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Volumn 66, Issue 17, 2006, Pages 8814-8821

Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1α

Author keywords

[No Author keywords available]

Indexed keywords

4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BUTYRIC ACID; FR 901228; HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 4 ENZYME; HISTONE DEACETYLASE 6 ENZYME; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID DERIVATIVE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; LBH 589; TRAPOXIN; TRICHOSTATIN A; UNCLASSIFIED DRUG; VALPROIC ACID; VON HIPPEL LINDAU PROTEIN;

EID: 33749006252     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-4598     Document Type: Article
Times cited : (294)

References (33)
  • 1
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza GL. Targeting HIF-1 for cancer therapy. Nat Rev Cancer 2003;3:721-32.
    • (2003) Nat Rev Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 2
    • 4644239258 scopus 로고    scopus 로고
    • Genetic basis of cancer of the kidney: Disease-specific approaches to therapy
    • Linehan WM, Vasselli J, Srinivasan R, et al. Genetic basis of cancer of the kidney: disease-specific approaches to therapy. Clin Cancer Res 2004;10:6282-9S.
    • (2004) Clin Cancer Res , vol.10
    • Linehan, W.M.1    Vasselli, J.2    Srinivasan, R.3
  • 3
    • 0034676331 scopus 로고    scopus 로고
    • Up-regulation of hypoxia-inducible factors HIF-1α and HIF-2α under normoxic conditions in renal carcinoma cells by von Hippel-Lindau tumor suppressor gene loss of function
    • Krieg M, Haas R, Brauch H, Acker T, Flamme I, Plate KH. Up-regulation of hypoxia-inducible factors HIF-1α and HIF-2α under normoxic conditions in renal carcinoma cells by von Hippel-Lindau tumor suppressor gene loss of function. Oncogene 2000;19:5435-43.
    • (2000) Oncogene , vol.19 , pp. 5435-5443
    • Krieg, M.1    Haas, R.2    Brauch, H.3    Acker, T.4    Flamme, I.5    Plate, K.H.6
  • 5
    • 18744375998 scopus 로고    scopus 로고
    • Regulation and destabilization of HIF-1α by ARD1-mediated acetylation
    • Jeong JW, Bae MK, Ahn MY, et al. Regulation and destabilization of HIF-1α by ARD1-mediated acetylation. Cell 2002;111:709-20.
    • (2002) Cell , vol.111 , pp. 709-720
    • Jeong, J.W.1    Bae, M.K.2    Ahn, M.Y.3
  • 6
    • 0036211013 scopus 로고    scopus 로고
    • Histone acetylation: A switch between repressive and permissive chromatin. Second in review series on chromatin dynamics
    • Eberharter A, Becker PB. Histone acetylation: a switch between repressive and permissive chromatin. Second in review series on chromatin dynamics. EMBO Rep 2002;3:224-9.
    • (2002) EMBO Rep , vol.3 , pp. 224-229
    • Eberharter, A.1    Becker, P.B.2
  • 7
    • 13844252820 scopus 로고    scopus 로고
    • Regulation of histone deacetylase activities
    • Sengupta N, Seto E. Regulation of histone deacetylase activities. J Cell Biochem 2004;93:57-67.
    • (2004) J Cell Biochem , vol.93 , pp. 57-67
    • Sengupta, N.1    Seto, E.2
  • 8
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • Grozinger CM, Schreiber SL. Deacetylase enzymes: biological functions and the use of small-molecule inhibitors. Chem Biol 2002;9:3-16.
    • (2002) Chem Biol , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 9
    • 16244366803 scopus 로고    scopus 로고
    • Class II histone deacetylases: From sequence to function, regulation, and clinical implication
    • Yang XJ, Gregoire S. Class II histone deacetylases: from sequence to function, regulation, and clinical implication. Mol Cell Biol 2005;25:2873-84.
    • (2005) Mol Cell Biol , vol.25 , pp. 2873-2884
    • Yang, X.J.1    Gregoire, S.2
  • 10
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • Johnstone RW. Histone-deacetylase inhibitors: novel drugs for the treatment of cancer. Nat Rev Drug Discov 2002;1:287-99.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 11
    • 8544225755 scopus 로고    scopus 로고
    • Differential protein acetylation induced by novel histone deacetylase inhibitors
    • Glaser KB, Li J, Pease LJ, et al. Differential protein acetylation induced by novel histone deacetylase inhibitors. Biochem Biophys Res Commun 2004;325:683-90.
