687741 scopus 로고    scopus 로고
    • Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase5
    • McKinsey T.A., Zhang C.L., Olson E.N. Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase5. Proc. Natl. Acad. Sci. USA. 97:2000;14400-14405.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14400-14405
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 24
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S., Armstrong C.M., Kaeberlein M., Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature. 403:2000;795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 26
    • 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. 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
  • 27
    • 0034721941 scopus 로고    scopus 로고
    • Inhibition of mitogenesis in Balb/c-3T3 cells by trichostatin A - Multiple alterations in the induction and activation of cyclin-cyclin-dependent kinase complexes
    • Wharton W., Savell J., Cress W.D., Seto E., Pledger W.J. Inhibition of mitogenesis in Balb/c-3T3 cells by trichostatin A - Multiple alterations in the induction and activation of cyclin-cyclin-dependent kinase complexes. J. Biol. Chem. 275:2000;33981-33987.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33981-33987
    • Wharton, W.1    Savell, J.2    Cress, W.D.3    Seto, E.4    Pledger, W.J.5
  • 28
    • 0025083327 scopus 로고
    • Structural specificity for biological activity of trichostatin A, a specific inhibitor of mammalian cell cycle with potent differentiation-inducing activity in Friend leukemia cells
    • Yoshida M., Hoshikawa Y., Koseki K., Mori K., Beppu T. Structural specificity for biological activity of trichostatin A, a specific inhibitor of mammalian cell cycle with potent differentiation-inducing activity in Friend leukemia cells. J. Antibiot. 43:1990;1101-1106.
    • (1990) J. Antibiot. , vol.43 , pp. 1101-1106
    • Yoshida, M.1    Hoshikawa, Y.2    Koseki, K.3    Mori, K.4    Beppu, T.5
  • 29
    • 0034901985 scopus 로고    scopus 로고
    • Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo
    • Vigushin D.M., Ali S., Pace P.E., Mirsaidi N., Ito K., Adcock I., Coombes R.C. Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo. Clin. Cancer Res. 7:2001;971-976.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 971-976
    • Vigushin, D.M.1    Ali, S.2    Pace, P.E.3    Mirsaidi, N.4    Ito, K.5    Adcock, I.6    Coombes, R.C.7
  • 30
    • 0029294663 scopus 로고
    • Trichostatin A and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function
    • Yoshida M., Horinouchi S., Beppu T. Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function. Bioessays. 17:1995;423-430.
    • (1995) Bioessays , vol.17 , pp. 423-430
    • Yoshida, M.1    Horinouchi, S.2    Beppu, T.3
  • 31
    • 0000032126 scopus 로고    scopus 로고
    • Depudecin induces morphological reversion of transformed fibroblast via the inhibition of histone deacetylase
    • Kwon H.J., Owa T., Hassig C.A., Shimada J., Schreiber S.L. Depudecin induces morphological reversion of transformed fibroblast via the inhibition of histone deacetylase. Proc. Natl. Acad. Sci. USA. 95:1998;3356-3361.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3356-3361
    • Kwon, H.J.1    Owa, T.2    Hassig, C.A.3    Shimada, J.4    Schreiber, S.L.5
  • 32
    • 0030796349 scopus 로고    scopus 로고
    • Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): Dependence on protein synthesis and synergy with mitochondiral/cytochrome c-dependent pathway
    • Medina V., Edmonds B., Young G.P., James R., Appleton S., Zalewski P.D. Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): dependence on protein synthesis and synergy with mitochondiral/cytochrome c-dependent pathway. Cancer Res. 57:1997;3697-3707.
