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Volumn 20, Issue 1-2, 2015, Pages 119-137

Histone deacetylases and cancer-associated angiogenesis: Current understanding of the biology and clinical perspectives

Author keywords

HDAC; Inhibitors; Preclinical; Sirtuins

Indexed keywords

ANGIOGENESIS INHIBITOR; BELINOSTAT; BEVACIZUMAB; CARBOPLATIN; CEDIRANIB; DACINOSTAT; DOCETAXEL; ENTINOSTAT; GEMCITABINE; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; IRINOTECAN; PACLITAXEL; PANOBINOSTAT; ROMIDEPSIN; TEMOZOLOMIDE; VALPROIC ACID; VATALANIB; VORINOSTAT;

EID: 84922763973     PISSN: 08939675     EISSN: 21626448     Source Type: Journal    
DOI: 10.1615/CritRevOncog.2014012423     Document Type: Article
Times cited : (21)

References (123)
  • 1
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey VG, Faulkner R, Mirsky AE. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci U S A. 1964;51:786–94.
    • (1964) Proc Natl Acad Sci U S A , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 2
    • 0035962644 scopus 로고    scopus 로고
    • Histone deacetylases: A common molecular target for differentiation treatment of acute myeloid leukemias?
    • Minucci S, Nervi C, Lo Coco F, Pelicci PG. Histone deacetylases: a common molecular target for differentiation treatment of acute myeloid leukemias? Oncogene. 2001;20(24):3110–5.
    • (2001) Oncogene , vol.20 , Issue.24 , pp. 3110-3115
    • Minucci, S.1    Nervi, C.2    Lo Coco, F.3    Pelicci, P.G.4
  • 3
    • 49249116407 scopus 로고    scopus 로고
    • A work in progress: The clinical development of histone deacetylase inhibitors
    • Marsoni S, Damia G, Camboni G. A work in progress: the clinical development of histone deacetylase inhibitors. Epigenetics. 2008;3(3):164–71.
    • (2008) Epigenetics , vol.3 , Issue.3 , pp. 164-171
    • Marsoni, S.1    Damia, G.2    Camboni, G.3
  • 4
    • 77955643796 scopus 로고    scopus 로고
    • The clinical development of histone deacetylase inhibitors as targeted anticancer drugs
    • Marks PA. The clinical development of histone deacetylase inhibitors as targeted anticancer drugs. Expert Opin Investig Drugs. 2010;19(9):1049–66.
    • (2010) Expert Opin Investig Drugs , vol.19 , Issue.9 , pp. 1049-1066
    • Marks, P.A.1
  • 7
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (And more) treatments for cancer
    • Minucci S, Pelicci PG. 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
  • 8
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • Gregoretti IV, Lee YM, Goodson HV. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J Mol Biol. 2004;338(1):17–31.
    • (2004) J Mol Biol , vol.338 , Issue.1 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 10
    • 36048958965 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Overview and perspectives
    • Dokmanovic M, Clarke C, Marks PA. Histone deacetylase inhibitors: overview and perspectives. Mol Cancer Res. 2007;5(10):981–9.
    • (2007) Mol Cancer Res , vol.5 , Issue.10 , pp. 981-989
    • Dokmanovic, M.1    Clarke, C.2    Marks, P.A.3
  • 11
    • 84875163565 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors suppress mutant p53 transcription via histone deacetylase 8
    • Yan W, Liu S, Xu E, Zhang J, Zhang Y, Chen X. Histone deacetylase inhibitors suppress mutant p53 transcription via histone deacetylase 8. Oncogene. 2013;32(5): 599–609.
    • (2013) Oncogene , vol.32 , Issue.5 , pp. 599-609
    • Yan, W.1    Liu, S.2    Xu, E.3    Zhang, J.4    Zhang, Y.5    Chen, X.6
  • 13
    • 4544358659 scopus 로고    scopus 로고
    • Histone deacetylases 5 and 9 govern responsiveness of the heart to a subset of stress signals and play redundant roles in heart development
    • Chang S, McKinsey TA, Zhang CL, Richardson JA, Hill JA, Olson EN. Histone deacetylases 5 and 9 govern responsiveness of the heart to a subset of stress signals and play redundant roles in heart development. Mol Cell Biol. 2004;24(19):8467–76.
    • (2004) Mol Cell Biol , vol.24 , Issue.19 , pp. 8467-8476
    • Chang, S.1    McKinsey, T.A.2    Zhang, C.L.3    Richardson, J.A.4    Hill, J.A.5    Olson, E.N.6
  • 14
    • 33746228132 scopus 로고    scopus 로고
    • Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10
    • Chang S, Young BD, Li S, Qi X, Richardson JA, Olson EN. Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10. Cell. 2006;126(2):321–334.
    • (2006) Cell , vol.126 , Issue.2 , pp. 321-334
    • Chang, S.1    Young, B.D.2    Li, S.3    Qi, X.4    Richardson, J.A.5    Olson, E.N.6
  • 15
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, Yao TP. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell. 2003;115(6):727–38.
