메뉴 건너뛰기




Volumn 12, Issue 4, 2012, Pages 407-413

Downregulation of hypoxia-related responses by novel antitumor histone deacetylase inhibitors in MDAMB231 breast cancer cells

Author keywords

Angiogenesis; Anticancer drugs; Breast cancer; Carbonic anhydrase; Cell proliferation; Epigenetic regulation; Gene expression; Glucose transporter; Histone deacetylase inhibitors; Hypoxia; Hypoxia inducible factor (HIF) 1alpha; Metabolism; Transcription factors; Tumor microenvironment; Vascular endothelial growth factor

Indexed keywords

ANTINEOPLASTIC AGENT; CARBONATE DEHYDRATASE IX; FR 235222; GLUCOSE TRANSPORTER 1; HISTONE DEACETYLASE INHIBITOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; PROTEIN BNIP3; SYNAPSIN II; TETRAPEPTIDE; TRICHOSTATIN A; UNCLASSIFIED DRUG; VASCULOTROPIN; VORINOSTAT;

EID: 84860511076     PISSN: 18715206     EISSN: 18755992     Source Type: Journal    
DOI: 10.2174/187152012800228706     Document Type: Article
Times cited : (16)

References (48)
  • 1
    • 33745303045 scopus 로고    scopus 로고
    • Hypoxia signalling in cancer and approaches to enforce tumor regression
    • Pouyssegur, J.; Dayan, F.; Mazure, N. M. Hypoxia signalling in cancer and approaches to enforce tumor regression. Nature, 2006, 44 (7092), 437-443.
    • (2006) Nature , vol.44 , Issue.7092 , pp. 437-443
    • Pouyssegur, J.1    Dayan, F.2    Mazure, N.M.3
  • 2
    • 0842303171 scopus 로고    scopus 로고
    • HIF-1 and hypoxic response: The plot thickens
    • Poellinger, L.; Johnson, R. S. HIF-1 and hypoxic response: the plot thickens. Curr. Opin. Genet. Dev., 2004, 14(1), 81-85.
    • (2004) Curr. Opin. Genet. Dev , vol.14 , Issue.1 , pp. 81-85
    • Poellinger, L.1    Johnson, R.S.2
  • 4
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza, G. L. Targeting HIF-1 for cancer therapy. Nat. Rev. Cancer, 2003, 3(10), 721-732.
    • (2003) Nat. Rev. Cancer , vol.3 , Issue.10 , pp. 721-732
    • Semenza, G.L.1
  • 5
    • 0028068606 scopus 로고
    • Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1
    • Semenza, G. L.; Roth, P. H.; Fang, H.-M.; Wang, G. L. Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1. J. Biol. Chem., 1994, 269(38), 23757-23763.
    • (1994) J. Biol. Chem , vol.269 , Issue.38 , pp. 23757-23763
    • Semenza, G.L.1    Roth, P.H.2    Fang, H.-M.3    Wang, G.L.4
  • 6
    • 0038037735 scopus 로고    scopus 로고
    • Regulation of angiogenesis by hypoxia: Role of the HIF system
    • Pugh, C. W.; Ratcliffe, P. J. Regulation of angiogenesis by hypoxia: role of the HIF system. Nat. Med., 2003, 9(6), 677-684.
    • (2003) Nat. Med , vol.9 , Issue.6 , pp. 677-684
    • Pugh, C.W.1    Ratcliffe, P.J.2
  • 7
    • 0038788826 scopus 로고    scopus 로고
    • Hypoxia-induced gene expression occurs solely through the action of hypoxia-inducible factor 1alpha (HIF-1alpha): Role of cytoplasmic trapping of HIF-2alpha
    • Park, S. K.; Dadak, A. M.; Haase, V. H.; Fontana, L.; Giaccia, A. J.; Johnson, R. S. Hypoxia-induced gene expression occurs solely through the action of hypoxia-inducible factor 1alpha (HIF-1alpha): role of cytoplasmic trapping of HIF-2alpha. Mol. Cell Biol., 2003, 23(14), 4959-4971.