    • (2004) Biochem Biophys Res Commun , vol.325 , pp. 683-690
    • Glaser, K.B.1    Li, J.2    Pease, L.J.3
  • 12
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin
    • Furumai R, Komatsu Y, Nishino N, Khochbin S, Yoshida M, Horinouchi S. Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc Natl Acad Sci U S A 2001;98:87-92.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 13
    • 18244383806 scopus 로고    scopus 로고
    • Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells
    • Gottlicher M, Minucci S, Zhu P, et al. Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells. EMBO J 2001;20:6969-78.
    • (2001) EMBO J , vol.20 , pp. 6969-6978
    • Gottlicher, M.1    Minucci, S.2    Zhu, P.3
  • 14
    • 0842325787 scopus 로고    scopus 로고
    • Histone deacetylase is a target of valproic acid-mediated cellular differentiation
    • Gurvich N, Tsygankova OM, Meinkoth JL, Klein PS. Histone deacetylase is a target of valproic acid-mediated cellular differentiation. Cancer Res 2004;64:1079-86.
    • (2004) Cancer Res , vol.64 , pp. 1079-1086
    • Gurvich, N.1    Tsygankova, O.M.2    Meinkoth, J.L.3    Klein, P.S.4
  • 15
    • 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 tyrosine kinase inhibitor PTK787/ZK222584
    • Qian DZ, Wang X, Kachhap SK, et al. The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584. Cancer Res 2004;64:6626-34.
    • (2004) Cancer Res , vol.64 , pp. 6626-6634
    • Qian, D.Z.1    Wang, X.2    Kachhap, S.K.3
  • 16
    • 0037225763 scopus 로고    scopus 로고
    • Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1α activity
    • Mie Lee Y, Kim SH, Kim HS, et al. Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1α activity. Biochem Biophys Res Commun 2003;300:241-6.
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 241-246
    • Mie Lee, Y.1    Kim, S.H.2    Kim, H.S.3
  • 17
    • 27744450043 scopus 로고    scopus 로고
    • Interaction between HIF-1α (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1α
    • Arnesen T, Kong X, Evjenth R, et al. Interaction between HIF-1α (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1α. FEBS Lett 2005;579:6428-32.
    • (2005) FEBS Lett , vol.579 , pp. 6428-6432
    • Arnesen, T.1    Kong, X.2    Evjenth, R.3
  • 18
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α-degradative pathway
    • Isaacs JS, Jung YJ, Mimnaugh EG, Martinez A, Cuttitta F, Neckers LM. Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α-degradative pathway. J Biol Chem 2002;277:29936-44.
    • (2002) J Biol Chem , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1    Jung, Y.J.2    Mimnaugh, E.G.3    Martinez, A.4    Cuttitta, F.5    Neckers, L.M.6
  • 19
    • 0030460724 scopus 로고    scopus 로고
    • Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase a gene promoters contain essential binding sites for hypoxia-inducible factor 1
    • Semenza GL, Jiang BH, Leung SW, et al. Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1. J Biol Chem 1996;271:32529-37.
    • (1996) J Biol Chem , vol.271 , pp. 32529-32537
    • Semenza, G.L.1    Jiang, B.H.2    Leung, S.W.3
  • 20
    • 0035012605 scopus 로고    scopus 로고
    • HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1α (HIF-1α) synthesis: Novel mechanism for HIF-1-mediated vascular endothelial growth factor expression
    • Laughner E, Taghavi P, Chiles K, Mahon PC, Semenza GL. HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1α (HIF-1α) synthesis: novel mechanism for HIF-1-mediated vascular endothelial growth factor expression. Mol Cell Biol 2001;21:3995-4004.
    • (2001) Mol Cell Biol , vol.21 , pp. 3995-4004
    • Laughner, E.1    Taghavi, P.2    Chiles, K.3    Mahon, P.C.4    Semenza, G.L.5
  • 21
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity
    • Mahon PC, Hirota K, Semenza GL. FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev 2001;15:2675-86.
    • (2001) Genes Dev , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 22
    • 25444465116 scopus 로고    scopus 로고
    • Both microtubule-stabilizing and microtubule-destabilizing drugs inhibit hypoxia-inducible factor-1α accumulation and activity by disrupting microtubule function