    • (2003) Cell , vol.115 , Issue.6 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.P.6
  • 16
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander G, Guarente L. The Sir2 family of protein deacetylases. Annu Rev Biochem. 2004;73:417–35.
    • (2004) Annu Rev Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 18
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell. 2003;11(2):437–47.
    • (2003) Mol Cell , vol.11 , Issue.2 , pp. 437-447
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 19
    • 78649738291 scopus 로고    scopus 로고
    • SIRT2 regulates NF-κB dependent gene expression through deacetylation of p65 Lys310
    • Rothgiesser KM, Erener S, Waibel S, Lüscher B, Hottiger MO. SIRT2 regulates NF-κB dependent gene expression through deacetylation of p65 Lys310. J Cell Sci. 2010;123(Pt 24):4251–8.
    • (2010) J Cell Sci , vol.123 , pp. 4251-4258
    • Rothgiesser, K.M.1    Erener, S.2    Waibel, S.3    Lüscher, B.4    Hottiger, M.O.5
  • 23
    • 50149103440 scopus 로고    scopus 로고
    • Substrates and regulation mechanisms for the human mito-chondrial sirtuins Sirt3 and Sirt5
    • Schlicker C, Gertz M, Papatheodorou P, Kachholz B, Becker CF, Steegborn C. Substrates and regulation mechanisms for the human mito-chondrial sirtuins Sirt3 and Sirt5. J Mol Biol. 2008;382(3):790–801.
    • (2008) J Mol Biol , vol.382 , Issue.3 , pp. 790-801
    • Schlicker, C.1    Gertz, M.2    Papatheodorou, P.3    Kachholz, B.4    Becker, C.F.5    Steegborn, C.6
  • 25
    • 79958755721 scopus 로고    scopus 로고
    • Kinetic folding mechanism of an integral membrane protein examined by pulsed oxidative labeling and mass spectrometry
    • Pan Y, Brown L, Konermann L. Kinetic folding mechanism of an integral membrane protein examined by pulsed oxidative labeling and mass spectrometry. J Mol Biol. 2011;410(1):146–58.
    • (2011) J Mol Biol , vol.410 , Issue.1 , pp. 146-158
    • Pan, Y.1    Brown, L.2    Konermann, L.3
  • 27
    • 84859541677 scopus 로고    scopus 로고
    • Suppression of histone deacetylase 11 promotes expression of IL-10 in Kupffer cells and induces tolerance following orthotopic liver transplantation in rats
    • Lian ZR, Xu YF, Wang XB, Gong JP, Liu ZJ. Suppression of histone deacetylase 11 promotes expression of IL-10 in Kupffer cells and induces tolerance following orthotopic liver transplantation in rats. J Surg Res. 2012;174(2):359–68.
    • (2012) J Surg Res , vol.174 , Issue.2 , pp. 359-368
    • Lian, Z.R.1    Xu, Y.F.2    Wang, X.B.3    Gong, J.P.4    Liu, Z.J.5
  • 28
    • 79953084657 scopus 로고    scopus 로고
    • HDAC11 plays an essential role in regulating OX40 ligand expression in Hodgkin lymphoma
    • Buglio D, Khaskhely NM, Voo KS, Martinez-Valdez H, Liu YJ, Younes A. HDAC11 plays an essential role in regulating OX40 ligand expression in Hodgkin lymphoma. Blood. 2011;117(10):2910–7.
    • (2011) Blood , vol.117 , Issue.10 , pp. 2910-2917
    • Buglio, D.1    Khaskhely, N.M.2    Voo, K.S.3    Martinez-Valdez, H.4    Liu, Y.J.5    Younes, A.6
  • 29
    • 21244456772 scopus 로고    scopus 로고
    • Complicated tails: Histone modifications and the DNA damage response
    • Vidanes GM, Bonilla CY, Toczyski DP. Complicated tails: histone modifications and the DNA damage response. Cell. 2005:121(7):973–6.
    • (2005) Cell , vol.121 , Issue.7 , pp. 973-976
    • Vidanes, G.M.1    Bonilla, C.Y.2    Toczyski, D.P.3
  • 30
    • 14644399796 scopus 로고    scopus 로고
    • Histone metabolic pathways and chromatin assembly factors as proliferation markers
    • Polo SE, Almouzni G. Histone metabolic pathways and chromatin assembly factors as proliferation markers. Cancer Lett. 2005;220(1):1–9.
    • (2005) Cancer Lett , vol.220 , Issue.1 , pp. 1-9
    • Polo, S.E.1    Almouzni, G.2
  • 31
    • 33845612203 scopus 로고    scopus 로고
    • Transcriptional silencing of the death gene BNIP3 by cooperative action of NF-kappaB and histone deacetylase 1 in ventricular myocytes
    • Shaw J, Zhang T, Rzeszutek M, Yurkova N, Baetz D, Davie JR, Kirshenbaum LA. Transcriptional silencing of the death gene BNIP3 by cooperative action of NF-kappaB and histone deacetylase 1 in ventricular myocytes. Circ Res. 2006;99(12):1347–54.