    • (1997) Cancer Res. , vol.57 , pp. 3697-3707
    • Medina, V.1    Edmonds, B.2    Young, G.P.3    James, R.4    Appleton, S.5    Zalewski, P.D.6
  • 33
    • 0034634635 scopus 로고    scopus 로고
    • Rapid induction of histone hyperacetylation and cellular differentiation in human breast tumor cell lines following degradation of histone deacetylase-1
    • Zhou Q., Melkoumian Z.K., Lucktong A., Moniwa M., Davie J.R., Strobl J.S. Rapid induction of histone hyperacetylation and cellular differentiation in human breast tumor cell lines following degradation of histone deacetylase-1. J. Biol. Chem. 275:2000;35256-35263.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35256-35263
    • Zhou, Q.1    Melkoumian, Z.K.2    Lucktong, A.3    Moniwa, M.4    Davie, J.R.5    Strobl, J.S.6
  • 35
    • 0032879920 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors are the potent inducer/enhancer of differentiation in acute myeloid leukemia: A new approach to anti-leukemia therapy
    • Kosugi H., Towatari M., Hatano S., Kitamura K., Kiyoi H., Kinoshita T., Tanimoto M., Murate T., Kawashima K., Saito H., Naoe T. Histone deacetylase inhibitors are the potent inducer/enhancer of differentiation in acute myeloid leukemia: a new approach to anti-leukemia therapy. Leukemia. 13:1999;1316-1324.
    • (1999) Leukemia , vol.13 , pp. 1316-1324
    • Kosugi, H.1    Towatari, M.2    Hatano, S.3    Kitamura, K.4    Kiyoi, H.5    Kinoshita, T.6    Tanimoto, M.7    Murate, T.8    Kawashima, K.9    Saito, H.10    Naoe, T.11
  • 36
    • 0034105047 scopus 로고    scopus 로고
    • Butyrate and trichostatin A effects on the proliferation/differentiation of human intestinal epithelial cells: Induction of cyclin D3 and p21 expression
    • Siavoshian S., Segain J.P., Kornprobst M., Bonnet C., Cherbut C., Galmiche J.P., Blottiere H.M. Butyrate and trichostatin A effects on the proliferation/differentiation of human intestinal epithelial cells: induction of cyclin D3 and p21 expression. Gut. 46:2000;507-514.
    • (2000) Gut , vol.46 , pp. 507-514
    • Siavoshian, S.1    Segain, J.P.2    Kornprobst, M.3    Bonnet, C.4    Cherbut, C.5    Galmiche, J.P.6    Blottiere, H.M.7
  • 37
    • 0033562343 scopus 로고    scopus 로고
    • Both Sp1 and Sp3 are responsible for p21(waf1) promoter activity induced by histone deacetylase inhibitor in NIH3T3 cells
    • Xiao H.Y., Hasegawa T., Isobe K. Both Sp1 and Sp3 are responsible for p21(waf1) promoter activity induced by histone deacetylase inhibitor in NIH3T3 cells. J. Cell. Biochem. 73:1999;291-302.
    • (1999) J. Cell. Biochem. , vol.73 , pp. 291-302
    • Xiao, H.Y.1    Hasegawa, T.2    Isobe, K.3
  • 38
    • 0031577480 scopus 로고    scopus 로고
    • Sodium butyrate induces NIH3T3 cells to senescence-like state and enhance promoter activity of p21 (waf/cip) in p53-independent manner
    • Xiao H.Y., Hasegawa T., Miyaishi O., Ohkusu K., Isobe K. Sodium butyrate induces NIH3T3 cells to senescence-like state and enhance promoter activity of p21 (waf/cip) in p53-independent manner. Biochem. Biophys. Res. Commun. 237:1997;457-460.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 457-460
    • Xiao, H.Y.1    Hasegawa, T.2    Miyaishi, O.3    Ohkusu, K.4    Isobe, K.5
  • 40
    • 0032499756 scopus 로고    scopus 로고
    • P21(Waf1) is required for butyrate-mediated growth inhibition of human colon cancer cells
    • Archer S.Y., Meng S.F., Shei A., Hodin R.A. P21(Waf1) is required for butyrate-mediated growth inhibition of human colon cancer cells. Proc. Natl. Acad. Sci. USA. 95:1998;6791-6796.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6791-6796
    • Archer, S.Y.1    Meng, S.F.2    Shei, A.3    Hodin, R.A.4
  • 41
  • 42
    • 0031596491 scopus 로고    scopus 로고
    • Butyrate-induced G(1) arrest results from P21-independent disruption of retinoblastoma protein-mediated signals
    • Vaziri C., Stice L., Faller D.V. Butyrate-induced G(1) arrest results from P21-independent disruption of retinoblastoma protein-mediated signals. Cell Growth Differ. 9:1998;465-474.
