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Volumn 9, Issue 5, 2007, Pages 278-289

Hypoxia-inducible factors and cancer

Author keywords

Angiogenesis; Cancer; HIF; Hypoxia; VHL

Indexed keywords

HEAT SHOCK PROTEIN 90 INHIBITOR; HYPOXIA INDUCIBLE FACTOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; OXYGEN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; TRANSCRIPTION FACTOR; BASIC HELIX LOOP HELIX TRANSCRIPTION FACTOR; ENDOTHELIAL PAS DOMAIN CONTAINING PROTEIN 1; ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1; HYPOXIA INDUCIBLE FACTOR 1; UNCLASSIFIED DRUG;

EID: 34848898470     PISSN: 1699048X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12094-007-0055-y     Document Type: Review
Times cited : (40)

References (150)
  • 1
    • 0027936404 scopus 로고
    • Activation of AP-1 and of a nuclear redox factor, Ref-1, in the response of HT29 colon cancer cells to hypoxia
    • Yao KS, Xanthoudakis S, Curran T, O'Dwyer PJ (1994) Activation of AP-1 and of a nuclear redox factor, Ref-1, in the response of HT29 colon cancer cells to hypoxia. Mol Cell Biol 14:5997-6003
    • (1994) Mol Cell Biol , vol.14 , pp. 5997-6003
    • Yao, K.S.1    Xanthoudakis, S.2    Curran, T.3    O'Dwyer, P.J.4
  • 2
    • 33749518516 scopus 로고    scopus 로고
    • Posttranslational hydroxylation of ankyrin repeats in IêB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)
    • Cockman ME, Lancaster DE, Stolze IP et al (2006) Posttranslational hydroxylation of ankyrin repeats in IêB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH). Proc Natl Acad Sci U S A 103:14767-14772
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 14767-14772
    • Cockman, M.E.1    Lancaster, D.E.2    Stolze, I.P.3
  • 3
    • 33845321931 scopus 로고    scopus 로고
    • Prolyl hydroxylase-1 negatively regulates IêB kinase-beta, giving insight into hypoxia-induced NFeêB activity
    • Cummins EP, Berra E, Comerford KM et al (2006) Prolyl hydroxylase-1 negatively regulates IêB kinase-beta, giving insight into hypoxia-induced NFeêB activity. Proc Natl Acad Sci U S A 103:18154-18159
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18154-18159
    • Cummins, E.P.1    Berra, E.2    Comerford, K.M.3
  • 4
    • 0028841622 scopus 로고
    • The genomic response of tumor cells to hypoxia and reoxygenation. Differential activation of transcription factors AP-1 and NF-kappa B
    • Rupec RA, Baeuerle PA (1995) The genomic response of tumor cells to hypoxia and reoxygenation. Differential activation of transcription factors AP-1 and NF-kappa B. Eur J Biochem 234:632-640
    • (1995) Eur J Biochem , vol.234 , pp. 632-640
    • Rupec, R.A.1    Baeuerle, P.A.2
  • 5
    • 8844284460 scopus 로고    scopus 로고
    • Genetic analysis of pathways regulated by the von Hippel-Lindau tumor suppressor in Caenorhabditis elegans
    • Bishop, T, Lau KW, Epstein ACR et al (2004) Genetic analysis of pathways regulated by the von Hippel-Lindau tumor suppressor in Caenorhabditis elegans. PLoS Biol 2:e289
    • (2004) PLoS Biol , vol.2
    • Bishop, T.1    Lau, K.W.2    Epstein, A.C.R.3
  • 6
    • 33646248422 scopus 로고    scopus 로고
    • Differential regulation of the transcriptional activities of hypoxia-inducible factor 1 alpha (HIF-1α) and HIF-2α in stem cells
    • Hu C-J, Iyer S, Sataur A et al (2006) Differential regulation of the transcriptional activities of hypoxia-inducible factor 1 alpha (HIF-1α) and HIF-2α in stem cells. Mol Cell Biol 26:3514-3526
    • (2006) Mol Cell Biol , vol.26 , pp. 3514-3526
    • Hu, C.-J.1    Iyer, S.2    Sataur, A.3
  • 7
    • 20144362749 scopus 로고    scopus 로고
    • Roles of the HIF-1 hypoxia-inducible factor during hypoxia response in Caenorhabditis elegans
    • Shen C, Nettleton D, Jiang M et al (2005) Roles of the HIF-1 hypoxia-inducible factor during hypoxia response in Caenorhabditis elegans. J Biol Chem 280:20580-20588
    • (2005) J Biol Chem , vol.280 , pp. 20580-20588
    • Shen, C.1    Nettleton, D.2    Jiang, M.3
  • 8
    • 17144416530 scopus 로고    scopus 로고
    • Differential gene up-regulation by hypoxia-inducible factor-1α and hypoxia-inducible factor-2α in HEK293T cells
    • Wang V, Davis DA, Haque M et al (2005) Differential gene up-regulation by hypoxia-inducible factor-1α and hypoxia-inducible factor-2α in HEK293T cells. Cancer Res 65:3299-3306
    • (2005) Cancer Res , vol.65 , pp. 3299-3306
    • Wang, V.1    Davis, D.A.2    Haque, M.3
  • 9
    • 31444444162 scopus 로고    scopus 로고
    • Integration of oxygen signaling at the consensus HRE
    • Wenger RH, Stiehl DP, Camenisch G (2005) Integration of oxygen signaling at the consensus HRE. Sci STKE 306:rE12
    • (2005) Sci STKE , vol.306
    • Wenger, R.H.1    Stiehl, D.P.2    Camenisch, G.3
  • 10
    • 0037837724 scopus 로고    scopus 로고
    • Multiple splice variants of the human HIF-3alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex
    • Maynard MA, Qi H, Chung J et al (2003) Multiple splice variants of the human HIF-3alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex. J Biol Chem 278:11032-11040
    • (2003) J Biol Chem , vol.278 , pp. 11032-11040
    • Maynard, M.A.1    Qi, H.2    Chung, J.3
  • 11
    • 0035969508 scopus 로고    scopus 로고
    • Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression
    • Makino Y, Cao R, Svensson K et al (2001) Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression. Nature 414:550-554
    • (2001) Nature , vol.414 , pp. 550-554
    • Makino, Y.1    Cao, R.2    Svensson, K.3
  • 12
    • 0037031808 scopus 로고    scopus 로고
    • Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus
    • Makino Y, Kanopka A, Wilson WJ et al (2002) Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus. J Biol Chem 277:32405-32408
    • (2002) J Biol Chem , vol.277 , pp. 32405-32408
    • Makino, Y.1    Kanopka, A.2    Wilson, W.J.3
  • 13
    • 0037337763 scopus 로고    scopus 로고
    • Oxygen-dependent regulation of hypoxia-inducible factors by prolyl and asparaginyl hydroxylation
    • Lando D, Gorman JJ, White MF, Peet DJ (2003) Oxygen-dependent regulation of hypoxia-inducible factors by prolyl and asparaginyl hydroxylation. Eur J Immunol 270:781-790
    • (2003) Eur J Immunol , vol.270 , pp. 781-790
    • Lando, D.1    Gorman, J.J.2    White, M.F.3    Peet, D.J.4
  • 14
    • 0035917313 scopus 로고    scopus 로고
    • HIFalpha targeted for VHL-mediated destruction by pro-line hydroxylation: Implications for O2 sensing
    • Ivan M, Kondo K, Yang H et al (2001) HIFalpha targeted for VHL-mediated destruction by pro-line hydroxylation: Implications for O2 sensing. Science 292:464-468
    • (2001) Science , vol.292 , pp. 464-468
    • Ivan, M.1    Kondo, K.2    Yang, H.3
  • 15
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • Jaakkola P, Mole DR, Tian YM et al (2001) Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 292:468-472
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1    Mole, D.R.2    Tian, Y.M.3
  • 16
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick RK, McKnight SL (2001) A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294:1337-1340
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 17
    • 17944375360 scopus 로고    scopus 로고
    • C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
    • Epstein AC, Gleadle JM, McNeill LA et al (2001) C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107:43-54
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.C.1    Gleadle, J.M.2    McNeill, L.A.3
  • 18
    • 33749410367 scopus 로고    scopus 로고
    • The length of peptide substrates has a marked effect on hydroxylation by the HIF prolyl 4-hydroxylases
    • Koivunen P, Hirsila M, Kivirikko KI, Myllyharju J (2006) The length of peptide substrates has a marked effect on hydroxylation by the HIF prolyl 4-hydroxylases. J Biol Chem 281:28712-28720
    • (2006) J Biol Chem , vol.281 , pp. 28712-28720
    • Koivunen, P.1    Hirsila, M.2    Kivirikko, K.I.3    Myllyharju, J.4
  • 19
    • 33846315497 scopus 로고    scopus 로고
    • Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay
    • Ehrismann D, Flashman E, Genn DN et al (2007) Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay. Biochem J 401:227-234
    • (2007) Biochem J , vol.401 , pp. 227-234
    • Ehrismann, D.1    Flashman, E.2    Genn, D.N.3
  • 20
    • 0035812318 scopus 로고    scopus 로고
    • Characterization and comparative analysis of the EGLN gene family
    • Taylor MS (2001) Characterization and comparative analysis of the EGLN gene family. Gene 275:125-132
    • (2001) Gene , vol.275 , pp. 125-132
    • Taylor, M.S.1
  • 22
    • 33745665335 scopus 로고    scopus 로고
    • HIF prolyl hydroxylases in the rat; organ distribution and changes in expression following hypoxia and coronary artery ligation
    • Willam C, Maxwell PH, Nichols L et al (2006) HIF prolyl hydroxylases in the rat; organ distribution and changes in expression following hypoxia and coronary artery ligation. J Mol Cell Cardiol 41:68-77
    • (2006) J Mol Cell Cardiol , vol.41 , pp. 68-77
    • Willam, C.1    Maxwell, P.H.2    Nichols, L.3
  • 23
    • 4644318828 scopus 로고    scopus 로고
    • Differential function of the prolyl hydroxylases PHD1, PHD2 and PHD3 in the regulation of the hypoxia inducible factor
    • Appelhoff RJ, Tian Y-M, Raval RR et al (2004) Differential function of the prolyl hydroxylases PHD1, PHD2 and PHD3 in the regulation of the hypoxia inducible factor. J Biol Chem 279:38458-38465
    • (2004) J Biol Chem , vol.279 , pp. 38458-38465
    • Appelhoff, R.J.1    Tian, Y.-M.2    Raval, R.R.3
  • 24
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1a in normoxia
    • Berra E, Benizri E, Ginouves A et al (2003) HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1a in normoxia. EMBO J 22:4082-4090
    • (2003) EMBO J , vol.22 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouves, A.3
  • 25
    • 33750976389 scopus 로고    scopus 로고
    • Placental but not heart defects are associated with elevated hypoxia-inducible factor α levels in mice lacking prolyl hydroxylase domain protein 2
    • Takeda K, Ho VC, Takeda H et al (2006) Placental but not heart defects are associated with elevated hypoxia-inducible factor α levels in mice lacking prolyl hydroxylase domain protein 2. Mol Cell Biol 26:8336-8346
    • (2006) Mol Cell Biol , vol.26 , pp. 8336-8346
    • Takeda, K.1    Ho, V.C.2    Takeda, H.3
  • 26
    • 1542300383 scopus 로고    scopus 로고
    • The von Hippel Lindau/hypoxia-inducible factor (HIF) pathway regulates the transcription of the HIF-proline hydroxylase genes in response to low oxygen
    • del Peso L, Castellanos MC, Temes E et al (2003) The von Hippel Lindau/ hypoxia-inducible factor (HIF) pathway regulates the transcription of the HIF-proline hydroxylase genes in response to low oxygen. J Biol Chem 278:48690-48695
    • (2003) J Biol Chem , vol.278 , pp. 48690-48695
    • del Peso, L.1    Castellanos, M.C.2    Temes, E.3
  • 27
    • 4344645563 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 (HIF-1) promotes its degradation by induction of HIF-a-prolyl-4-hydroxylases
