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Volumn 65, Issue 23, 2005, Pages 11094-11100

Induction of the hypoxia-inducible factor system by low levels of heat shock protein 90 inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; 17 DIMETHYLAMINOETHYLAMINO 17 DEMETHOXYGELDANAMYCIN; CARBONATE DEHYDRATASE; CARBONATE DEHYDRATASE IX; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HYPOXIA INDUCIBLE FACTOR 1; HYPOXIA INDUCIBLE FACTOR 1ALPHA; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROLYL 4 HYDROXYLASE DOMAIN PROTEIN 3; UNCLASSIFIED DRUG; VASCULOTROPIN;

EID: 28244466794     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-1877     Document Type: Article
Times cited : (42)

References (48)
  • 1
    • 0034021690 scopus 로고    scopus 로고
    • Hypoxra, clonal selection, and the role of HIF-1 in tumor progression
    • Semenza GL. Hypoxra, clonal selection, and the role of HIF-1 in tumor progression. Crit Rev Biochem Mol Biol 2000;35:71-103.
    • (2000) Crit Rev Biochem Mol Biol , vol.35 , pp. 71-103
    • Semenza, G.L.1
  • 2
    • 0036320934 scopus 로고    scopus 로고
    • 2- regulated gene expression
    • 2- regulated gene expression. FASEB J 2002;16:1151-62.
    • (2002) FASEB J , vol.16 , pp. 1151-1162
    • Wenger, R.H.1
  • 3
    • 28244454503 scopus 로고    scopus 로고
    • Proline hydroxylation and gene expression
    • Kaelin WG, Jr. Proline hydroxylation and gene expression. Annu Rev Biochem 2004;19:19.
    • (2004) Annu Rev Biochem , vol.19 , pp. 19
    • Kaelin Jr., W.G.1
  • 4
    • 0033587146 scopus 로고    scopus 로고
    • The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
    • Maxwell PH, Wiesener MS, Chang GW, et al. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 1999;399:271-5.
    • (1999) Nature , vol.399 , pp. 271-275
    • Maxwell, P.H.1    Wiesener, M.S.2    Chang, G.W.3
  • 7
    • 17944375360 scopus 로고    scopus 로고
    • C. elegans EGL-9 and mammalian homologs define a family of droxygenases that regulate HIF by prolyl hydroxylation
    • Epstein AC, Gleadle JM, McNeill LA, et al. C. elegans EGL-9 and mammalian homologs define a family of droxygenases that regulate HIF by prolyl hydroxylation. Cell 2001;107:43-54.
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.C.1    Gleadle, J.M.2    McNeill, L.A.3
  • 8
    • 0036216692 scopus 로고    scopus 로고
    • HIF-1 and tumor progression: Pathophysiology and therapeutics
    • Semenza GL. HIF-1 and tumor progression: pathophysiology and therapeutics. Trends Mol Med 2002;8: S62-7.
    • (2002) Trends Mol Med , vol.8
    • Semenza, G.L.1
  • 9
    • 10644234769 scopus 로고    scopus 로고
    • The role of hypoxia-induced factors in tumor progression
    • Vaupel P. The role of hypoxia-induced factors in tumor progression. Oncologist 2004;9:10-7.
    • (2004) Oncologist , vol.9 , pp. 10-17
    • Vaupel, P.1
  • 10
    • 2942590732 scopus 로고    scopus 로고
    • Exploiting tumour hypoxia in cancer treatment
    • Brown JM, Wilson WR. Exploiting tumour hypoxia in cancer treatment. Nat Rev Cancer 2004;4:437-47.
    • (2004) Nat Rev Cancer , vol.4 , pp. 437-447
    • Brown, J.M.1    Wilson, W.R.2
  • 11
    • 0034671307 scopus 로고    scopus 로고
    • Hypoxia-inducible expression of tumor-associated carbonic anhydrases
    • Wykoff CC, Beasley NJ, Watson PH, et al. Hypoxia-inducible expression of tumor-associated carbonic anhydrases. Cancer Res 2000;60:7075-83.