    • (1998) Cell Growth Differ. , vol.9 , pp. 465-474
    • Vaziri, C.1    Stice, L.2    Faller, D.V.3
  • 43
    • 0033767848 scopus 로고    scopus 로고
    • Mechanism of cell cycle arrest caused by histone deacetylase inhibitors in human carcinoma cells
    • Kim Y.B., Ki S.W., Yoshida M., Horinouchi S. Mechanism of cell cycle arrest caused by histone deacetylase inhibitors in human carcinoma cells. J. Antibiot. 53:2000;1191-1200.
    • (2000) J. Antibiot. , vol.53 , pp. 1191-1200
    • Kim, Y.B.1    Ki, S.W.2    Yoshida, M.3    Horinouchi, S.4
  • 45
    • 0034672294 scopus 로고    scopus 로고
    • Effect of trichostatin A on cell growth and expression of cell cycle- and apoptosis-related molecules in human gastric and oral carcinoma cell lines
    • Suzuki T., Yokozaki H., Kuniyasu H., Hayashi K., Naka K., Ono S., Ishikawa T., Tahara E., Yasui W. Effect of trichostatin A on cell growth and expression of cell cycle- and apoptosis-related molecules in human gastric and oral carcinoma cell lines. Int. J. Cancer. 88:2000;992-997.
    • (2000) Int. J. Cancer , vol.88 , pp. 992-997
    • Suzuki, T.1    Yokozaki, H.2    Kuniyasu, H.3    Hayashi, K.4    Naka, K.5    Ono, S.6    Ishikawa, T.7    Tahara, E.8    Yasui, W.9
  • 46
    • 0022930702 scopus 로고
    • Inducibility of kappa immunogobulin enhancer-binding protein NF-kappa B by posttranslational mechanism
    • Sen R., Baltimore D. Inducibility of kappa immunogobulin enhancer-binding protein NF-kappa B by posttranslational mechanism. Cell. 47:1986;921-928.
    • (1986) Cell , vol.47 , pp. 921-928
    • Sen, R.1    Baltimore, D.2
  • 47
    • 0025769412 scopus 로고
    • Primary response genes induced by growth factor and tumor promoters
    • Herschman H.R. Primary response genes induced by growth factor and tumor promoters. Annu. Rev. Biochem. 60:1991;281-319.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 281-319
    • Herschman, H.R.1
  • 48
    • 0030051916 scopus 로고    scopus 로고
    • Superinduction of NF-kappa B by actinomycin D and cyclohexamide in epithelial cells
    • Newton R., Adcock I.M., Barnes P.J. Superinduction of NF-kappa B by actinomycin D and cyclohexamide in epithelial cells. Biochem. Biophys. Res. Commun. 218:1996;518-523.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 518-523
    • Newton, R.1    Adcock, I.M.2    Barnes, P.J.3
  • 50
    • 0033613436 scopus 로고    scopus 로고
    • Inhibition of cyclo-oxygenase 2 expression in colon cells by the chemopreventive agent curcumin involves inhibition of NF-kappaB activation via the NIK/IKK signalling complex
    • Plummer S.M., Holloway K.A., Manson M.M., Munks R.J., Kaptein A., Farrow S., Howells L. Inhibition of cyclo-oxygenase 2 expression in colon cells by the chemopreventive agent curcumin involves inhibition of NF-kappaB activation via the NIK/IKK signalling complex. Oncogene. 18:1999;6013-6020.