    • Escuin D, Kline ER, Giannakakou P. Both microtubule-stabilizing and microtubule-destabilizing drugs inhibit hypoxia-inducible factor-1α accumulation and activity by disrupting microtubule function. Cancer Res 2005;65:9021-8.
    • (2005) Cancer Res , vol.65 , pp. 9021-9028
    • Escuin, D.1    Kline, E.R.2    Giannakakou, P.3
  • 23
    • 0037448671 scopus 로고    scopus 로고
    • Cell biology: Tubulin acetylation and cell motility
    • Palazzo A, Ackerman B, Gundersen GG. Cell biology: tubulin acetylation and cell motility. Nature 2003;421:230.
    • (2003) Nature , vol.421 , pp. 230
    • Palazzo, A.1    Ackerman, B.2    Gundersen, G.G.3
  • 24
    • 12244295468 scopus 로고    scopus 로고
    • In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation
    • Matsuyama A, Shimazu T, Sumida Y, et al. In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation. EMBO J 2002;21:6820-31.
    • (2002) EMBO J , vol.21 , pp. 6820-6831
    • Matsuyama, A.1    Shimazu, T.2    Sumida, Y.3
  • 25
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • Hubbert C, Guardiola A, Shao R, et al. HDAC6 is a microtubule-associated deacetylase. Nature 2002;417:455-8.
    • (2002) Nature , vol.417 , pp. 455-458
    • Hubbert, C.1    Guardiola, A.2    Shao, R.3
  • 26
    • 0036682284 scopus 로고    scopus 로고
    • Identification of small molecule inhibitors of hypoxia-inducible factor 1 transcriptional activation pathway
    • Rapisarda A, Uranchimeg B, Scudiero DA, et al. Identification of small molecule inhibitors of hypoxia-inducible factor 1 transcriptional activation pathway. Cancer Res 2002;62:4316-24.
    • (2002) Cancer Res , vol.62 , pp. 4316-4324
    • Rapisarda, A.1    Uranchimeg, B.2    Scudiero, D.A.3
  • 27
    • 0037413948 scopus 로고    scopus 로고
    • Is HIF-1α a valid therapeutic target?
    • Pili R, Donehower RC. Is HIF-1α a valid therapeutic target? J Natl Cancer Inst 2003;95:498-9.
    • (2003) J Natl Cancer Inst , vol.95 , pp. 498-499
    • Pili, R.1    Donehower, R.C.2
  • 28
    • 4744368147 scopus 로고    scopus 로고
    • Histone deacetylase 7 associates with hypoxia-inducible factor 1α and increases transcriptional activity
    • Kato H, Tamamizu-Kato S, Shibasaki F. Histone deacetylase 7 associates with hypoxia-inducible factor 1α and increases transcriptional activity. J Biol Chem 2004;279:41966-74.
    • (2004) J Biol Chem , vol.279 , pp. 41966-41974
    • Kato, H.1    Tamamizu-Kato, S.2    Shibasaki, F.3
  • 29
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P, Pranpat M, Bradner J, et al. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J Biol Chem 2005;280:26729-34.
    • (2005) J Biol Chem , vol.280 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3
  • 30
    • 21144444486 scopus 로고    scopus 로고
    • HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor
    • Kovacs JJ, Murphy PJ, Gaillard S, et al. HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Mol Cell 2005;18:601-7.
    • (2005) Mol Cell , vol.18 , pp. 601-607
    • Kovacs, J.J.1    Murphy, P.J.2    Gaillard, S.3
  • 31
    • 14844344773 scopus 로고    scopus 로고
    • Association with class IIa histone deacetylases up-regulates the sumoylation of MEF2 transcription factors
    • Gregoire S, Yang XJ. Association with class IIa histone deacetylases up-regulates the sumoylation of MEF2 transcription factors. Mol Cell Biol 2005;25:2273-87.
    • (2005) Mol Cell Biol , vol.25 , pp. 2273-2287
    • Gregoire, S.1    Yang, X.J.2
  • 32
    • 2342661143 scopus 로고    scopus 로고
    • Intratumoral hypoxia, radiation resistance, and HIF-1
    • Semenza GL. Intratumoral hypoxia, radiation resistance, and HIF-1. Cancer Cell 2004;5:405-6.
    • (2004) Cancer Cell , vol.5 , pp. 405-406
    • Semenza, G.L.1
  • 33
    • 31144458716 scopus 로고    scopus 로고
    • How avastin potentiates chemotherapeutic drugs: Action and reaction in antiangiogenic therapy
    • Blagosklonny MV. How avastin potentiates chemotherapeutic drugs: action and reaction in antiangiogenic therapy. Cancer Biol Ther 2005;4:1307-10.
    • (2005) Cancer Biol Ther , vol.4 , pp. 1307-1310
    • Blagosklonny, M.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.