    • Marxsen JH, Stengel P, Doege K et al (2004) Hypoxia-inducible factor-1 (HIF-1) promotes its degradation by induction of HIF-a-prolyl-4-hydroxylases. Biochem J 381:761-767
    • (2004) Biochem J , vol.381 , pp. 761-767
    • Marxsen, J.H.1    Stengel, P.2    Doege, K.3
  • 28
    • 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 (2005) Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: Identification of a functional hypoxia-responsive element. Biochem J 387:711-717
    • (2005) Biochem J , vol.387 , pp. 711-717
    • Metzen, E.1    Stiehl, D.P.2    Doege, K.3
  • 29
    • 23944454868 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 (2005) Identification of a functional hypoxia-responsive element that regulates the expression of the egl nine homologue 3 (egln3/phd3) gene. Biochem J 390:189-197
    • (2005) Biochem J , vol.390 , pp. 189-197
    • Pescador, N.1    Cuevas, Y.2    Naranjo, S.3
  • 30
    • 0035936886 scopus 로고    scopus 로고
    • HIF-1-dependent transcriptional activity is requiered for oxygen-mediated HIF-1a degradation
    • Berra E, Richard DE, Gothie E, Pouyssegur J (2001) HIF-1-dependent transcriptional activity is requiered for oxygen-mediated HIF-1a degradation. FEBS Lett 491:85-90
    • (2001) FEBS Lett , vol.491 , pp. 85-90
    • Berra, E.1    Richard, D.E.2    Gothie, E.3    Pouyssegur, J.4
  • 31
    • 0141643358 scopus 로고    scopus 로고
    • Hypoxia up-regulates prolyl hydroxylase activity: A feedback mechansim that limits HIF-1 responses during reoxygenation
    • D'Angelo G, Duplan E, Boyer N et al (2003) Hypoxia up-regulates prolyl hydroxylase activity: A feedback mechansim that limits HIF-1 responses during reoxygenation. J Biol Chem 278:38183-38187
    • (2003) J Biol Chem , vol.278 , pp. 38183-38187
    • D'Angelo, G.1    Duplan, E.2    Boyer, N.3
  • 32
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch
    • Lando D, Peet DJ, Whelan DA et al (2002) Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science 295:858-861
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3
  • 33
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando D, Peet DJ, Gorman JJ et al (2002) FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev 16:1466-1471
    • (2002) Genes Dev , vol.16 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3
  • 34
    • 18544386401 scopus 로고    scopus 로고
    • Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family
    • Hewitson KS, McNeill LA, Riordan MV et al (2002) Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family. J Biol Chem 277:26351-26355
    • (2002) J Biol Chem , vol.277 , pp. 26351-26355
    • Hewitson, K.S.1    McNeill, L.A.2    Riordan, M.V.3
  • 36
    • 34247583794 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 phosphorylates hypoxia-inducible factor-1 alpha and mediates its destabilization in a VHL-independent manner
    • Flugel D, Gorlach A, Michiels C, Kietzmann T (2007) Glycogen synthase kinase-3 phosphorylates hypoxia-inducible factor-1 alpha and mediates its destabilization in a VHL-independent manner. Mol Cell Biol 27:3253-3265
    • (2007) Mol Cell Biol , vol.27 , pp. 3253-3265
    • Flugel, D.1    Gorlach, A.2    Michiels, C.3    Kietzmann, T.4
  • 37
    • 33845403070 scopus 로고    scopus 로고
    • Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor-1α
    • Mylonis I, Chachami G, Samiotaki M et al (2006) Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor-1α. J Biol Chem 281:33095-33106
    • (2006) J Biol Chem , vol.281 , pp. 33095-33106
    • Mylonis, I.1    Chachami, G.2    Samiotaki, M.3
  • 38
    • 0024273450 scopus 로고
    • Regulation of the erythropoietin gene: Evidence that the oxygen sensor is a heme protein
    • Goldberg MA, Dunning SP, Bunn HF (1988) Regulation of the erythropoietin gene: Evidence that the oxygen sensor is a heme protein. Science 242:1412-1415
    • (1988) Science , vol.242 , pp. 1412-1415
    • Goldberg, M.A.1    Dunning, S.P.2    Bunn, H.F.3
  • 39
    • 24144467846 scopus 로고    scopus 로고
    • ROS: Really involved in oxygen sensing
    • Kaelin JWG (2005) ROS: Really involved in oxygen sensing. Cell Metab 1:357-358
    • (2005) Cell Metab , vol.1 , pp. 357-358
    • Kaelin, J.W.G.1
  • 40
    • 0035971220 scopus 로고    scopus 로고
    • Evidence for the involvement of diacylglycerol kinase in the activation of hypoxia-inducible transcription factor 1 by low oxygen tension
    • Aragones J, Jones DR, Martin S et al (2001) Evidence for the involvement of diacylglycerol kinase in the activation of hypoxia-inducible transcription factor 1 by low oxygen tension. J Biol Chem 276:10548-10555
    • (2001) J Biol Chem , vol.276 , pp. 10548-10555
    • Aragones, J.1    Jones, D.R.2    Martin, S.3
  • 41
    • 33745303045 scopus 로고    scopus 로고
    • Hypoxia signalling in cancer and approaches to enforce tumour regression
    • Pouyssegur J, Dayan F, Mazure NM (2006) Hypoxia signalling in cancer and approaches to enforce tumour regression. Nature 441:437-443
    • (2006) Nature , vol.441 , pp. 437-443
    • Pouyssegur, J.1    Dayan, F.2    Mazure, N.M.3
  • 42
    • 0347334750 scopus 로고    scopus 로고
    • IL-1β mediated up-regulation of HIF-1α via an NFkB/COX-2 pathway identifies HIF-1 as a critical link between inflammation and oncogenesis
    • Jung Y-J, Isaacs JS, Lee S et al (2003) IL-1β mediated up-regulation of HIF-1α via an NFkB/COX-2 pathway identifies HIF-1 as a critical link between inflammation and oncogenesis. FASEB J 17:2115-2117
    • (2003) FASEB J , vol.17 , pp. 2115-2117
    • Jung, Y.-J.1    Isaacs, J.S.2    Lee, S.3
