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Volumn 5, Issue 10, 2015, Pages

Romidepsin targets multiple survival signaling pathways in malignant T cells

Author keywords

[No Author keywords available]

Indexed keywords

BETA CATENIN; DNA; HISTONE DEACETYLASE; HISTONE DEMETHYLASE; MAMMALIAN TARGET OF RAPAMYCIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; REACTIVE OXYGEN METABOLITE; ROMIDEPSIN; SECRETED FRIZZLED RELATED PROTEIN 1; STRESS ACTIVATED PROTEIN KINASE; ANTINEOPLASTIC AGENT; DEPSIPEPTIDE;

EID: 84989299928     PISSN: None     EISSN: 20445385     Source Type: Journal    
DOI: 10.1038/bcj.2015.83     Document Type: Article
Times cited : (52)

References (35)
  • 1
    • 0028258610 scopus 로고
    • Fr901228, a novel antitumor bicyclic depsipeptide produced by chromobacterium violaceum no. 968. I. Taxonomy, fermentation, isolation, physic-chemical and biological properties, and antitumor activity
    • Ueda H, Nakajima H, Hori Y, Fujita T, Nishimura M, Goto T et al. FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum No. 968. I. Taxonomy, fermentation, isolation, physic-chemical and biological properties, and antitumor activity. J Antibiot 1994; 47: 301-310.
    • (1994) J Antibiot , vol.47 , pp. 301-310
    • Ueda, H.1    Nakajima, H.2    Hori, Y.3    Fujita, T.4    Nishimura, M.5    Goto, T.6
  • 2
    • 0028299638 scopus 로고
    • Fr901228, a novel antitumor bicyclic depsipeptide produced by chromobacterium violaceum no. 968. II. Structure determination
    • Shigematsu N, Ueda H, Takase S, Tanaka H, Yamamoto K, Tada T. FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum No. 968. II. Structure determination. J Antibiot 1994; 47: 311-314.
    • (1994) J Antibiot , vol.47 , pp. 311-314
    • Shigematsu, N.1    Ueda, H.2    Takase, S.3    Tanaka, H.4    Yamamoto, K.5    Tada, T.6
  • 3
    • 38949140475 scopus 로고    scopus 로고
    • Romidepsin (depsipeptide) induced cell cycle arrest apoptosis and histone hyperacetylation in lung carcinoma cells ( a549) are associated with increase in p21 and hypophosphorylated retinoblastoma proteins expression
    • Vinodhkumar R, Song YS, Devaki T. Romidepsin (depsipeptide) induced cell cycle arrest, apoptosis and histone hyperacetylation in lung carcinoma cells (A549) are associated with increase in p21 and hypophosphorylated retinoblastoma proteins expression. Biomed Pharma 2008; 62: 85-93.
    • (2008) Biomed Pharma , vol.62 , pp. 85-93
    • Vinodhkumar, R.1    Song, Y.S.2    Devaki, T.3
  • 4
    • 77957023872 scopus 로고    scopus 로고
    • Romidepsin (fk228), a potent histone deacetylase inhibitor, induces apoptosis through the generation of hydrogen peroxide
    • Mizutani H, Hiraku Y, Tada-Oikawa S, Murata M, Ikemura K, Iwamoto T et al. Romidepsin (FK228), a potent histone deacetylase inhibitor, induces apoptosis through the generation of hydrogen peroxide. Cancer Sci 2010; 101: 2214-2219.
    • (2010) Cancer Sci , vol.101 , pp. 2214-2219
    • Mizutani, H.1    Hiraku, Y.2    Tada-Oikawa, S.3    Murata, M.4    Ikemura, K.5    Iwamoto, T.6
  • 5
    • 70349564782 scopus 로고    scopus 로고
    • Role of reactive oxygen species in proapoptotic ability of oncogenic h-ras to increase human bladder cancer cell susceptibility to histone deacetylase inhibitor for caspase induction
    • Choudhary S, Wang HC. Role of reactive oxygen species in proapoptotic ability of oncogenic H-Ras to increase human bladder cancer cell susceptibility to histone deacetylase inhibitor for caspase induction. J Cancer Res Clin Oncol 2009; 135: 1601-1613.
    • (2009) J Cancer Res Clin Oncol , vol.135 , pp. 1601-1613
    • Choudhary, S.1    Wang, H.C.2
  • 6
    • 9444238027 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor fr901228 induces caspase-dependent apoptosis via the mitochondrial pathway in small cell lung cancer cells
    • Doi S, Soda H, Oka M, Tsurutani J, Kitazaki T, Nakamura Y et al. The histone deacetylase inhibitor FR901228 induces caspase-dependent apoptosis via the mitochondrial pathway in small cell lung cancer cells. Mol Cancer Ther 2004; 3: 1397-1402.