    • (2000) Cancer Res , vol.60 , pp. 7075-7083
    • Wykoff, C.C.1    Beasley, N.J.2    Watson, P.H.3
  • 12
    • 0035027828 scopus 로고    scopus 로고
    • Transcription factor HIF-1 is a necessary mediator of the Pasteur effect in mammalian cells
    • Seagroves TN, Ryan HE, Lu H, et al. Transcription factor HIF-1 is a necessary mediator of the Pasteur effect in mammalian cells. Mol Cell Biol 2001;21: 3436-44.
    • (2001) Mol Cell Biol , vol.21 , pp. 3436-3444
    • Seagroves, T.N.1    Ryan, H.E.2    Lu, H.3
  • 13
    • 0038282482 scopus 로고    scopus 로고
    • The hypoxia-inducible factor-1 α is a negative factor for tumor therapy
    • Unruh A, Kessel A, Mohamed UG, et al. The hypoxia-inducible factor-1 α is a negative factor for tumor therapy. Oncogene 2003;22:3213-20.
    • (2003) Oncogene , vol.22 , pp. 3213-3220
    • Unruh, A.1    Kessel, A.2    Mohamed, U.G.3
  • 14
    • 20944449117 scopus 로고    scopus 로고
    • Enhanced response to radiotherapy in tumours deficient in the function of hypoxia-indncible factor-1
    • Williams KJ, Telfer BA, Xenaki D, et al. Enhanced response to radiotherapy in tumours deficient in the function of hypoxia-indncible factor-1. Radiother Oncol 2005;75:89-98.
    • (2005) Radiother Oncol , vol.75 , pp. 89-98
    • Williams, K.J.1    Telfer, B.A.2    Xenaki, D.3
  • 16
    • 4143050461 scopus 로고    scopus 로고
    • New anticancer strategies targeting HIF-1
    • Yeo EJ, Chun YS, Park JW. New anticancer strategies targeting HIF-1. Biochem Pharmacol 2004;68:1061-9.
    • (2004) Biochem Pharmacol , vol.68 , pp. 1061-1069
    • Yeo, E.J.1    Chun, Y.S.2    Park, J.W.3
  • 17
    • 0037088576 scopus 로고    scopus 로고
    • Heat induction of tbe unphosphorylated form of hypoxia-inducible factor-1α is dependent on heat shock protein-90 activity
    • Katschinski DM, Le L, Heinrich D, et al. Heat induction of tbe unphosphorylated form of hypoxia-inducible factor-1α is dependent on heat shock protein-90 activity. J Biol Chem 2002;277:9262-7.
    • (2002) J Biol Chem , vol.277 , pp. 9262-9267
    • Katschinski, D.M.1    Le, L.2    Heinrich, D.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, et al. 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
  • 19
    • 1842691021 scopus 로고    scopus 로고
    • PI3K/Akt is required for heat shock proteins to protect hypoxia-inducible factor 1α from pVHL-independent degradation
    • Zhou J, Schmid T, Frank R, Brune B. PI3K/Akt is required for heat shock proteins to protect hypoxia-inducible factor 1α from pVHL-independent degradation. J Biol Chem 2004;279:13506-13.
    • (2004) J Biol Chem , vol.279 , pp. 13506-13513
    • Zhou, J.1    Schmid, T.2    Frank, R.3    Brune, B.4
  • 20
    • 4444260675 scopus 로고    scopus 로고
    • Interaction of the PAS B domain with HSP90 accelerates hypoxia-inducible factor-1α stabilization
    • Katschinski DM, Le L, Schindler SG, et al. Interaction of the PAS B domain with HSP90 accelerates hypoxia-inducible factor-1α stabilization. Cell Physiol Biochem 2004;14:351-60.
    • (2004) Cell Physiol Biochem , vol.14 , pp. 351-360
    • Katschinski, D.M.1    Le, L.2    Schindler, S.G.3
  • 21
    • 0036569704 scopus 로고    scopus 로고
    • Geldanamycin induces degradation of hypoxia-inducible factor 1α protein via the proteosome pathway in prostate cancer cells
    • Mabjeesh NJ, Post DE, Willard MT, et al. Geldanamycin induces degradation of hypoxia-inducible factor 1α protein via the proteosome pathway in prostate cancer cells. Cancer Res 2002;62:2478-82.