  • 43
    • 0035012605 scopus 로고    scopus 로고
    • HER2 (neu) signaling increases the rate of hypoxia-inducible factor-1a (HIF-1a) synthesis: Novel mechanism for HIF-1-mediated vascular endothelial growth factor expression
    • Laughner E, Taghavi P, Chiles K et al (2001) HER2 (neu) signaling increases the rate of hypoxia-inducible factor-1a (HIF-1a) synthesis: novel mechanism for HIF-1-mediated vascular endothelial growth factor expression. Mol Cell Biol 21:3995-4004
    • (2001) Mol Cell Biol , vol.21 , pp. 3995-4004
    • Laughner, E.1    Taghavi, P.2    Chiles, K.3
  • 44
    • 33746899015 scopus 로고    scopus 로고
    • Akt1 activation can augment hypoxia-inducible factor-1α expression by increasing protein translation through a mammalian target of rapamycin-independent pathway
    • Pore N, Jiang Z, Shu H-K et al (2006) Akt1 activation can augment hypoxia-inducible factor-1α expression by increasing protein translation through a mammalian target of rapamycin-independent pathway. Mol Cancer Res 4:471-479
    • (2006) Mol Cancer Res , vol.4 , pp. 471-479
    • Pore, N.1    Jiang, Z.2    Shu, H.-K.3
  • 45
    • 0037134442 scopus 로고    scopus 로고
    • Lack of evidence for the involvement of the phosphoinositide 3-kinase/ Akt pathway in the activation of hypoxia inducible factors by low oxygen tension
    • αlvarez-Tejado M, Alfranca A, Aragones J et al (2002) Lack of evidence for the involvement of the phosphoinositide 3-kinase/Akt pathway in the activation of hypoxia inducible factors by low oxygen tension. J Biol Chem 28:13508-13517
    • (2002) J Biol Chem , vol.28 , pp. 13508-13517
    • αlvarez-Tejado, M.1    Alfranca, A.2    Aragones, J.3
  • 46
    • 0037177867 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase/Akt signaling is neither required for hypoxic stabilization of HIF-1 alpha nor sufficient for HIF-1-dependent target gene transcription
    • Arsham AM, Plas DR, Thompson CB, Simon MC (2002) Phosphatidylinositol 3-kinase/Akt signaling is neither required for hypoxic stabilization of HIF-1 alpha nor sufficient for HIF-1-dependent target gene transcription. J Biol Chem 277:15162-15170
    • (2002) J Biol Chem , vol.277 , pp. 15162-15170
    • Arsham, A.M.1    Plas, D.R.2    Thompson, C.B.3    Simon, M.C.4
  • 47
    • 0036718539 scopus 로고    scopus 로고
    • Molecular basis of the VHL hereditary cancer syndrome
    • Kaelin WG Jr (2002) Molecular basis of the VHL hereditary cancer syndrome. Nat Rev Cancer 2:673-682
    • (2002) Nat Rev Cancer , vol.2 , pp. 673-682
    • Kaelin Jr., W.G.1
  • 48
    • 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 (1999) The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 399:271-275
    • (1999) Nature , vol.399 , pp. 271-275
    • Maxwell, P.H.1    Wiesener, M.S.2    Chang, G.W.3
  • 50
    • 33745819269 scopus 로고    scopus 로고
    • Formation of primary cilia in the renal epithelium is regulated by the von hippel-lindau tumor suppressor protein
    • Esteban MA, Harten SK, Tran MG, Maxwell PH (2006) Formation of primary cilia in the renal epithelium is regulated by the von hippel-lindau tumor suppressor protein. J Am Soc Nephrol 17:1801-1806
    • (2006) J Am Soc Nephrol , vol.17 , pp. 1801-1806
    • Esteban, M.A.1    Harten, S.K.2    Tran, M.G.3    Maxwell, P.H.4
  • 51
    • 33645748171 scopus 로고    scopus 로고
    • Regulation of E-cadherin expression by VHL and hypoxia-inducible factor
    • Esteban MA, Tran MG, Harten SK et al (2006) Regulation of E-cadherin expression by VHL and hypoxia-inducible factor. Cancer Res 66:3567-3575
    • (2006) Cancer Res , vol.66 , pp. 3567-3575
    • Esteban, M.A.1    Tran, M.G.2    Harten, S.K.3
  • 52
    • 33845724527 scopus 로고    scopus 로고
    • VHL promotes E2 box-dependent E-cadherin transcription by HIF-mediated regulation of SIP1 and snail
    • Evans AJ, Russell RC, Roche O et al (2007) VHL promotes E2 box-dependent E-cadherin transcription by HIF-mediated regulation of SIP1 and snail. Mol Cell Biol 27:157-169
    • (2007) Mol Cell Biol , vol.27 , pp. 157-169
    • Evans, A.J.1    Russell, R.C.2    Roche, O.3
  • 53
    • 33645090169 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1-dependent repression of E-cadherin in von Hippel-Lindau tumor suppressor-null renal cell carcinoma mediated by TCF3, ZFHX1A, and ZFHX1B
    • Krishnamachary B, Zagzag D, Nagasawa H et al (2006) Hypoxia-inducible factor-1-dependent repression of E-cadherin in von Hippel-Lindau tumor suppressor-null renal cell carcinoma mediated by TCF3, ZFHX1A, and ZFHX1B. Cancer Res 66:2725-2731
    • (2006) Cancer Res , vol.66 , pp. 2725-2731
    • Krishnamachary, B.1    Zagzag, D.2    Nagasawa, H.3
  • 54
    • 33646365644 scopus 로고    scopus 로고
    • Lysyl oxidase is essential for hypoxia-induced metastasis
    • Erler JT, Bennewith KL, Nicolau M et al (2006) Lysyl oxidase is essential for hypoxia-induced metastasis. Nature 440:1222-1226
    • (2006) Nature , vol.440 , pp. 1222-1226
    • Erler, J.T.1    Bennewith, K.L.2    Nicolau, M.3
  • 55
    • 27144518237 scopus 로고    scopus 로고
    • A molecular role for lysyl oxidase-like 2 enzyme in snail regulation and tumor progression
    • Peinado H, Del Carmen Iglesias-de la Cruz M, Olmeda D et al (2005) A molecular role for lysyl oxidase-like 2 enzyme in snail regulation and tumor progression. EMBO J 24:3446-3458
    • (2005) EMBO J , vol.24 , pp. 3446-3458
    • Peinado, H.1    Del Carmen Iglesias-de la Cruz, M.2    Olmeda, D.3
  • 56
    • 32944457801 scopus 로고    scopus 로고