    • (2006) Circ Res , vol.99 , Issue.12 , pp. 1347-1354
    • Shaw, J.1    Zhang, T.2    Rzeszutek, M.3    Yurkova, N.4    Baetz, D.5    Davie, J.R.6    Kirshenbaum, L.A.7
  • 33
    • 0035838991 scopus 로고    scopus 로고
    • Coordination of a transcrip-tional switch by HMGI(Y) acetylation
    • Munshi N, Agalioti T, Lomvardas S, Merika M, Chen G, Tanos D. Coordination of a transcrip-tional switch by HMGI(Y) acetylation. Science. 2001;293(5532):1133–6.
    • (2001) Science , vol.293 , Issue.5532 , pp. 1133-1136
    • Munshi, N.1    Agalioti, T.2    Lomvardas, S.3    Merika, M.4    Chen, G.5    Tanos, D.6
  • 34
    • 12244251445 scopus 로고    scopus 로고
    • Stat3 dimerization regulated by reversible acetylation of a single lysine residue
    • Yuan ZL, Guan YJ, Chatterjee D, Chin YE. Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science. 2005;307(5707): 269–73.
    • (2005) Science , vol.307 , Issue.5707 , pp. 269-273
    • Yuan, Z.L.1    Guan, Y.J.2    Chatterjee, D.3    Chin, Y.E.4
  • 35
    • 15744385061 scopus 로고    scopus 로고
    • Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation
    • Wang R, Cherukuri P, Luo J. Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation. J Biol Chem 2005;280(12):11528–34.
    • (2005) J Biol Chem , vol.280 , Issue.12 , pp. 11528-11534
    • Wang, R.1    Cherukuri, P.2    Luo, J.3
  • 38
    • 0036753547 scopus 로고    scopus 로고
    • Control of Smad7 stability by competition between acetylation and ubiquitination
    • Grönroos E, Hellman U, Heldin CH, Ericsson J. Control of Smad7 stability by competition between acetylation and ubiquitination. Mol Cell. 2002;10(3):483–93.
    • (2002) Mol Cell , vol.10 , Issue.3 , pp. 483-493
    • Grönroos, E.1    Hellman, U.2    Heldin, C.H.3    Ericsson, J.4
  • 39
    • 2442544457 scopus 로고    scopus 로고
    • MDM2 mediates p300/CREB-binding protein-associated factor ubiquitination and degradation
    • Jin Y, Zeng SX, Lee H, Lu H. MDM2 mediates p300/CREB-binding protein-associated factor ubiquitination and degradation. J Biol Chem. 2004;279(19):20035–43.
    • (2004) J Biol Chem , vol.279 , Issue.19 , pp. 20035-20043
    • Jin, Y.1    Zeng, S.X.2    Lee, H.3    Lu, H.4
  • 40
    • 5644302201 scopus 로고    scopus 로고
    • Stability of the hepatocyte nuclear factor 6 transcription factor requires acetylation by the CREB-binding protein coactivator
    • Rausa FM 3rd, Hughes DE, Costa RH. Stability of the hepatocyte nuclear factor 6 transcription factor requires acetylation by the CREB-binding protein coactivator. J Biol Chem. 2004;279(41):43070–6.
    • (2004) J Biol Chem , vol.279 , Issue.41 , pp. 43070-43076
    • Rausa, F.M.1    Hughes, D.E.2    Costa, R.H.3
  • 42
    • 27744518040 scopus 로고    scopus 로고
    • FoxO1 protects against pancreatic beta cell failure through NeuroD and MafA induction
    • Kitamura YI, Kitamura T, Kruse JP, Raum JC, Stein R, Gu W, Accili D. FoxO1 protects against pancreatic beta cell failure through NeuroD and MafA induction. Cell Metab. 2005;2(3):153–63.
    • (2005) Cell Metab , vol.2 , Issue.3 , pp. 153-163
    • Kitamura, Y.I.1    Kitamura, T.2    Kruse, J.P.3    Raum, J.C.4    Stein, R.5    Gu, W.6    Accili, D.7
  • 43
    • 0034905085 scopus 로고    scopus 로고
    • Regulation of transcription factor YY1 by acetylation and deacetylation
    • Yao YL, Yang WM, Seto E. Regulation of transcription factor YY1 by acetylation and deacetylation. Mol Cell Biol. 2001;21(17):5979–91.
    • (2001) Mol Cell Biol , vol.21 , Issue.17 , pp. 5979-5991
    • Yao, Y.L.1    Yang, W.M.2    Seto, E.3
  • 45
    • 0034969453 scopus 로고    scopus 로고
    • Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300
    • Hasan S, Stucki M, Hassa PO, Imhof R, Gehrig P, Hunziker P, Hübscher U, Hottiger MO. Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300. Mol Cell. 2001;7(6):1221–31.
    • (2001) Mol Cell , vol.7 , Issue.6 , pp. 1221-1231
    • Hasan, S.1    Stucki, M.2    Hassa, P.O.3    Imhof, R.4    Gehrig, P.5    Hunziker, P.6    Hübscher, U.7    Hottiger, M.O.8
  • 47
  • 49
    • 34347206854 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors sensitize prostate cancer cells to agents that produce DNA double-strand breaks by targeting Ku70 acetylation
    • Chen CS, Wang YC, Yang HC, Huang PH, Kulp SK, Yang CC, Lu YS, Matsuyama S, Chen CY, Chen CS. Histone deacetylase inhibitors sensitize prostate cancer cells to agents that produce DNA double-strand breaks by targeting Ku70 acetylation. Cancer Res. 2007;67(11):5318–27.