    • (2003) Mol. Cell Biol , vol.23 , Issue.14 , pp. 4959-4971
    • Park, S.K.1    Dadak, A.M.2    Haase, V.H.3    Fontana, L.4    Giaccia, A.J.5    Johnson, R.S.6
  • 9
    • 4644370374 scopus 로고    scopus 로고
    • Signalling via the hypoxia-inducible factor-1alpha requires multiple posttranslational modifications
    • Brahimi-Horn, C.; Mazure, N.; Pouyssegur, J. Signalling via the hypoxia-inducible factor-1alpha requires multiple posttranslational modifications. Cell Signal., 2005, 17(1), 1-9.
    • (2005) Cell Signal , vol.17 , Issue.1 , pp. 1-9
    • Brahimi-Horn, C.1    Mazure, N.2    Pouyssegur, J.3
  • 10
    • 33644780111 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1alpha
    • Kong, X.; Lin, Z.; Liang, D.; Fath, D.; Sang, N.; Caro, J. Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1alpha. Mol. Cell Biol., 2006, 26(6), 2019-2028.
    • (2006) Mol. Cell Biol , vol.26 , Issue.6 , pp. 2019-2028
    • Kong, X.1    Lin, Z.2    Liang, D.3    Fath, D.4    Sang, N.5    Caro, J.6
  • 11
    • 33749006252 scopus 로고    scopus 로고
    • Class II histone deacetylases are associated with VHL-independent regulation of hypoxiainducible factor 1 alpha
    • Qian, D. Z.; Kachhap, S. K.; Collis, S. J.; Verheul, H. M.; Carducci, M. A.; Atadja, P.; Pili, R. Class II histone deacetylases are associated with VHL-independent regulation of hypoxiainducible factor 1 alpha. Cancer Res., 2006, 66(17), 8814-8821.
    • (2006) Cancer Res , vol.66 , Issue.17 , pp. 8814-8821
    • Qian, D.Z.1    Kachhap, S.K.2    Collis, S.J.3    Verheul, H.M.4    Carducci, M.A.5    Atadja, P.6    Pili, R.7
  • 12
    • 4744368147 scopus 로고    scopus 로고
    • Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity
    • Kato, H.; Tamamizu-Kato, S.; Shibasaki, F. Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity. J. Biol. Chem., 2004, 279(40), 41966-41974.
    • (2004) J. Biol. Chem , vol.279 , Issue.40 , pp. 41966-41974
    • Kato, H.1    Tamamizu-Kato, S.2    Shibasaki, F.3
  • 14
    • 0037225763 scopus 로고    scopus 로고
    • Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1alpha activity
    • Mie, L. Y.; Kim, S. H.; Kim, H. S.; Jin, S. M.; Nakajima, H.; Jeong, K. H.; Kim, K. W. Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1alpha activity. Biochem. Biophys. Res. Commun., 2003, 300(1), 241-246.
    • (2003) Biochem. Biophys. Res. Commun , vol.300 , Issue.1 , pp. 241-246
    • Mie, L.Y.1    Kim, S.H.2    Kim, H.S.3    Jin, S.M.4    Nakajima, H.5    Jeong, K.H.6    Kim, K.W.7
  • 15
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon, V. M.; Sandhoff, T. W.; Rifkind, R. A.; Marks, P. A. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc. Natl. Acad. Sci. U. S. A, 2000, 97(18), 10014-10019.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , Issue.18 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 16
    • 33746338907 scopus 로고    scopus 로고
    • G1/S arrest induced by histone deacetylase inhibitor sodium butyrate in E1A + Rastransformed cells is mediated through down-regulation of E2F activity and stabilization of beta-catenin
    • Abramova, M. V.; Pospelova, T. V.; Nikulenkov, F. P.; Hollander, C. M.; Fornace, A. J., Jr.; Pospelov, V. A. G1/S arrest induced by histone deacetylase inhibitor sodium butyrate in E1A + Rastransformed cells is mediated through down-regulation of E2F activity and stabilization of beta-catenin. J. Biol. Chem., 2006, 281(30), 21040-21051.
    • (2006) J. Biol. Chem , vol.281 , Issue.30 , pp. 21040-21051
    • Abramova, M.V.1    Pospelova, T.V.2    Nikulenkov, F.P.3    Hollander, C.M.4    Fornace Jr., A.J.5    Pospelov, V.A.6
  • 17
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci, S.; Pelicci, P. G. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat. Rev. Cancer, 2006, 6(1), 38-51.