    • (1999) Oncogene , vol.18 , pp. 6013-6020
    • Plummer, S.M.1    Holloway, K.A.2    Manson, M.M.3    Munks, R.J.4    Kaptein, A.5    Farrow, S.6    Howells, L.7
  • 51
    • 0032055394 scopus 로고    scopus 로고
    • Inhibition of nuclear factor kappaB by direct modification in whole cells - Mechanism of action of nordihydroguaiaritic acid, curcumin and thiol modifiers
    • Brennan P., O'Neill L.A. Inhibition of nuclear factor kappaB by direct modification in whole cells - Mechanism of action of nordihydroguaiaritic acid, curcumin and thiol modifiers. Biochem. Pharmacol. 55:1998;965-973.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 965-973
    • Brennan, P.1    O'Neill, L.A.2
  • 52
    • 0033615543 scopus 로고    scopus 로고
    • Role of the cyclic AMP-protein kinase A pathway in lipopolysaccharide-induced nitric oxide synthase expression in RAW264.7 macrophages. Involvement of cyclooxygenase-2′
    • Chen C.C., Chiu K., Y T., Sun T., Chen W.C. Role of the cyclic AMP-protein kinase A pathway in lipopolysaccharide-induced nitric oxide synthase expression in RAW264.7 macrophages. Involvement of cyclooxygenase-2′ J. Biol. Chem. 274:1999;31559-31564.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31559-31564
    • Chen, C.C.1    Chiu, K.Y.T.2    Sun, T.3    Chen, W.C.4
  • 53
    • 0031716184 scopus 로고    scopus 로고
    • Curcumin induces a P53-dependent apoptosis in human basal cell carcinoma cells
    • Jee S.H., Shen S.C., Tseng C.R., Chiu H.C., Kuo M.L. Curcumin induces a P53-dependent apoptosis in human basal cell carcinoma cells. J. Invest. Dermatol. 111:1998;656-661.
    • (1998) J. Invest. Dermatol. , vol.111 , pp. 656-661
    • Jee, S.H.1    Shen, S.C.2    Tseng, C.R.3    Chiu, H.C.4    Kuo, M.L.5
  • 54
    • 0034982359 scopus 로고    scopus 로고
    • In vivo effects of a histone deacetylase inhibitor, FK228, on human acute promyelocytic leukemia in NOD/Shi-scid/scid mice
    • Kosugi H., Ito M., Yamamoto Y., Towatari M., Ito M., Ueda R., Saito H., Naoe T. In vivo effects of a histone deacetylase inhibitor, FK228, on human acute promyelocytic leukemia in NOD/Shi-scid/scid mice. Jpn. J. Cancer Res. 92:2001;529-536.
    • (2001) Jpn. J. Cancer Res. , vol.92 , pp. 529-536
    • Kosugi, H.1    Ito, M.2    Yamamoto, Y.3    Towatari, M.4    Ito, M.5    Ueda, R.6    Saito, H.7    Naoe, T.8
  • 55
    • 0034596309 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Inducers of differentiation or apoptosis of transformed cells
    • Marks P.A., Richon V.M., Rifkind R.A. Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells. J. Natl. Cancer Inst. 92:2000;1210-1216.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1210-1216
    • Marks, P.A.1    Richon, V.M.2    Rifkind, R.A.3
  • 56
    • 0344995285 scopus 로고    scopus 로고
    • Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0
    • Hobbs W.E. 2nd, DeLuca N.A. Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0. J. Virol. 73:1999;8245-8255.
    • (1999) J. Virol. , vol.73 , pp. 8245-8255
    • Hobbs W.E. II1    DeLuca, N.A.2
  • 57
    • 0034490876 scopus 로고    scopus 로고
    • Butyrate as a model for 'gene-regulating chemoprevention and chemotherapy'
    • Sowa Y., Sakai T. Butyrate as a model for 'gene-regulating chemoprevention and chemotherapy'. Biofactors. 12:2000;283-287.