    • (2007) Cancer Res , vol.67 , Issue.11 , pp. 5318-5327
    • Chen, C.S.1    Wang, Y.C.2    Yang, H.C.3    Huang, P.H.4    Kulp, S.K.5    Yang, C.C.6    Lu, Y.S.7    Matsuyama, S.8    Chen, C.Y.9    Chen, C.S.10
  • 50
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon VM, Sandhof TW, Rifkind RA, Marks PA. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc Natl Acad Sci U S A. 2000;97(18):10014–9.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.18 , pp. 10014-10019
    • Richon, V.M.1    Sandhof, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 53
    • 2942584501 scopus 로고    scopus 로고
    • Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochon-drial damage and apoptosis in human leukemia cells
    • Rosato RR, Almenara JA, Dai Y, Grant S. Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochon-drial damage and apoptosis in human leukemia cells. Mol Cancer Ter. 2003;2(12):1273–84.
    • (2003) Mol Cancer Ter , vol.2 , Issue.12 , pp. 1273-1284
    • Rosato, R.R.1    Almenara, J.A.2    Dai, Y.3    Grant, S.4
  • 54
    • 33750288048 scopus 로고    scopus 로고
    • Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor
    • Xu W, Ngo L, Perez G, Dokmanovic M, Marks PA. Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor. Proc Natl Acad Sci U S A. 2006;103(42):15540–5.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.42 , pp. 15540-15545
    • Xu, W.1    Ngo, L.2    Perez, G.3    Dokmanovic, M.4    Marks, P.A.5
  • 55
    • 0141744707 scopus 로고    scopus 로고
    • Histone hyperacetylation in mitosis prevents sister chromatid separation and produces chromosome segregation defects
    • Cimini D, Mattiuzzo M, Torosantucci L, Degrassi F. Histone hyperacetylation in mitosis prevents sister chromatid separation and produces chromosome segregation defects. Mol Biol Cell. 2003;14(9):3821–33.
    • (2003) Mol Biol Cell , vol.14 , Issue.9 , pp. 3821-3833
    • Cimini, D.1    Mattiuzzo, M.2    Torosantucci, L.3    Degrassi, F.4
  • 56
    • 33751185927 scopus 로고    scopus 로고
    • Tioredoxin in cancer-role of his-tone deacetylase inhibitors
    • Marks PA. Tioredoxin in cancer-role of his-tone deacetylase inhibitors. Semin Cancer Biol. 2006;16(6):436–43.
    • (2006) Semincancer Biol , vol.16 , Issue.6 , pp. 436-443
    • Marks, P.A.1
  • 58
    • 33750463070 scopus 로고    scopus 로고
    • Cytotoxic effects of histone deacetylase inhibitor FK228 (Depsipeptide, formally named FR901228) in combination with conventional anti-leukemia/lymphoma agents against human leukemia/lymphoma cell lines
    • Kano Y, Akutsu M, Tsunoda S, Izumi T, Kobayashi H, Mano H, Furukawa Y. Cytotoxic effects of histone deacetylase inhibitor FK228 (depsipeptide, formally named FR901228) in combination with conventional anti-leukemia/lymphoma agents against human leukemia/lymphoma cell lines. Invest New Drugs. 2007;25(1):31–40.
    • (2007) Invest New Drugs , vol.25 , Issue.1 , pp. 31-40
    • Kano, Y.1    Akutsu, M.2    Tsunoda, S.3    Izumi, T.4    Kobayashi, H.5    Mano, H.6    Furukawa, Y.7
  • 59
    • 61849144810 scopus 로고    scopus 로고
    • HDAC family: What are the cancer relevant targets?
    • Witt O, Deubzer HE, Milde T, Oehme I. HDAC family: What are the cancer relevant targets? Cancer Lett. 2009;277(1):8–21.
    • (2009) Cancer Lett , vol.277 , Issue.1 , pp. 8-21
    • Witt, O.1    Deubzer, H.E.2    Milde, T.3    Oehme, I.4
  • 61
    • 33645950778 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Multifunctional anticancer agents
    • Liu T, Kuljaca S, Tee A, Marshall GM. Histone deacetylase inhibitors: multifunctional anticancer agents. Cancer Treat Rev. 2006;32(3):157–65.
    • (2006) Cancer Treat Rev , vol.32 , Issue.3 , pp. 157-165
    • Liu, T.1    Kuljaca, S.2    Tee, A.3    Marshall, G.M.4
  • 62
    • 27744450043 scopus 로고    scopus 로고
    • Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha
    • Arnesen T1, Kong X, Evjenth R, Gromyko D, Varhaug JE, Lin Z, Sang N, Caro J, Lillehaug JR. Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha. FEBS Lett. 2005;579(28):6428–32.