    • von Hippel-Lindau tumor suppressor protein regulates the assembly of intercellular junctions in renal cancer cells through hypoxia-inducible factor-independent mechanisms
    • Calzada MJ, Esteban MA, Feijoo-Cuaresma M et al (2006) von Hippel-Lindau tumor suppressor protein regulates the assembly of intercellular junctions in renal cancer cells through hypoxia-inducible factor-independent mechanisms. Cancer Res 66:1553-1560
    • (2006) Cancer Res , vol.66 , pp. 1553-1560
    • Calzada, M.J.1    Esteban, M.A.2    Feijoo-Cuaresma, M.3
  • 57
    • 33744954679 scopus 로고    scopus 로고
    • Endocytic function of von Hippel-Lindau tumor suppressor protein regulates surface localization of fibroblast growth factor receptor 1 and cell motility
    • Hsu T, Adereth Y, Kose N, Dammai V (2006) Endocytic function of von Hippel-Lindau tumor suppressor protein regulates surface localization of fibroblast growth factor receptor 1 and cell motility. J Biol Chem 281:12069-12080
    • (2006) J Biol Chem , vol.281 , pp. 12069-12080
    • Hsu, T.1    Adereth, Y.2    Kose, N.3    Dammai, V.4
  • 58
    • 0035872434 scopus 로고    scopus 로고
    • von Hippel-Lindau protein promotes the assembly of actin and vinculin and inhibits cell motility
    • Kamada M, Suzuki K, Kato Y et al (2001) von Hippel-Lindau protein promotes the assembly of actin and vinculin and inhibits cell motility. Cancer Res 61:4184-4189
    • (2001) Cancer Res , vol.61 , pp. 4184-4189
    • Kamada, M.1    Suzuki, K.2    Kato, Y.3
  • 59
    • 0032795938 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor gene inhibits hepatocyte growth factor/scatter factor-induced invasion and branching morphogenesis in renal carcinoma cells
    • Koochekpour S, Jeffers M, Wang PH et al (1999) The von Hippel-Lindau tumor suppressor gene inhibits hepatocyte growth factor/scatter factor-induced invasion and branching morphogenesis in renal carcinoma cells. Mol Cell Biol 19:5902-5912
    • (1999) Mol Cell Biol , vol.19 , pp. 5902-5912
    • Koochekpour, S.1    Jeffers, M.2    Wang, P.H.3
  • 60
    • 9144232529 scopus 로고    scopus 로고
    • Fibronectin is a hypoxia-independent target of the tumor suppressor VHL
    • Bluyssen HA, Lolkema MP, van Beest M et al (2004) Fibronectin is a hypoxia-independent target of the tumor suppressor VHL. FEBS Lett 556:137-142
    • (2004) FEBS Lett , vol.556 , pp. 137-142
    • Bluyssen, H.A.1    Lolkema, M.P.2    van Beest, M.3
  • 61
    • 0037223823 scopus 로고    scopus 로고
    • Regulation of microtubule stability by the von Hippel-Lindau tumour suppressor protein pVHL
    • Hergovich A, Lisztwan J, Barry R et al (2003) Regulation of microtubule stability by the von Hippel-Lindau tumour suppressor protein pVHL. Nat Cell Biol 5:64-70
    • (2003) Nat Cell Biol , vol.5 , pp. 64-70
    • Hergovich, A.1    Lisztwan, J.2    Barry, R.3
  • 62
    • 0036606006 scopus 로고    scopus 로고
    • VHL-mediated hypoxia regulation of cyclin D1 in renal carcinoma cells
    • Bindra RS, Vasselli JR, Stearman R et al (2002) VHL-mediated hypoxia regulation of cyclin D1 in renal carcinoma cells. Cancer Res 62:3014-3019
    • (2002) Cancer Res , vol.62 , pp. 3014-3019
    • Bindra, R.S.1    Vasselli, J.R.2    Stearman, R.3
  • 63
    • 3042760528 scopus 로고    scopus 로고
    • Ectopic expression of von Hippel-Lindau tumor suppressor induces apoptosis in 786-O renal cell carcinoma cells and regresses tumor growth of 786-O cells in nude mouse
    • Kim, M, Yan Y, Lee K et al (2004) Ectopic expression of von Hippel-Lindau tumor suppressor induces apoptosis in 786-O renal cell carcinoma cells and regresses tumor growth of 786-O cells in nude mouse. Biochem Biophys Res Commun 320:945-950
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 945-950
    • Kim, M.1    Yan, Y.2    Lee, K.3
  • 64
    • 0035136533 scopus 로고    scopus 로고
    • VHL induces renal cell differentiation and growth arrest through integration of cell-cell and cell-extracellular matrix signaling
    • Davidowitz EJ, Schoenfeld AR, Burk RD (2001) VHL induces renal cell differentiation and growth arrest through integration of cell-cell and cell-extracellular matrix signaling. Mol Cell Biol 21:865-874
    • (2001) Mol Cell Biol , vol.21 , pp. 865-874
    • Davidowitz, E.J.1    Schoenfeld, A.R.2    Burk, R.D.3
  • 65
    • 0037093099 scopus 로고    scopus 로고
    • Role of the von Hippel-Lindau tumor suppressor gene in the formation of beta1-integrin fibrillar adhesions
    • Esteban-Barragan MA, Avila P, Alvarez-Tejado M et al (2002) Role of the von Hippel-Lindau tumor suppressor gene in the formation of beta1-integrin fibrillar adhesions. Cancer Res 62:29229-29236
    • (2002) Cancer Res , vol.62 , pp. 29229-29236
    • Esteban-Barragan, M.A.1    Avila, P.2    Alvarez-Tejado, M.3
  • 66
    • 0038339910 scopus 로고    scopus 로고
    • Role of nuclear and cytoplasmic localization in the tumour-suppressor activity of the von Hippel-Lindau protein
    • Lewis MD, Roberts BJ (2003) Role of nuclear and cytoplasmic localization in the tumour-suppressor activity of the von Hippel-Lindau protein. Oncogene 22:3992-3997
    • (2003) Oncogene , vol.22 , pp. 3992-3997
    • Lewis, M.D.1    Roberts, B.J.2
  • 67
    • 33646140913 scopus 로고    scopus 로고
    • p53 stabilization and transactivation by a von Hippel-Lindau protein
    • Roe JS, Kim H, Lee SM et al (2006) p53 stabilization and transactivation by a von Hippel-Lindau protein. Mol Cell 22:395-405
    • (2006) Mol Cell , vol.22 , pp. 395-405
    • Roe, J.S.1    Kim, H.2    Lee, S.M.3
  • 68