    • (2004) Mol Cancer Ther , vol.3 , pp. 1397-1402
    • Doi, S.1    Soda, H.2    Oka, M.3    Tsurutani, J.4    Kitazaki, T.5    Nakamura, Y.6
  • 7
    • 15044343269 scopus 로고    scopus 로고
    • Suppression of phosphatidylinositol 3-kinase/akt signaling pathway is a determinant of the sensitivity to a novel histone deacetylase inhibitor, fk228, in lung adenocarcinoma cells
    • Kodani M, Igishi T, Matsumoto S, Chikumi H, Shigeoka Y, Nakanishi H et al. Suppression of phosphatidylinositol 3-kinase/Akt signaling pathway is a determinant of the sensitivity to a novel histone deacetylase inhibitor, FK228, in lung adenocarcinoma cells. Oncol Rep 2005; 13: 477-483.
    • (2005) Oncol Rep , vol.13 , pp. 477-483
    • Kodani, M.1    Igishi, T.2    Matsumoto, S.3    Chikumi, H.4    Shigeoka, Y.5    Nakanishi, H.6
  • 8
    • 84868207385 scopus 로고    scopus 로고
    • Romidepsin (fk228) and its analogs directly inhibit phosphatidylinositol 3-kinase activity and potently induce apoptosis as histone deacetylase/phosphatidylinositol 3-kinase dual inhibitors
    • Saijo K, Katoh T, Shimodaira H, Oda A, Takahashi O, Ishioka C. Romidepsin (FK228) and its analogs directly inhibit phosphatidylinositol 3-kinase activity and potently induce apoptosis as histone deacetylase/phosphatidylinositol 3-kinase dual inhibitors. Cancer Sci 2012; 103: 1994-2001.
    • (2012) Cancer Sci , vol.103 , pp. 1994-2001
    • Saijo, K.1    Katoh, T.2    Shimodaira, H.3    Oda, A.4    Takahashi, O.5    Ishioka, C.6
  • 9
    • 84931569035 scopus 로고    scopus 로고
    • Romidepsin in peripheral and cutaneous t-cell lymphoma: Mechanistic implications from clinical and correlative data
    • Bates SE, Eisch R, Ling A, Rosing D, Turner M, Pittaluga S et al. Romidepsin in peripheral and cutaneous T-cell lymphoma: mechanistic implications from clinical and correlative data. Br J Haematol 2015; 170: 96-109.
    • (2015) Br J Haematol , vol.170 , pp. 96-109
    • Bates, S.E.1    Eisch, R.2    Ling, A.3    Rosing, D.4    Turner, M.5    Pittaluga, S.6
  • 10
    • 0018817727 scopus 로고
    • Establishment and characterization of a new leukaemic t-cell line (peer) with an unusual phenotype
    • Ravid Z, Goldblum N, Zaizov R, Schlesinger M, Kertes T, Minowada J et al. Establishment and characterization of a new leukaemic T-cell line (Peer) with an unusual phenotype. Int J Cancer 1980; 25: 705-710.
    • (1980) Int J Cancer , vol.25 , pp. 705-710
    • Ravid, Z.1    Goldblum, N.2    Zaizov, R.3    Schlesinger, M.4    Kertes, T.5    Minowada, J.6
  • 11
    • 0022580334 scopus 로고
    • Cytogenetic and immunophenotypic analysis of cell lines established from patients with t cell leukemia/lymphoma
    • Smith SD, Morgan R, Link MP, McFall P, Hecht F. Cytogenetic and immunophenotypic analysis of cell lines established from patients with T cell leukemia/lymphoma. Blood 1986; 67: 650-656.
    • (1986) Blood , vol.67 , pp. 650-656
    • Smith, S.D.1    Morgan, R.2    Link, M.P.3    McFall, P.4    Hecht, F.5
  • 12
    • 77649186646 scopus 로고    scopus 로고
    • 5-Aza-2'-deoxycytidine sensitizes busulfan-resistant myeloid leukemia cells by regulating expression of genes involved in cell cycle checkpoint and apoptosis
    • Valdez BC, Li Y, Murray D, Corn P, Champlin RE, Andersson BS. 5-Aza-2'-deoxycytidine sensitizes busulfan-resistant myeloid leukemia cells by regulating expression of genes involved in cell cycle checkpoint and apoptosis. Leuk Res 2010; 34: 364-372.
    • (2010) Leuk Res , vol.34 , pp. 364-372
    • Valdez, B.C.1    Li, Y.2    Murray, D.3    Corn, P.4    Champlin, R.E.5    Andersson, B.S.6
  • 13
    • 84930480894 scopus 로고    scopus 로고
    • Comparison of the cytotoxicity of cladribine and clofarabine when combined with fludarabine and busulfan in AML cells: Enhancement of cytotoxicity with epigenetic modulators
    • Valdez BC, Li Y, Murray D, Ji J, Liu Y, Popat U et al. Comparison of the cytotoxicity of cladribine and clofarabine when combined with fludarabine and busulfan in AML cells: Enhancement of cytotoxicity with epigenetic modulators. Exp Hematol 2015; 43: 448-461.