    • (2000) Biofactors , vol.12 , pp. 283-287
    • Sowa, Y.1    Sakai, T.2
  • 59
    • 0033964512 scopus 로고    scopus 로고
    • P300 collaborates with Sp1 and Sp3 in p21(waf1/cip1) promoter activation induced by histone deacetylase inhibitor
    • Xiao H.Y., Hasegawa T., Isobe K. p300 collaborates with Sp1 and Sp3 in p21(waf1/cip1) promoter activation induced by histone deacetylase inhibitor. J. Biol. Chem. 275:2000;1371-1376.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1371-1376
    • Xiao, H.Y.1    Hasegawa, T.2    Isobe, K.3
  • 65
    • 0031946364 scopus 로고    scopus 로고
    • Tumor suppressor P53 can participate in transcriptional induction of the GADD45 promoter in the absence of direct DNA binding
    • Zhan Q.M., Chen I.T., Antinore M.J., Fornace A.J. Tumor suppressor P53 can participate in transcriptional induction of the GADD45 promoter in the absence of direct DNA binding. Mol. Cell Biol. 18:1998;2768-2778.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 2768-2778
    • Zhan, Q.M.1    Chen, I.T.2    Antinore, M.J.3    Fornace, A.J.4
  • 68
    • 0035110714 scopus 로고    scopus 로고
    • Involvement of the Oct-1 regulatory element of the gadd45 promoter in the p53-independent response to ultraviolet irradiation
    • Takahashi S., Saito S., Ohtani N., Sakai T. Involvement of the Oct-1 regulatory element of the gadd45 promoter in the p53-independent response to ultraviolet irradiation. Cancer Res. 61:2001;1187-1195.
    • (2001) Cancer Res. , vol.61 , pp. 1187-1195
    • Takahashi, S.1    Saito, S.2    Ohtani, N.3    Sakai, T.4
  • 71
    • 0028793807 scopus 로고
    • GADD45 is a nuclear cell cycle regulated protein which interacts with P21(Cip1)
    • Kearsey J.M., Coates P.J., Prescott A.R., Warbrick E., Hall P.A. GADD45 is a nuclear cell cycle regulated protein which interacts with P21(Cip1). Oncogene. 11:1995;1675-1683.
    • (1995) Oncogene , vol.11 , pp. 1675-1683
    • Kearsey, J.M.1    Coates, P.J.2    Prescott, A.R.3    Warbrick, E.4    Hall, P.A.5
  • 73
    • 0029922537 scopus 로고    scopus 로고
    • The differentiation primary response gene MYD118, related to GADD45 encodes for a nuclear protein which interacts with PCNA and p21 WAF/CIP1
    • Vairapandi M., Ballier A.G., Fornace A.J.J., Hoffman B., Libermann D.A. The differentiation primary response gene MYD118, related to GADD45 encodes for a nuclear protein which interacts with PCNA and p21 WAF/CIP1. Oncogene. 12:1996;2579-2594.
    • (1996) Oncogene , vol.12 , pp. 2579-2594
    • Vairapandi, M.1    Ballier, A.G.2    Fornace, A.J.J.3    Hoffman, B.4    Libermann, D.A.5
  • 75
    • 0032520755 scopus 로고    scopus 로고
    • Evidence for distinct kinase-mediated pathways in GADD gene responses
    • Carrier F., Zhan Q.M., Alamo I., Hanaoka F., Fornace A.J. Evidence for distinct kinase-mediated pathways in GADD gene responses. Biochem. Pharm. 55:1998;853-861.
    • (1998) Biochem. Pharm. , vol.55 , pp. 853-861
    • Carrier, F.1    Zhan, Q.M.2    Alamo, I.3    Hanaoka, F.4    Fornace, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.