    • (2005) FEBS Lett , vol.579 , Issue.28 , pp. 6428-6432
    • Arnesen, T.1    Kong, X.2    Evjenth, R.3    Gromyko, D.4    Varhaug, J.E.5    Lin, Z.6    Sang, N.7    Caro, J.8    Lillehaug, J.R.9
  • 63
    • 33645236747 scopus 로고    scopus 로고
    • Purified recombinanthARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro
    • Murray-Rust TA, Oldham NJ, Hewitson KS, Schofield CJ. Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro. FEBS Lett. 2006;580(8):1911–8.
    • (2006) FEBS Lett , vol.580 , Issue.8 , pp. 1911-1918
    • Murray-Rust, T.A.1    Oldham, N.J.2    Hewitson, K.S.3    Schofield, C.J.4
  • 66
    • 80055077899 scopus 로고    scopus 로고
    • HDAC4 protein regulates HIF1α protein lysine acetylation and cancer cell response to hypoxia
    • Geng H, Harvey CT, Pittsenbarger J, Liu Q, Beer TM, Xue C, Qian DZ. HDAC4 protein regulates HIF1α protein lysine acetylation and cancer cell response to hypoxia. J Biol Chem. 2011;286(44):38095–102.
    • (2011) J Biol Chem , vol.286 , Issue.44 , pp. 38095
    • Geng, H.1    Harvey, C.T.2    Pittsenbarger, J.3    Liu, Q.4    Beer, T.M.5    Xue, C.6    Qian, D.Z.7
  • 68
    • 0036842460 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis
    • Rössig L, Li H, Fisslthaler B, Urbich C, Fleming I, Förstermann U, Zeiher AM, Dimmeler S. Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis. Circ Res. 2002;91(9):837–44.
    • (2002) Circ Res , vol.91 , Issue.9 , pp. 837-844
    • Rössig, L.1    Li, H.2    Fisslthaler, B.3    Urbich, C.4    Fleming, I.5    Förstermann, U.6    Zeiher, A.M.7    Dimmeler, S.8
  • 69
    • 16644379041 scopus 로고    scopus 로고
    • Valproic acid and interferon-alpha synergistically inhibit neuroblastoma cell growth in vitro and in vivo
    • Michaelis M, Suhan T, Cinatl J, Driever PH, Cinatl J Jr. Valproic acid and interferon-alpha synergistically inhibit neuroblastoma cell growth in vitro and in vivo. Int J Oncol. 2004;25(6):1795–9.
    • (2004) Int J Oncol , vol.25 , Issue.6 , pp. 1795-1799
    • Michaelis, M.1    Suhan, T.2    Cinatl, J.3    Driever, P.H.4    Cinatl, J.5
  • 73
    • 3242875556 scopus 로고    scopus 로고
    • Histone deacetylase 1 is required to repress Notch target gene expression during zebraf-ish neurogenesis and to maintain the production of motoneurones in response to hedgehog signalling
    • Cunliffe V T. Histone deacetylase 1 is required to repress Notch target gene expression during zebraf-ish neurogenesis and to maintain the production of motoneurones in response to hedgehog signalling. Development. 2004;131(12):2983–9.
    • (2004) Development , vol.131 , Issue.12 , pp. 2983-2989
    • Cunliffe, V.T.1
  • 74
    • 84859367110 scopus 로고    scopus 로고
    • Different levels of Notch signaling regulate quiescence, renewal and differentiation in pancreatic endocrine progenitors
    • Ninov N, Borius M, Stainier DY. Different levels of Notch signaling regulate quiescence, renewal and differentiation in pancreatic endocrine progenitors. Development. 2012;139(9):1557–67.
    • (2012) Development , vol.139 , Issue.9 , pp. 1557-1567
    • Ninov, N.1    Borius, M.2    Stainier, D.Y.3
  • 75
    • 4644364508 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyro-sine kinase inhibitor PTK787/ZK222584
    • Qian DZ, Wang X, Kachhap SK, Kato Y, Wei Y, Zhang L, Atadja P, Pili R. The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyro-sine kinase inhibitor PTK787/ZK222584. Cancer Res. 2004;64(18):6626–34.
    • (2004) Cancer Res , vol.64 , Issue.18 , pp. 6626-6634
    • Qian, D.Z.1    Wang, X.2    Kachhap, S.K.3    Kato, Y.4    Wei, Y.5    Zhang, L.6    Atadja, P.7    Pili, R.8
  • 76
    • 78751652828 scopus 로고    scopus 로고
    • Effects of disturbed flow on vascular endothelium: Pathophysiological basis and clinical perspectives
    • Chiu JJ, Chien S. Effects of disturbed flow on vascular endothelium: pathophysiological basis and clinical perspectives. Physiol Rev. 2011;91(1):327–87.
    • (2011) Physiol Rev , vol.91 , Issue.1 , pp. 327-387
    • Chiu, J.J.1    Chien, S.2
  • 79
    • 11244297196 scopus 로고    scopus 로고
    • Extracellular phosphorylation converts pigment epithelium-derived factor from a neurotrophic to an antiangio-genic factor
    • Maik-Rachline G, Shaltiel S, Seger R. Extracellular phosphorylation converts pigment epithelium-derived factor from a neurotrophic to an antiangio-genic factor. Blood. 2005;105(2):670–8.