    • (2006) Nat. Rev. Cancer , vol.6 , Issue.1 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 18
    • 79251576774 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: The epigenetic therapeutics that repress hypoxia-inducible factors
    • Chen, S.; Sang, N. Histone deacetylase inhibitors: the epigenetic therapeutics that repress hypoxia-inducible factors. J. Biomed. Biotechnol., 2011, 2011, 197946.
    • (2011) J. Biomed. Biotechnol , pp. 197946
    • Chen, S.1    Sang, N.2
  • 19
    • 35048875691 scopus 로고    scopus 로고
    • Evaluation of HIF-1 inhibitors as anticancer agents
    • Semenza, G. L. Evaluation of HIF-1 inhibitors as anticancer agents. Drug Discov. Today, 2007, 12(19-20), 853-859.
    • (2007) Drug Discov. Today , vol.12 , Issue.19-20 , pp. 853-859
    • Semenza, G.L.1
  • 20
    • 67349201377 scopus 로고    scopus 로고
    • Targeting tumor angiogenesis with histone deacetylase inhibitors
    • Ellis, L.; Hammers, H.; Pili, R. Targeting tumor angiogenesis with histone deacetylase inhibitors. Cancer Lett., 2009, 280 (2), 145-153.
    • (2009) Cancer Lett , vol.280 , Issue.2 , pp. 145-153
    • Ellis, L.1    Hammers, H.2    Pili, R.3
  • 23
    • 78649648097 scopus 로고    scopus 로고
    • AS1387392, a novel immunosuppressive cyclic tetrapeptide compound with inhibitory activity against mammalian histone deacetylase
    • Sasamura, S.; Sakamoto, K.; Takagaki, S.; Yamada, T.; Takase, S.; Mori, H.; Fujii, T.; Hino, M.; Hashimoto, M. AS1387392, a novel immunosuppressive cyclic tetrapeptide compound with inhibitory activity against mammalian histone deacetylase. J. Antibiot. (Tokyo), 2010, 63(11), 633-636.
    • (2010) J. Antibiot. (Tokyo) , vol.63 , Issue.11 , pp. 633-636
    • Sasamura, S.1    Sakamoto, K.2    Takagaki, S.3    Yamada, T.4    Takase, S.5    Mori, H.6    Fujii, T.7    Hino, M.8    Hashimoto, M.9
  • 24
    • 0025807618 scopus 로고
    • 2 tension measurements
    • Vaupel, P.; Schlenger, K.; Knoop, C.; Höckel, M. Oxygenation of human tumors: evaluation of tissue oxygen distribution in breast cancers by computerized O2 tension measurements. Cancer Res., 1991, 51, 3316-3322.
    • (1991) Cancer Res , vol.51 , pp. 3316-3322
    • Vaupel, P.1    Schlenger, K.2    Knoop, C.3    Höckel, M.4
  • 25
    • 31144479698 scopus 로고    scopus 로고
    • Synthesis of 2-amino-8-oxodecanoic acids (Aodas) present in natural hystone deacetylase inhibitors
    • Rodriquez, M.; Bruno, I.; Cini, E.; Marchetti, M.; Taddei, M.; Gomez-Paloma, L. Synthesis of 2-amino-8-oxodecanoic acids (Aodas) present in natural hystone deacetylase inhibitors. J. Org. Chem., 2006, 71(1), 103-107.
    • (2006) J. Org. Chem , vol.71 , Issue.1 , pp. 103-107
    • Rodriquez, M.1    Bruno, I.2    Cini, E.3    Marchetti, M.4    Taddei, M.5    Gomez-Paloma, L.6
  • 26
    • 0030771005 scopus 로고    scopus 로고
    • Hypoxia affects cytokine production and proliferative responses by human peripheral mononuclear cells
    • Naldini, A.; Carraro, F.; Silvestri, S.; Bocci, V. Hypoxia affects cytokine production and proliferative responses by human peripheral mononuclear cells. J. Cell. Physiol., 1997, 173(3), 335-342.