    • (2002) Cancer Res , vol.62 , pp. 2478-2482
    • Mabjeesh, N.J.1    Post, D.E.2    Willard, M.T.3
  • 22
    • 1942533543 scopus 로고    scopus 로고
    • Aryl hydrocarbon nuclear translocator (ABNT) promotes oxygen-independent stabilization of hypoxia-inducible factor-1α by modulating an Hsp90-dependent regulatory pathway
    • Isaacs JS, Jung YJ, Neckers L. Aryl hydrocarbon nuclear translocator (ABNT) promotes oxygen-independent stabilization of hypoxia-inducible factor-1α by modulating an Hsp90-dependent regulatory pathway. J Biol Chem 2004;279:16128-35.
    • (2004) J Biol Chem , vol.279 , pp. 16128-16135
    • Isaacs, J.S.1    Jung, Y.J.2    Neckers, L.3
  • 23
    • 0042885973 scopus 로고    scopus 로고
    • The Hsp90 chaperone complex as a novel target for cancer therapy
    • Goetz MP, Toft DO, Ames MM, Erlichman C. The Hsp90 chaperone complex as a novel target for cancer therapy. Ann Oncol 2003;14:1169-76.
    • (2003) Ann Oncol , vol.14 , pp. 1169-1176
    • Goetz, M.P.1    Toft, D.O.2    Ames, M.M.3    Erlichman, C.4
  • 24
    • 11244313935 scopus 로고    scopus 로고
    • Geldanamycin analogs
    • Sausville EA. Geldanamycin analogs. J Chemother 2004;16:68-9.
    • (2004) J Chemother , vol.16 , pp. 68-69
    • Sausville, E.A.1
  • 25
    • 20044384168 scopus 로고    scopus 로고
    • Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer
    • Goetz MP, Toft D, Reid J, et al. Phase I trial of 17-allylamino-17- demethoxygeldanamycin in patients with advanced cancer. J Clin Oncol 2005;23:1078-87.
    • (2005) J Clin Oncol , vol.23 , pp. 1078-1087
    • Goetz, M.P.1    Toft, D.2    Reid, J.3
  • 26
    • 20944444881 scopus 로고    scopus 로고
    • Phase I pharmacokinetic-pharmacodynamic study of 17-(allylamino)-17- demethoxygeldanamycin (17AAG, NSC 330507), a novel inhibitor of heat shock protein 90, in patients with refractory advanced cancers
    • Ramanathan RK, Trump DL, Eiseman JU et al. Phase I pharmacokinetic- pharmacodynamic study of 17-(allylamino)-17-demethoxygeldanamycin (17AAG, NSC 330507), a novel inhibitor of heat shock protein 90, in patients with refractory advanced cancers. Clin Cancer Res 2005;11:3385-91.
    • (2005) Clin Cancer Res , vol.11 , pp. 3385-3391
    • Ramanathan, R.K.1    Trump, D.L.2    Eiseman, J.U.3
  • 27
    • 23044441106 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies
    • Banerji U, O'Donnell A, Scurr M, et al. Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. J Clin Oncol 2005;23: 4152-61.
    • (2005) J Clin Oncol , vol.23 , pp. 4152-4161
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3
  • 28
    • 0030792094 scopus 로고    scopus 로고
    • Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1
    • Rolfs A, Kvietikova I, Gassmann M, Wenger RH. Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1. J Biol Chem 1997;272: 20055-62.
    • (1997) J Biol Chem , vol.272 , pp. 20055-20062
    • Rolfs, A.1    Kvietikova, I.2    Gassmann, M.3    Wenger, R.H.4
  • 29
    • 0037390915 scopus 로고    scopus 로고
    • The antimycotic ciclopirox olamine induces HIF-1α stability, VEGF expression, and angiogenesis
    • Linden T, Katschinski DM, Eckhardt K, et al. The antimycotic ciclopirox olamine induces HIF-1α stability, VEGF expression, and angiogenesis. FASEB J 2003;17: 761-3.
    • (2003) FASEB J , vol.17 , pp. 761-763
    • Linden, T.1    Katschinski, D.M.2    Eckhardt, K.3
  • 30
    • 4344569643 scopus 로고    scopus 로고
    • Geldanamycin induces Hsp70 and prevents α-synuclein aggregation and toxicity in vitro
    • McLean PJ, Klucken J, Shin Y, Hyman BT. Geldanamycin induces Hsp70 and prevents α-synuclein aggregation and toxicity in vitro. Biochem Biophys Res Commun 2004;321:665-9.