    • (2005) Blood , vol.105 , Issue.2 , pp. 670-678
    • Maik-Rachline, G.1    Shaltiel, S.2    Seger, R.3
  • 80
    • 0034654497 scopus 로고    scopus 로고
    • Controlling TGF-beta signaling
    • Massagué J, Chen YG. Controlling TGF-beta signaling. Genes Dev. 2000;4(6):627–644.
    • (2000) Genes Dev , vol.4 , Issue.6 , pp. 627-644
    • Massagué, J.1    Chen, Y.G.2
  • 81
    • 0033515620 scopus 로고    scopus 로고
    • A Smad transcriptional corepressor
    • Wotton D, Lo RS, Lee S, Massagué J. A Smad transcriptional corepressor. Cell. 1999;97(1):29–39.
    • (1999) Cell , vol.97 , Issue.1 , pp. 29-39
    • Wotton, D.1    Lo, R.S.2    Lee, S.3    Massagué, J.4
  • 82
    • 0033200361 scopus 로고    scopus 로고
    • The Ski oncoprotein interacts with the Smad proteins to repress TGFbeta signaling
    • Luo K, Stroschein SL, Wang W, Chen D, Martens E, Zhou S, Zhou Q. The Ski oncoprotein interacts with the Smad proteins to repress TGFbeta signaling. Genes Dev. 1999;13(17):2196–206.
    • (1999) Genes Dev , vol.13 , Issue.17 , pp. 2196-2206
    • Luo, K.1    Stroschein, S.L.2    Wang, W.3    Chen, D.4    Martens, E.5    Zhou, S.6    Zhou, Q.7
  • 84
    • 34848863333 scopus 로고    scopus 로고
    • Histone deacetylase 4 is required for TGFbeta1-induced myofibroblastic differentiation
    • Glenisson W, Castronovo V, Waltregny D. Histone deacetylase 4 is required for TGFbeta1-induced myofibroblastic differentiation. Biochim Biophys Acta. 2007;1773(10):1572–82.
    • (2007) Biochim Biophys Acta , vol.1773 , Issue.10 , pp. 1572-1582
    • Glenisson, W.1    Castronovo, V.2    Waltregny, D.3
  • 85
    • 84858592019 scopus 로고    scopus 로고
    • The role of stromal myofibroblast and extracellular matrix in tumor angiogenesis
    • Vong S, Kalluri R. The role of stromal myofibroblast and extracellular matrix in tumor angiogenesis. Genes Cancer. 2011;2(12):1139–45.
    • (2011) Genes Cancer , vol.2 , Issue.12 , pp. 1139-1145
    • Vong, S.1    Kalluri, R.2
  • 86
    • 77958450885 scopus 로고    scopus 로고
    • The role of wnt signaling in physiological and pathological angiogenesis
    • Dejana E. The role of wnt signaling in physiological and pathological angiogenesis. Circ Res. 2010;107(8):943–52.
    • (2010) Circ Res , vol.107 , Issue.8 , pp. 943-952
    • Dejana, E.1
  • 87
    • 84875052732 scopus 로고    scopus 로고
    • A histone deacety-lase inhibitor, largazole, decreases liver fibrosis and angiogenesis by inhibiting transforming growth factor-β and vascular endothelial growth factor signalling
    • Liu Y, Wang Z, Wang J, Lam W, Kwong S, Li F, Friedman SL, Zhou S, Ren Q, Xu Z, Wang X, Ji L, Tang S, Zhang H, Lui EL, Ye T. A histone deacety-lase inhibitor, largazole, decreases liver fibrosis and angiogenesis by inhibiting transforming growth factor-β and vascular endothelial growth factor signalling. Liver Int. 2013;33(4):504–15.
    • (2013) Liver Int , vol.33 , Issue.4 , pp. 504-515
    • Liu, Y.1    Wang, Z.2    Wang, J.3    Lam, W.4    Kwong, S.5    Li, F.6    Friedman, S.L.7    Zhou, S.8    Ren, Q.9    Xu, Z.10    Wang, X.11    Ji, L.12    Tang, S.13    Zhang, H.14    Lui, E.L.15    Ye, T.16
  • 88
    • 84884569020 scopus 로고    scopus 로고
    • Loss of epigenetic Kruppel-like factor 4 histone deacetylase (KLF-4-HDAC)-mediated transcriptional suppression is crucial in increasing vascular endothelial growth factor (VEGF) expression in breast cancer
    • Ray A, Alalem M, Ray BK. Loss of epigenetic Kruppel-like factor 4 histone deacetylase (KLF-4-HDAC)-mediated transcriptional suppression is crucial in increasing vascular endothelial growth factor (VEGF) expression in breast cancer. J Biol Chem. 2013;288(38):27232–342.