    • (1997) J. Cell. Physiol , vol.173 , Issue.3 , pp. 335-342
    • Naldini, A.1    Carraro, F.2    Silvestri, S.3    Bocci, V.4
  • 27
    • 59149088848 scopus 로고    scopus 로고
    • Identification of a functional role for the protease-activated receptor-1 in hypoxic breast cancer cells
    • Naldini, A.; Filippi, I.; Ardinghi, C.; Silini, A.; Giavazzi, R.; Carraro, F. Identification of a functional role for the protease-activated receptor-1 in hypoxic breast cancer cells. Eur. J. Cancer, 2009, 45(3), 454-460.
    • (2009) Eur. J. Cancer , vol.45 , Issue.3 , pp. 454-460
    • Naldini, A.1    Filippi, I.2    Ardinghi, C.3    Silini, A.4    Giavazzi, R.5    Carraro, F.6
  • 28
    • 36248972186 scopus 로고    scopus 로고
    • Hypoxia influences the cellular crosstalk of human dermal fibroblasts. A proteomic approach
    • Boraldi, F.; Annovi, G.; Carraro, F.; Naldini, A.; Tiozzo, R.; Sommer, P.; Quaglino, D. Hypoxia influences the cellular crosstalk of human dermal fibroblasts. A proteomic approach. Biochim. Biophys. Acta, 2007, 1774(11), 1402-1413.
    • (2007) Biochim. Biophys. Acta , vol.1774 , Issue.11 , pp. 1402-1413
    • Boraldi, F.1    Annovi, G.2    Carraro, F.3    Naldini, A.4    Tiozzo, R.5    Sommer, P.6    Quaglino, D.7
  • 30
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • Vandesompele, J.; De, P. K.; Pattyn, F.; Poppe, B.; Van, R. N.; De, P. A.; Speleman, F. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol., 2002, 3(7), 1-12.
    • (2002) Genome Biol , vol.3 , Issue.7 , pp. 1-12
    • Vandesompele, J.1    De, P.K.2    Pattyn, F.3    Poppe, B.4    Van, R.N.5    De, P.A.6    Speleman, F.7
  • 32
    • 12244289602 scopus 로고    scopus 로고
    • A paradigm for therapy-induced microenvironmental changes in solid tumors leading to drug resistance
    • Yu, J. L.; Coomber, B. L.; Kerbel, R. S. A paradigm for therapy-induced microenvironmental changes in solid tumors leading to drug resistance. Differentiation, 2002, 70(9-10), 599-609.
    • (2002) Differentiation , vol.70 , Issue.9-10 , pp. 599-609
    • Yu, J.L.1    Coomber, B.L.2    Kerbel, R.S.3
  • 33
  • 34
    • 0026356726 scopus 로고
    • 2 tension measurements
    • Höckel, M.; Schlenger, K.; Knoop, C.; Vaupel, P. Oxygenation of carcinomas of the uterine cervix: evaluation by computerized O2 tension measurements. Cancer Res., 1991, 51, 6098-6102.
    • (1991) Cancer Res , vol.51 , pp. 6098-6102
    • Höckel, M.1    Schlenger, K.2    Knoop, C.3    Vaupel, P.4
  • 35
    • 0033552873 scopus 로고    scopus 로고
    • A human homologue of the checkpoint kinase Cds1 directly inhibits Cdc25 phosphatase
    • Blasina, A.; de Weyer, I. V.; Laus, M. C.; Luyten, W. H.; Parker, A. E.; McGowan, C. H. A human homologue of the checkpoint kinase Cds1 directly inhibits Cdc25 phosphatase. Curr. Biol., 1999, 9(1), 1-10.
    • (1999) Curr. Biol , vol.9 , Issue.1 , pp. 1-10
    • Blasina, A.1    de Weyer, I.V.2    Laus, M.C.3    Luyten, W.H.4    Parker, A.E.5    McGowan, C.H.6
  • 37
    • 0033233243 scopus 로고    scopus 로고
    • Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1
    • Semenza, G. L. Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1. Annu. Rev. Cell Dev. Biol., 1999, 15, 551-578.
    • (1999) Annu. Rev. Cell Dev. Biol , vol.15 , pp. 551-578
    • Semenza, G.L.1
  • 38
    • 36148954660 scopus 로고    scopus 로고
    • The role of the hypoxia-inducible BH3-only proteins BNIP3 and BNIP3L in cancer
    • Mellor, H. R.; Harris, A. L. The role of the hypoxia-inducible BH3-only proteins BNIP3 and BNIP3L in cancer. Cancer Metastasis Rev., 2007, 26(3-4), 553-566.