    • 33745537991 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumour-suppressor protein interaction with protein kinase Cdelta
    • Iturrioz X, Durgan J, Calleja V et al (2006) The von Hippel-Lindau tumour-suppressor protein interaction with protein kinase Cdelta. Biochem J 397:109-120
    • (2006) Biochem J , vol.397 , pp. 109-120
    • Iturrioz, X.1    Durgan, J.2    Calleja, V.3
  • 69
    • 0030735367 scopus 로고    scopus 로고
    • The von Hippel-Lindau gene product inhibits vascular permeability factor/ vascular endothelial growth factor expression in renal cell carcinoma by blocking protein kinase C pathways
    • Pal S, Claffey KP, Dvorak HF, Mukhopadhyay D (1997) The von Hippel-Lindau gene product inhibits vascular permeability factor/ vascular endothelial growth factor expression in renal cell carcinoma by blocking protein kinase C pathways. J Biol Chem 272:27509-27512
    • (1997) J Biol Chem , vol.272 , pp. 27509-27512
    • Pal, S.1    Claffey, K.P.2    Dvorak, H.F.3    Mukhopadhyay, D.4
  • 70
    • 0035941291 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein mediates ubiquitination of activated atypical protein kinase C
    • Okuda H, Saitoh K, Hirai S et al (2001) The von Hippel-Lindau tumor suppressor protein mediates ubiquitination of activated atypical protein kinase C. J Biol Chem 276:43611-43617
    • (2001) J Biol Chem , vol.276 , pp. 43611-43617
    • Okuda, H.1    Saitoh, K.2    Hirai, S.3
  • 71
    • 0035339044 scopus 로고    scopus 로고
    • Contrasting effects on HIF-1alpha regulation by disease-causing pVHL mutations correlate with patterns of tumourigenesis in von Hippel-Lindau disease
    • Clifford SC, Cockman ME, Smallwood AC et al (2001) Contrasting effects on HIF-1alpha regulation by disease-causing pVHL mutations correlate with patterns of tumourigenesis in von Hippel-Lindau disease. Hum Mol Genet 10:1029-1038
    • (2001) Hum Mol Genet , vol.10 , pp. 1029-1038
    • Clifford, S.C.1    Cockman, M.E.2    Smallwood, A.C.3
  • 72
    • 0035336706 scopus 로고    scopus 로고
    • von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF
    • Hoffman MA, Ohh M, Yang H et al (2001) von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF. Hum Mol Genet 10:1019-1027
    • (2001) Hum Mol Genet , vol.10 , pp. 1019-1027
    • Hoffman, M.A.1    Ohh, M.2    Yang, H.3
  • 73
    • 0032085240 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein is required for proper assembly of an extracellular fibronectin matrix
    • Ohh M, Yauch RL, Lonergan KM et al (1998) The von Hippel-Lindau tumor suppressor protein is required for proper assembly of an extracellular fibronectin matrix. Mol Cell 1:959-968
    • (1998) Mol Cell , vol.1 , pp. 959-968
    • Ohh, M.1    Yauch, R.L.2    Lonergan, K.M.3
  • 74
    • 32944464205 scopus 로고    scopus 로고
    • Characterization of a von Hippel Lindau pathway involved in extracellular matrix remodeling, cell invasion, and angiogenesis
    • Kurban G, Hudon V, Duplan E et al (2006) Characterization of a von Hippel Lindau pathway involved in extracellular matrix remodeling, cell invasion, and angiogenesis. Cancer Res 66:1313-1319
    • (2006) Cancer Res , vol.66 , pp. 1313-1319
    • Kurban, G.1    Hudon, V.2    Duplan, E.3
  • 75
    • 33644748673 scopus 로고    scopus 로고
    • pVHL function is essential for endothelial extracellular matrix deposition
    • Tang N, Mack F, Haase VH et al (2006) pVHL function is essential for endothelial extracellular matrix deposition. Mol Cell Biol 26:2519-2530
    • (2006) Mol Cell Biol , vol.26 , pp. 2519-2530
    • Tang, N.1    Mack, F.2    Haase, V.H.3
  • 76
    • 0030847165 scopus 로고    scopus 로고
    • Defective placental vasculogenesis causes embryonic lethality in VHL-deficient mice
    • Gnarra JR, Ward JM, Porter FD et al (1997) Defective placental vasculogenesis causes embryonic lethality in VHL-deficient mice. Proc Natl Acad Sci U S A 94:9102-9107
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 9102-9107
    • Gnarra, J.R.1    Ward, J.M.2    Porter, F.D.3
  • 77
    • 16244381736 scopus 로고    scopus 로고
    • Inactivation of the arylhydrocarbon receptor nuclear translocator (Arnt) suppresses von Hippel-Lindau disease-associated vascular tumors in mice
    • Rankin EB, Higgins DF, Walisser JA et al (2005) Inactivation of the arylhydrocarbon receptor nuclear translocator (Arnt) suppresses von Hippel-Lindau disease-associated vascular tumors in mice. Mol Cell Biol 25:3163-3172
    • (2005) Mol Cell Biol , vol.25 , pp. 3163-3172
    • Rankin, E.B.1    Higgins, D.F.2    Walisser, J.A.3
  • 78
    • 33645070535 scopus 로고    scopus 로고
    • Renal cyst development in mice with conditional inactivation of the von Hippel-Lindau tumor suppressor
    • Rankin EB, Tomaszewski JE, Haase VH (2006) Renal cyst development in mice with conditional inactivation of the von Hippel-Lindau tumor suppressor. Cancer Res 66:2576-2583
    • (2006) Cancer Res , vol.66 , pp. 2576-2583
    • Rankin, E.B.1    Tomaszewski, J.E.2    Haase, V.H.3
  • 79
    • 9244228551 scopus 로고    scopus 로고
    • In vitro and in vivo models analyzing von Hippel-Lindau disease-specif ic mutations
    • Rathmell WK, Hickey MM, Bezman NA et al (2004) In vitro and in vivo models analyzing von Hippel-Lindau disease-specif ic mutations. Cancer Res 64:8595-8603
    • (2004) Cancer Res , vol.64 , pp. 8595-8603
    • Rathmell, W.K.1    Hickey, M.M.2    Bezman, N.A.3
  • 80
    • 0034050050 scopus 로고    scopus 로고
    • Loss of PTEN facilitates HIF-1-mediated gene expression
    • Zundel W, Schindler C, Haas-Kogan D et al (2000) Loss of PTEN facilitates HIF-1-mediated gene expression. Genes Dev 14:391-396