    • (2013) J Biol Chem , vol.288 , Issue.38 , pp. 27232-27342
    • Ray, A.1    Alalem, M.2    Ray, B.K.3
  • 89
    • 36248983372 scopus 로고    scopus 로고
    • Kruppel-like factor 4 is acetylated by p300 and regulates gene transcription via modulation of histone acetylation
    • Evans PM, Zhang W, Chen X, Yang J, Bhakat KK, Liu C. Kruppel-like factor 4 is acetylated by p300 and regulates gene transcription via modulation of histone acetylation. J Biol Chem. 2007;282(47):33994–4002.
    • (2007) J Biol Chem , vol.282 , Issue.47 , pp. 33994-34002
    • Evans, P.M.1    Zhang, W.2    Chen, X.3    Yang, J.4    Bhakat, K.K.5    Liu, C.6
  • 97
    • 53449086522 scopus 로고    scopus 로고
    • VEGF stimulates HDAC7 phosphorylation and cytoplasmic accumulation modulating matrix metalloproteinase expression and angiogenesis
    • Ha CH, Jhun BS, Kao HY, Jin ZG. VEGF stimulates HDAC7 phosphorylation and cytoplasmic accumulation modulating matrix metalloproteinase expression and angiogenesis. Arterioscler Tromb Vasc Biol. 2008;28(10):1782–8.
    • (2008) Arterioscler Tromb Vasc Biol , vol.28 , Issue.10 , pp. 1782-1788
    • Ha, C.H.1    Jhun, B.S.2    Kao, H.Y.3    Jin, Z.G.4
  • 100
  • 101
    • 62449178216 scopus 로고    scopus 로고
    • The critical role of the class III histone deacetylase SIRT1 in cancer
    • Liu T1, Liu PY, Marshall GM. The critical role of the class III histone deacetylase SIRT1 in cancer. Cancer Res. 2009;69(5):1702–5.
    • (2009) Cancer Res , vol.69 , Issue.5 , pp. 1702-1705
    • Liu, T.1    Liu, P.Y.2    Marshall, G.M.3
  • 102
    • 84860743760 scopus 로고    scopus 로고
    • FOXOs and sirtuins in vascular growth, maintenance, and aging
    • Oellerich MF, Potente M. FOXOs and sirtuins in vascular growth, maintenance, and aging. Circ Res. 2012;110(9):1238–51.
    • (2012) Circ Res , vol.110 , Issue.9 , pp. 1238-1251
    • Oellerich, M.F.1    Potente, M.2
  • 103
    • 84864722456 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in the treatment of cancer: Overview and perspectives
    • Giannini G, Cabri W, Fattorusso C, Rodriquez M. Histone deacetylase inhibitors in the treatment of cancer: overview and perspectives. Future Med Chem. 2012;4(11):1439–60.
    • (2012) Future Med Chem , vol.4 , Issue.11 , pp. 1439-1460
    • Giannini, G.1    Cabri, W.2    Fattorusso, C.3    Rodriquez, M.4
  • 104
    • 77649171884 scopus 로고    scopus 로고
    • Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents
    • Tan J, Cang S, Ma Y, Petrillo RL, Liu D. Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents. J Hematol Oncol. 2010;3: 5–17.
    • (2010) J Hematol Oncol , vol.3 , pp. 5-17
    • Tan, J.1    Cang, S.2    Ma, Y.3    Petrillo, R.L.4    Liu, D.5
  • 105
    • 84893846614 scopus 로고    scopus 로고
    • Valproic acid inhibits tumor angiogenesis in mice transplanted with Kasumi-1 leukemia cells
    • Zhang ZH, Hao CL, Liu P, Tian X, Wang LH, Zhao L, Zhu CM. Valproic acid inhibits tumor angiogenesis in mice transplanted with Kasumi-1 leukemia cells. Mol Med Rep. 2014;9(2):443–9.
    • (2014) Mol Med Rep , vol.9 , Issue.2 , pp. 443-449
    • Zhang, Z.H.1    Hao, C.L.2    Liu, P.3    Tian, X.4    Wang, L.H.5    Zhao, L.6    Zhu, C.M.7
  • 106
    • 84859954464 scopus 로고    scopus 로고
    • Valproic acid inhibits angiogenesis in vitro and glioma angiogenesis in vivo in the brain
    • Osuka S, Takano S, Watanabe S, Ishikawa E, Yamamoto T, Matsumura A. Valproic acid inhibits angiogenesis in vitro and glioma angiogenesis in vivo in the brain. Neurol Med Chir. 2012;52(4):186–93.
    • (2012) Neurol Med Chir , vol.52 , Issue.4 , pp. 186-193
    • Osuka, S.1    Takano, S.2    Watanabe, S.3    Ishikawa, E.4    Yamamoto, T.5    Matsumura, A.6
  • 108
    • 78650443648 scopus 로고    scopus 로고
    • MS-275 sensitizes TRAIL-resistant breast cancer cells, inhibits angiogenesis and metastasis, and reverses epithelial-mesenchymal transition in vivo
    • Srivastava RK, Kurzrock R, Shankar S. MS-275 sensitizes TRAIL-resistant breast cancer cells, inhibits angiogenesis and metastasis, and reverses epithelial-mesenchymal transition in vivo. Mol Cancer Ter. 2010;9(12):3254–66.