    • (2007) Cancer Metastasis Rev , vol.26 , Issue.3-4 , pp. 553-566
    • Mellor, H.R.1    Harris, A.L.2
  • 39
    • 66349121718 scopus 로고    scopus 로고
    • Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains
    • Bellot, G.; Garcia-Medina, R.; Gounon, P.; Chiche, J.; Roux, D.; Pouyssegur, J.; Mazure, N. M. Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains. Mol. Cell Biol., 2009, 29(10), 2570-2581.
    • (2009) Mol. Cell Biol , vol.29 , Issue.10 , pp. 2570-2581
    • Bellot, G.1    Garcia-Medina, R.2    Gounon, P.3    Chiche, J.4    Roux, D.5    Pouyssegur, J.6    Mazure, N.M.7
  • 42
    • 46749121459 scopus 로고    scopus 로고
    • Causes and consequences of increased glucose metabolism of cancers
    • Gillies, R. J.; Robey, I.; Gatenby, R. A. Causes and consequences of increased glucose metabolism of cancers. J. Nucl. Med., 2008, 49 Suppl 2, 24S-42S.
    • (2008) J. Nucl. Med , vol.49 , Issue.2 SUPPL.
    • Gillies, R.J.1    Robey, I.2    Gatenby, R.A.3
  • 43
    • 58249094845 scopus 로고    scopus 로고
    • Hypoxia-inducible carbonic anhydrase IX and XII promote tumor cell growth by counteracting acidosis through the regulation of the intracellular pH
    • Chiche, J.; Ilc, K.; Laferriere, J.; Trottier, E.; Dayan, F.; Mazure, N. M.; Brahimi-Horn, M. C.; Pouyssegur, J. Hypoxia-inducible carbonic anhydrase IX and XII promote tumor cell growth by counteracting acidosis through the regulation of the intracellular pH. Cancer Res., 2009, 69(1), 358-368.
    • (2009) Cancer Res , vol.69 , Issue.1 , pp. 358-368
    • Chiche, J.1    Ilc, K.2    Laferriere, J.3    Trottier, E.4    Dayan, F.5    Mazure, N.M.6    Brahimi-Horn, M.C.7    Pouyssegur, J.8
  • 45
    • 44449147036 scopus 로고    scopus 로고
    • Tumor cell metabolism: Cancer's Achilles' heel
    • Kroemer, G.; Pouyssegur, J. Tumor cell metabolism: cancer's Achilles' heel. Cancer Cell, 2008, 13(6), 472-482.
    • (2008) Cancer Cell , vol.13 , Issue.6 , pp. 472-482
    • Kroemer, G.1    Pouyssegur, J.2
  • 46
    • 0035117937 scopus 로고    scopus 로고
    • Tumor hypoxia, the physiological link between Trousseau's syndrome (carcinoma-induced coagulopathy) and metastasis
    • Denko, N. C.; Giaccia, A. J. Tumor hypoxia, the physiological link between Trousseau's syndrome (carcinoma-induced coagulopathy) and metastasis. Cancer Res., 2001, 61(3), 795-798.
    • (2001) Cancer Res , vol.61 , Issue.3 , pp. 795-798
    • Denko, N.C.1    Giaccia, A.J.2
  • 47
    • 0032053823 scopus 로고    scopus 로고
    • The unique physiology of solid tumors: Opportunities (and problems) for cancer therapy
    • Brown, J. M.; Giaccia, A. J. The unique physiology of solid tumors: opportunities (and problems) for cancer therapy. Cancer Res., 1998, 58, 1408-1416.
    • (1998) Cancer Res , vol.58 , pp. 1408-1416
    • Brown, J.M.1    Giaccia, A.J.2
  • 48
    • 16844379997 scopus 로고    scopus 로고
    • Immunosuppressive networks in the tumor environment and their therapeutic relevance
    • Zou, W. Immunosuppressive networks in the tumor environment and their therapeutic relevance. Nat. Rev. Cancer, 2005, 5(4), 263-274.
    • (2005) Nat. Rev. Cancer , vol.5 , Issue.4 , pp. 263-274
    • Zou, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.