    • (2015) Exp Hematol , vol.43 , pp. 448-461
    • Valdez, B.C.1    Li, Y.2    Murray, D.3    Ji, J.4    Liu, Y.5    Popat, U.6
  • 14
    • 78650722823 scopus 로고    scopus 로고
    • Physiological roles of class i hdac complex and histone demethylase
    • Hayakawa T, Nakayama J. Physiological roles of class I HDAC complex and histone demethylase. J Biomed Biotech 2011; 2011: 129383.
    • (2011) J Biomed Biotech , vol.2011 , pp. 129383
    • Hayakawa, T.1    Nakayama, J.2
  • 15
    • 59349089711 scopus 로고    scopus 로고
    • Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin
    • Creppe C, Malinouskaya L, Volvert ML, Gillard M, Close P, Malaise O et al. Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin. Cell 2009; 136: 551-564.
    • (2009) Cell , vol.136 , pp. 551-564
    • Creppe, C.1    Malinouskaya, L.2    Volvert, M.L.3    Gillard, M.4    Close, P.5    Malaise, O.6
  • 16
    • 84871745733 scopus 로고    scopus 로고
    • The coactivator role of histone deacetylase 3 in il-1-signaling involves deacetylation of p65 nf-?b
    • Ziesché E, Kettner-Buhrow D, Weber A, Wittwer T, Jurida L, Soelch J et al. The coactivator role of histone deacetylase 3 in IL-1-signaling involves deacetylation of p65 NF-?B. Nucleic Acids Res 2013; 41: 90-109.
    • (2013) Nucleic Acids Res , vol.41 , pp. 90-109
    • Ziesché, E.1    Kettner-Buhrow, D.2    Weber, A.3    Wittwer, T.4    Jurida, L.5    Soelch, J.6
  • 17
    • 23644434852 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Insights into mechanisms of lethality
    • Rosato RR, Grant S. Histone deacetylase inhibitors: insights into mechanisms of lethality. Expert Opin Ther Targets 2005; 9: 809-824.
    • (2005) Expert Opin Ther Targets , vol.9 , pp. 809-824
    • Rosato, R.R.1    Grant, S.2
  • 18
    • 33748427812 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors (hdi) cause DNA damage in leukemia cells: A mechanism for leukemia-specific hdi-dependent apoptosis?
    • Gaymes TJ, Padua RA, Pla M, Orr S, Omidvar N, Chomienne C et al. Histone deacetylase inhibitors (HDI) cause DNA damage in leukemia cells: a mechanism for leukemia-specific HDI-dependent apoptosis? Mol Cancer Res 2006; 4: 563-573.
    • (2006) Mol Cancer Res , vol.4 , pp. 563-573
    • Gaymes, T.J.1    Padua, R.A.2    Pla, M.3    Orr, S.4    Omidvar, N.5    Chomienne, C.6
  • 19
    • 77953170728 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase in cancer cells slows down replication forks, activates dormant origins, and induces DNA damage
    • Conti C, Leo E, Eichler GS, Sordet O, Martin MM, Fan A et al. Inhibition of histone deacetylase in cancer cells slows down replication forks, activates dormant origins, and induces DNA damage. Cancer Res 2010; 70: 4470-4480.
    • (2010) Cancer Res , vol.70 , pp. 4470-4480
    • Conti, C.1    Leo, E.2    Eichler, G.S.3    Sordet, O.4    Martin, M.M.5    Fan, A.6
  • 20
    • 0037155837 scopus 로고    scopus 로고
    • Direct activation of mitochondrial apoptosis machinery by c-jun n-terminal kinase in adult cardiac myocytes
    • Aoki H, Kang PM, Hampe J, Yoshimura K, Noma T, Matsuzaki M et al. Direct activation of mitochondrial apoptosis machinery by c-Jun N-terminal kinase in adult cardiac myocytes. J Biol Chem 2002; 277: 10244-10250.
    • (2002) J Biol Chem , vol.277 , pp. 10244-10250
    • Aoki, H.1    Kang, P.M.2    Hampe, J.3    Yoshimura, K.4    Noma, T.5    Matsuzaki, M.6
  • 21
    • 0027465942 scopus 로고
    • The promoter region of the yeast kar2 (bip) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum
    • Kohno K, Normington K, Sambrook J, Gething MJ, Mori K. The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol Cell Biol 1993; 13: 877-890.
    • (1993) Mol Cell Biol , vol.13 , pp. 877-890
    • Kohno, K.1    Normington, K.2    Sambrook, J.3    Gething, M.J.4    Mori, K.5
  • 22
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: Substrate interactions and functional properties