    • (2010) Mol Cancer Ter , vol.9 , Issue.12 , pp. 3254-3266
    • Srivastava, R.K.1    Kurzrock, R.2    Shankar, S.3
  • 109
    • 52649109068 scopus 로고    scopus 로고
    • The TRAIL apoptotic pathway in cancer onset, progression and therapy
    • Johnstone RW, Frew AJ, Smyth MJ. The TRAIL apoptotic pathway in cancer onset, progression and therapy. Nat Rev Cancer. 2008;8(10):782–98.
    • (2008) Nat Rev Cancer , vol.8 , Issue.10 , pp. 782-798
    • Johnstone, R.W.1    Frew, A.J.2    Smyth, M.J.3
  • 112
    • 77952673621 scopus 로고    scopus 로고
    • Mechanisms of resistance to anti-angiogenic therapy and development of third-generation anti-angiogenic drug candidates
    • Loges S, Schmidt T, Carmeliet P. Mechanisms of resistance to anti-angiogenic therapy and development of third-generation anti-angiogenic drug candidates. Genes Cancer. 2010;1(1):12–25.
    • (2010) Genes Cancer , vol.1 , Issue.1 , pp. 12-25
    • Loges, S.1    Schmidt, T.2    Carmeliet, P.3
  • 113
    • 0036947771 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors such as sodium butyrate and trichostatin A inhibit vascular endothelial growth factor (VEGF) secretion from human glioblastoma cells
    • Sawa H, Murakami H, Ohshima Y, Murakami M, Yamazaki I, Tamura Y, Mima T, Satone A, Ide W, Hashimoto I, Kamada H. Histone deacetylase inhibitors such as sodium butyrate and trichostatin A inhibit vascular endothelial growth factor (VEGF) secretion from human glioblastoma cells. Brain Tumor Pathol. 2002;19(2):77–81.
    • (2002) Brain Tumor Pathol , vol.19 , Issue.2 , pp. 77-81
    • Sawa, H.1    Murakami, H.2    Ohshima, Y.3    Murakami, M.4    Yamazaki, I.5    Tamura, Y.6    Mima, T.7    Satone, A.8    Ide, W.9    Hashimoto, I.10    Kamada, H.11
  • 114
    • 84879621346 scopus 로고    scopus 로고
    • Inhibition of proliferation, sprouting, tube formation and Tie2 signaling of lymphatic endothelial cells by the histone deacetylase inhibitor SAHA
    • Cheng HT, Hung WC. Inhibition of proliferation, sprouting, tube formation and Tie2 signaling of lymphatic endothelial cells by the histone deacetylase inhibitor SAHA. Oncol Rep. 2013;30(2):961–7.
    • (2013) Oncol Rep , vol.30 , Issue.2 , pp. 961-967
    • Cheng, H.T.1    Hung, W.C.2
  • 116
    • 84868486023 scopus 로고    scopus 로고
    • Angiopoietins in angio-genesis
    • Fagiani E, Christofori G. Angiopoietins in angio-genesis. Cancer Lett. 2013;328(1):18–26.
    • (2013) Cancer Lett , vol.328 , Issue.1 , pp. 18-26
    • Fagiani, E.1    Christofori, G.2
  • 117
    • 21644482527 scopus 로고    scopus 로고
    • Inhibition of angiogenesis in human glioma cell lines by antisense RNA from the soluble guanylate cyclase genes, GUCY1A3 and GUCY1B3
    • Saino M, Maruyama T, Sekiya T, Kayama T, Murakami Y. Inhibition of angiogenesis in human glioma cell lines by antisense RNA from the soluble guanylate cyclase genes, GUCY1A3 and GUCY1B3. Oncol Rep. 2004;12(1):47–52.
    • (2004) Oncol Rep , vol.12 , Issue.1 , pp. 47-52
    • Saino, M.1    Maruyama, T.2    Sekiya, T.3    Kayama, T.4    Murakami, Y.5
  • 118
    • 0036362236 scopus 로고    scopus 로고
    • Trombospondin-1 as an endogenous inhibitor of angiogenesis and tumor growth
    • Lawler J. Trombospondin-1 as an endogenous inhibitor of angiogenesis and tumor growth. J Cell Mol Med. 2002;6(1):1–12.
    • (2002) J Cell Mol Med , vol.6 , Issue.1 , pp. 1-12
    • Lawler, J.1
  • 121
    • 34250323467 scopus 로고    scopus 로고
    • CXCR4/CXCL12 axis promotes VEGF-mediated tumor angiogenesis through Akt signaling pathway
    • Liang Z, Brooks J, Willard M, Liang K, Yoon Y, Kang S, Shim H. CXCR4/CXCL12 axis promotes VEGF-mediated tumor angiogenesis through Akt signaling pathway. Biochem Biophys Res Commun. 2007;359(3):716–22.
    • (2007) Biochem Biophys Rescommun , vol.359 , Issue.3 , pp. 716-722
    • Liang, Z.1    Brooks, J.2    Willard, M.3    Liang, K.4    Yoon, Y.5    Kang, S.6    Shim, H.7


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