    • (2000) Genes Dev , vol.14 , pp. 391-396
    • Zundel, W.1    Schindler, C.2    Haas-Kogan, D.3
  • 81
    • 20444445920 scopus 로고    scopus 로고
    • Epidermal growth factor and hypoxia-induced expression of CXC chemokine receptor 4 on non-small cell lung cancer cells is regulated by the phosphatidylinositol 3-kinase/PTEN/AKT/mammalian target of rapamycin signaling pathway and activation of hypoxia inducible factor-1alpha
    • Phillips RJ, Mestas J, Gharaee-Kermani M et al (2005) Epidermal growth factor and hypoxia-induced expression of CXC chemokine receptor 4 on non-small cell lung cancer cells is regulated by the phosphatidylinositol 3-kinase/PTEN/AKT/mammalian target of rapamycin signaling pathway and activation of hypoxia inducible factor-1alpha. J Biol Chem 280:22473-22481
    • (2005) J Biol Chem , vol.280 , pp. 22473-22481
    • Phillips, R.J.1    Mestas, J.2    Gharaee-Kermani, M.3
  • 82
    • 0034654174 scopus 로고    scopus 로고
    • Modulation of hypoxia-inducible factor 1alpha expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: Implications for tumor angiogenesis and therapeutics
    • Zhong H, Chiles K, Feldser D et al (2000) Modulation of hypoxia-inducible factor 1alpha expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: Implications for tumor angiogenesis and therapeutics. Cancer Res 60:1541-1545
    • (2000) Cancer Res , vol.60 , pp. 1541-1545
    • Zhong, H.1    Chiles, K.2    Feldser, D.3
  • 83
    • 0035933726 scopus 로고    scopus 로고
    • Hypoxia induces the activation of the phosphatidylinositol 3-kinase/Akt cell survival pathway in PC12 cells: Protective role in apoptosis
    • αlvarez-Tejado M, Naranjo-Suarez S, Jimenez C et al (2001) Hypoxia induces the activation of the phosphatidylinositol 3-kinase/Akt cell survival pathway in PC12 cells: Protective role in apoptosis. J Biol Chem 276:22368-22374
    • (2001) J Biol Chem , vol.276 , pp. 22368-22374
    • αlvarez-Tejado, M.1    Naranjo-Suarez, S.2    Jimenez, C.3
  • 85
    • 0041920901 scopus 로고    scopus 로고
    • TSC2 regulates VEGF through mTOR-dependent and-independent pathways
    • Brugarolas JB, Vazquez F, Reddy A et al (2003) TSC2 regulates VEGF through mTOR-dependent and-independent pathways. Cancer Cell 4:147-158
    • (2003) Cancer Cell , vol.4 , pp. 147-158
    • Brugarolas, J.B.1    Vazquez, F.2    Reddy, A.3
  • 86
    • 10044276783 scopus 로고    scopus 로고
    • Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/ TSC2 tumor suppressor complex
    • Brugarolas J, Lei K, Hurley RL et al (2004) Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex. Genes Dev 18:2893-2904
    • (2004) Genes Dev , vol.18 , pp. 2893-2904
    • Brugarolas, J.1    Lei, K.2    Hurley, R.L.3
  • 87
    • 32944456143 scopus 로고    scopus 로고
    • Mutations in the PI3K/PTEN/TSC2 pathway contribute to mammalian target of rapamycin activity and increased translation under hypoxic conditions
    • Kaper F, Dornhoefer N, Giaccia AJ (2006) Mutations in the PI3K/PTEN/TSC2 pathway contribute to mammalian target of rapamycin activity and increased translation under hypoxic conditions. Cancer Res 66:1561-1569
    • (2006) Cancer Res , vol.66 , pp. 1561-1569
    • Kaper, F.1    Dornhoefer, N.2    Giaccia, A.J.3
  • 88
    • 33747488399 scopus 로고    scopus 로고
    • PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR
    • Bernardi R, Guernah I, Jin D et al (2006) PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR. Nature 442:779-785
    • (2006) Nature , vol.442 , pp. 779-785
    • Bernardi, R.1    Guernah, I.2    Jin, D.3
  • 89
    • 0037447245 scopus 로고    scopus 로고
    • Protein homeostasis: A degrading role for Int6/eIF3e
    • von Arnim AG, Chamovitz DA (2003) Protein homeostasis: A degrading role for Int6/eIF3e. Curr Biol 13:R323-325
    • (2003) Curr Biol , vol.13
    • von Arnim, A.G.1    Chamovitz, D.A.2
  • 90
    • 34250354450 scopus 로고    scopus 로고
    • Mammalian tumor suppressor Int6 specifically targets HIF-2alpha for degradation by hypoxiaand pVHL-independent regulation
    • Chen L, Uchida K, Endler A, Shibasaki F (2007) Mammalian tumor suppressor Int6 specifically targets HIF-2alpha for degradation by hypoxiaand pVHL-independent regulation. J Biol Chem 282:12707-12716
    • (2007) J Biol Chem , vol.282 , pp. 12707-12716
    • Chen, L.1    Uchida, K.2    Endler, A.3    Shibasaki, F.4
  • 91
    • 2642574174 scopus 로고    scopus 로고
    • p300 relieves p53-evoked transcriptional repression of hypoxia-inducible factor-1 (HIF-1)
    • Schmid T, Zhou J, Kohl R, Brune B (2004) p300 relieves p53-evoked transcriptional repression of hypoxia-inducible factor-1 (HIF-1). Biochem J 380:289-295
    • (2004) Biochem J , vol.380 , pp. 289-295
    • Schmid, T.1    Zhou, J.2    Kohl, R.3    Brune, B.4
  • 92
    • 11344292626 scopus 로고    scopus 로고
    • Binding of natively unfolded HIF-1alpha ODD domain to p53
    • Sanchez-Puig N, Veprintsev DB, Fersht AR (2005) Binding of natively unfolded HIF-1alpha ODD domain to p53. Mol Cell 17:11-21
    • (2005) Mol Cell , vol.17 , pp. 11-21
    • Sanchez-Puig, N.1    Veprintsev, D.B.2    Fersht, A.R.3
  • 93
    • 2942590732 scopus 로고    scopus 로고
    • Exploiting tumour hypoxia in cancer treatment
    • Brown JM, Wilson WR (2004) Exploiting tumour hypoxia in cancer treatment. Nat Rev Cancer 4:437-447
    • (2004) Nat Rev Cancer , vol.4 , pp. 437-447
    • Brown, J.M.1    Wilson, W.R.2
  • 94
    • 0031000736 scopus 로고    scopus 로고
    • A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development