    • Ellgaard L, Ruddock LW. The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep 2005; 6: 28-32.
    • (2005) EMBO Rep , vol.6 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 23
    • 0026546365 scopus 로고
    • Chop a novel developmentally regulated nuclear protein that dimerizes with transcription factors c/ebp and lap and functions as a dominantnegative inhibitor of gene transcription
    • Ron D, Habener J. CHOP a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominantnegative inhibitor of gene transcription. Genes Dev 1992; 6: 439-453.
    • (1992) Genes Dev , vol.6 , pp. 439-453
    • Ron, D.1    Habener, J.2
  • 24
    • 84887620237 scopus 로고    scopus 로고
    • Er stress-induced cell death mechanisms
    • Sano R, Reed JC. ER stress-induced cell death mechanisms. Biochim Biophys Acta 2013; 1833: 3460-3470.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 3460-3470
    • Sano, R.1    Reed, J.C.2
  • 25
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox JS, Shamu CE, Walter P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 1993; 73: 1197-1206.
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 26
    • 84902438993 scopus 로고    scopus 로고
    • The traf3 adaptor protein drives proliferation of anaplastic large cell lymphoma cells by regulating multiple signaling pathways
    • Muro I, Fang G, Gardella KA, Mahajan IM, Wright CW. The TRAF3 adaptor protein drives proliferation of anaplastic large cell lymphoma cells by regulating multiple signaling pathways. Cell Cycle 2014; 13: 1918-1927.
    • (2014) Cell Cycle , vol.13 , pp. 1918-1927
    • Muro, I.1    Fang, G.2    Gardella, K.A.3    Mahajan, I.M.4    Wright, C.W.5
  • 28
    • 0036124896 scopus 로고    scopus 로고
    • Tcf: Lady justice casting the final verdict on the outcome of wnt signalling
    • Brantjes H, Barker N, van Es J, Clevers H. TCF: Lady Justice casting the final verdict on the outcome of Wnt signalling. Biol Chem 2002; 383: 255-261.
    • (2002) Biol Chem , vol.383 , pp. 255-261
    • Brantjes, H.1    Barker, N.2    Van Es, J.3    Clevers, H.4
  • 29
    • 0038783316 scopus 로고    scopus 로고
    • Secreted antagonists of the wnt signalling pathway
    • Kawano Y, Kypta R. Secreted antagonists of the Wnt signalling pathway. J Cell Sci 2003; 116: 2627-2634.
    • (2003) J Cell Sci , vol.116 , pp. 2627-2634
    • Kawano, Y.1    Kypta, R.2
  • 31
    • 84927155246 scopus 로고    scopus 로고
    • Matrine induces mitochondrial apoptosis in cisplatinresistant non-small cell lung cancer cells via suppression of β-catenin/surviving signaling
    • Wang HQ, Jin JJ, Wang J. Matrine induces mitochondrial apoptosis in cisplatinresistant non-small cell lung cancer cells via suppression of β-catenin/surviving signaling. Oncol Rep 2015; 33: 2561-2566.
    • (2015) Oncol Rep , vol.33 , pp. 2561-2566
    • Wang, H.Q.1    Jin, J.J.2    Wang, J.3
  • 32
    • 0034717270 scopus 로고    scopus 로고
    • Apoptosis-induced cleavage of beta-catenin by caspase-3 results in proteolytic fragments with reduced transactivation potential
    • Steinhusen U, Badock V, Bauer A, Behrens J, Wittman-Liebold B, Dörken B et al. Apoptosis-induced cleavage of beta-catenin by caspase-3 results in proteolytic fragments with reduced transactivation potential. J Biol Chem 2000; 26: 16345-16353.
    • (2000) J Biol Chem , vol.26 , pp. 16345-16353
    • Steinhusen, U.1    Badock, V.2    Bauer, A.3    Behrens, J.4    Wittman-Liebold, B.5    Dörken, B.6
  • 34
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action
    • Xu WS, Parmigiani RB, Marks PA. Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene 2007; 26: 5541-5552.
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 35
    • 84908265816 scopus 로고    scopus 로고
    • Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
    • Falkenberg KJ, Johnstone RW. Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders. Nat Rev Drug Discov 2014; 13: 673-691.
    • (2014) Nat Rev Drug Discov , vol.13 , pp. 673-691
    • Falkenberg, K.J.1    Johnstone, R.W.2


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