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 665-669
    • McLean, P.J.1    Klucken, J.2    Shin, Y.3    Hyman, B.T.4
  • 31
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler A, Lurz R, Lueder G, et al. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum Mol Genet 2001;10:1307-15.
    • (2001) Hum Mol Genet , vol.10 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3
  • 32
    • 0042855994 scopus 로고    scopus 로고
    • 17AAG: Low target binding affinity and potent cell activity-finding an explanation
    • Chiosis G, Huezo H, Rosen N, et al. 17AAG: low target binding affinity and potent cell activity-finding an explanation. Mol Cancer Ther 2003;2:123-9.
    • (2003) Mol Cancer Ther , vol.2 , pp. 123-129
    • Chiosis, G.1    Huezo, H.2    Rosen, N.3
  • 33
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou B, Prodromou C, Roe SM, et al. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J 1998;17: 4829-36.
    • (1998) EMBO J , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3
  • 34
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe SM, Prodromou C, O'Brien R, et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 1999;42:260-6.
    • (1999) J Med Chem , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3
  • 35
    • 0034050050 scopus 로고    scopus 로고
    • Loss of PTEN facilitates HIF-1-mediated gene expression
    • Zundel W, Schindler C, Haas-Kogan D, et al. Loss of PTEN facilitates HIF-1-mediated gene expression. Genes Dev 2000;14:391-6.
    • (2000) Genes Dev , vol.14 , pp. 391-396
    • Zundel, W.1    Schindler, C.2    Haas-Kogan, D.3
  • 36
    • 4344674482 scopus 로고    scopus 로고
    • Targeting multiple signal transduction pathways through inhibition of Hsp90
    • Zhang H, Burrows F. Targeting multiple signal transduction pathways through inhibition of Hsp90. J Mol Med 2004;82:488-99.
    • (2004) J Mol Med , vol.82 , pp. 488-499
    • Zhang, H.1    Burrows, F.2
  • 37
    • 16844371490 scopus 로고    scopus 로고
    • Heat shock protein 90 stabilization of ErbB2 expression is disrupted by ATP depletion in myocytes
    • Peng X, Guo X, Borkan SC, et al. Heat shock protein 90 stabilization of ErbB2 expression is disrupted by ATP depletion in myocytes. J Biol Chem 2005;280: 13148-52.
    • (2005) J Biol Chem , vol.280 , pp. 13148-13152
    • Peng, X.1    Guo, X.2    Borkan, S.C.3
  • 38
    • 3342967945 scopus 로고    scopus 로고
    • Strict regulation of CAIK(G250/MN) by HIF-1α in clear cell renal cell carcinoma
    • Grabmaier K, MC AdW, Verhaegh GW, Schalken JA, Oosterwijk E. Strict regulation of CAIK(G250/MN) by HIF-1α in clear cell renal cell carcinoma. Oncogene 2004;23:5624-31.
    • (2004) Oncogene , vol.23 , pp. 5624-5631
    • Grabmaier, K.1    Adw, M.C.2    Verhaegh, G.W.3    Schalken, J.A.4    Oosterwijk, E.5
  • 39
    • 2542601328 scopus 로고    scopus 로고
    • Hypoxia inducible carbonic anhydrase IX, marker of tumour hypoxia, survival pathway and therapy target
    • Potter C, Harris AL. Hypoxia inducible carbonic anhydrase IX, marker of tumour hypoxia, survival pathway and therapy target. Cell Cycle 2004;3:164-7.
    • (2004) Cell Cycle , vol.3 , pp. 164-167
    • Potter, C.1    Harris, A.L.2
  • 40
    • 18844408840 scopus 로고    scopus 로고
    • Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: Identification of a functional hypoxia-responsive element
    • Metzen E, Stiehl DP, Doege K, et al. Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: identification of a functional hypoxia-responsive element. Biochem J 2005;387:711-7.
    • (2005) Biochem J , vol.387 , pp. 711-717
    • Metzen, E.1    Stiehl, D.P.2    Doege, K.3
  • 41
    • 28244485179 scopus 로고    scopus 로고
    • Identification of a functional hypoxia-responsive element that regulates the expression of the egl nine homologue 3 (egln3/phd3) gene
    • Pescador N, Cuevas Y, Naranjo S, et al. Identification of a functional hypoxia-responsive element that regulates the expression of the egl nine homologue 3 (egln3/phd3) gene. Biochem J 2005;12:12.
    • (2005) Biochem J , vol.12 , pp. 12
    • Pescador, N.1    Cuevas, Y.2    Naranjo, S.3
  • 42
    • 4644318828 scopus 로고    scopus 로고
    • Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor
    • Appelhoff RJ, Tian YM, Raval RR, et al. Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. J Biol Chem 2004;279:38458-65.
    • (2004) J Biol Chem , vol.279 , pp. 38458-38465
    • Appelhoff, R.J.1    Tian, Y.M.2    Raval, R.R.3
  • 43
    • 4344645563 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 (HIF-1) promotes its degradation by induction of HIF-α-prolyl-4-hydroxylases
    • Marxsen JH, Stengel P, Doege K, et al. Hypoxia-inducible factor-1 (HIF-1) promotes its degradation by induction of HIF-α-prolyl-4-hydroxylases. Biochem J 2004;381:761-7.
    • (2004) Biochem J , vol.381 , pp. 761-767
    • Marxsen, J.H.1    Stengel, P.2    Doege, K.3
  • 44
    • 3242670482 scopus 로고    scopus 로고
    • Antiangiogenic properties of 17-(dimethylaminoethylamino)-17- demethoxygeldanamycin: An orally bioavailable heat shock protein 90 modulator
    • Kaur G, Belotti D, Burger AM, et al. Antiangiogenic properties of 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin: an orally bioavailable heat shock protein 90 modulator. Clin Cancer Res 2004;10: 4813-21.
    • (2004) Clin Cancer Res , vol.10 , pp. 4813-4821
    • Kaur, G.1    Belotti, D.2    Burger, A.M.3
  • 45
    • 10644261537 scopus 로고    scopus 로고
    • Induction of angiogenesis by heat shock protein 90 mediated by protein kinase Akt and endothelial nitric oxide synthase
    • Sun J, Liao JK, Induction of angiogenesis by heat shock protein 90 mediated by protein kinase Akt and endothelial nitric oxide synthase. Arterioscler Thromb Vasc Biol 2004;24:2238-44.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 2238-2244
    • Sun, J.1    Liao, J.K.2
  • 46
    • 7944224442 scopus 로고    scopus 로고
    • Loss of HIF-1α in endothelial cells disrupts a hypoxia-driven VEGF autocrine loop necessary for tumorigenesis
    • Tang N, Wang L, Esko J, et al. Loss of HIF-1α in endothelial cells disrupts a hypoxia-driven VEGF autocrine loop necessary for tumorigenesis. Cancer Cell 2004;6:485-95.
    • (2004) Cancer Cell , vol.6 , pp. 485-495
    • Tang, N.1    Wang, L.2    Esko, J.3
  • 47
    • 3442881606 scopus 로고    scopus 로고
    • The potential role of hypoxia inducible factor 1α in tumor progression after hypoxia and chemotherapy in hepatocellular carcinoma
    • Yang ZF, Poon RT, To J, Ho DW, Fan ST. The potential role of hypoxia inducible factor 1α in tumor progression after hypoxia and chemotherapy in hepatocellular carcinoma. Cancer Res 2004;64:5496-503.
    • (2004) Cancer Res , vol.64 , pp. 5496-5503
    • Yang, Z.F.1    Poon, R.T.2    To, J.3    Ho, D.W.4    Fan, S.T.5
  • 48
    • 11844269261 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 activation by (-)-epicutechin gallate: Potential adverse effects of cancer chemoprevention with high-dose green tea extracts
    • Zhou YD, Kim YP, Li XC, et al. Hypoxia-inducible factor-1 activation by (-)-epicutechin gallate: potential adverse effects of cancer chemoprevention with high-dose green tea extracts. J Nat Prod 2004;67: 2063-9.
    • (2004) J Nat Prod , vol.67 , pp. 2063-2069
    • Zhou, Y.D.1    Kim, Y.P.2    Li, X.C.3


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