    • Ema M, Taya S, Yokotani N et al (1997) A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development. Proc Natl Acad Sci U S A 94:4273-4278
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 4273-4278
    • Ema, M.1    Taya, S.2    Yokotani, N.3
  • 95
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • Tian H, McKnight SL, Russell DW (1997) Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev 11:72-82
    • (1997) Genes Dev , vol.11 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2    Russell, D.W.3
  • 96
    • 0037315337 scopus 로고    scopus 로고
    • Widespread hypoxia-inducible expression of HIF-2alpha in distinct cell populations of different organs
    • Wiesener MS, Jurgensen JS, Rosenberger C et al (2003) Widespread hypoxia-inducible expression of HIF-2alpha in distinct cell populations of different organs. FASEB J 17:271-273
    • (2003) FASEB J , vol.17 , pp. 271-273
    • Wiesener, M.S.1    Jurgensen, J.S.2    Rosenberger, C.3
  • 97
    • 0032581277 scopus 로고    scopus 로고
    • Role of HIF-1alpha in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis
    • [published erratum appears in Nature 1998; 395:525]
    • Carmeliet P, Dor Y, Herbert JM et al (1998) Role of HIF-1alpha in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis [published erratum appears in Nature 1998; 395:525]. Nature 394:485-490
    • (1998) Nature , vol.394 , pp. 485-490
    • Carmeliet, P.1    Dor, Y.2    Herbert, J.M.3
  • 98
    • 0032167784 scopus 로고    scopus 로고
    • The human hypoxia-inducible factor 1alpha gene: HIF1A structure and evolutionary conservation
    • Iyer NV, Leung SW, Semenza GL (1998) The human hypoxia-inducible factor 1alpha gene: HIF1A structure and evolutionary conservation. Genomics 52:159-165
    • (1998) Genomics , vol.52 , pp. 159-165
    • Iyer, N.V.1    Leung, S.W.2    Semenza, G.L.3
  • 99
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1 alpha is required for solid tumor formation and embryonic vascularization
    • Ryan HE, Lo J, Johnson RS (1998) HIF-1 alpha is required for solid tumor formation and embryonic vascularization. EMBO J 17:3005-3015
    • (1998) EMBO J , vol.17 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 100
    • 0035983324 scopus 로고    scopus 로고
    • Loss of HIF-2alpha and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice
    • Compernolle V, Brusselmans K, Acker T et al (2002) Loss of HIF-2alpha and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice. Nat Med 8:702-710
    • (2002) Nat Med , vol.8 , pp. 702-710
    • Compernolle, V.1    Brusselmans, K.2    Acker, T.3
  • 101
    • 0034682513 scopus 로고    scopus 로고
    • The transcription factor EPAS-1/hypoxia-inducible factor 2alpha plays an important role in vascular remodeling
    • Peng J, Zhang L, Drysdale L, Fong GH (2000) The transcription factor EPAS-1/hypoxia-inducible factor 2alpha plays an important role in vascular remodeling. Proc Natl Acad Sci U S A 97:8386-8391
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8386-8391
    • Peng, J.1    Zhang, L.2    Drysdale, L.3    Fong, G.H.4
  • 102
    • 0344826529 scopus 로고    scopus 로고
    • Multiple organ pathology, metabolic abnormalities and impaired homeostasis of reactive oxygen species in Epas1-/-mice
    • Scortegagna M, Ding K, Oktay Y et al (2003) Multiple organ pathology, metabolic abnormalities and impaired homeostasis of reactive oxygen species in Epas1-/-mice. Nat Genet 35:331-340
    • (2003) Nat Genet , vol.35 , pp. 331-340
    • Scortegagna, M.1    Ding, K.2    Oktay, Y.3
  • 103
    • 2342597973 scopus 로고    scopus 로고
    • Inhibition of HIF2alpha is sufficient to suppress pVHL-defective tumor growth
    • Kondo K, Kim WY, Lechpammer M, Kaelin WG Jr (2003) Inhibition of HIF2alpha is sufficient to suppress pVHL-defective tumor growth. PLoS Biol 1:E83
    • (2003) PLoS Biol , vol.1
    • Kondo, K.1    Kim, W.Y.2    Lechpammer, M.3    Kaelin Jr., W.G.4
  • 104
    • 20744445650 scopus 로고    scopus 로고
    • Contrasting properties of hypoxia-inducible factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-associated renal cell carcinoma
    • Raval RR, Lau KW, Tran MG et al (2005) Contrasting properties of hypoxia-inducible factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-associated renal cell carcinoma. Mol Cell Biol 25:5675-5686
    • (2005) Mol Cell Biol , vol.25 , pp. 5675-5686
    • Raval, R.R.1    Lau, K.W.2    Tran, M.G.3
  • 105
    • 16844386959 scopus 로고    scopus 로고
    • Targeted replacement of hypoxia-inducible factor-1alpha by a hypoxia-inducible factor-2alpha knock-in allele promotes tumor growth
    • Covello KL, Simon MC, Keith B (2005) Targeted replacement of hypoxia-inducible factor-1alpha by a hypoxia-inducible factor-2alpha knock-in allele promotes tumor growth. Cancer Res 65:2277-2286
    • (2005) Cancer Res , vol.65 , pp. 2277-2286
    • Covello, K.L.1    Simon, M.C.2    Keith, B.3
  • 106
    • 33644747418 scopus 로고    scopus 로고
    • HIF-2α regulates Oct-4: Effects of hypoxia on stem cell function, embryonic development, and tumor growth
    • Covello KL, Kehler J, Yu H et al (2006) HIF-2α regulates Oct-4: effects of hypoxia on stem cell function, embryonic development, and tumor growth. Genes Dev 20:557-570
    • (2006) Genes Dev , vol.20 , pp. 557-570
    • Covello, K.L.1    Kehler, J.2    Yu, H.3
  • 107
    • 34047156190 scopus 로고    scopus 로고
    • HIF-2alpha promotes hypoxic cell proliferation by enhancing c-Myc transcriptional activity
    • Gordan JD, Bertout JA, Hu CJ et al (2007) HIF-2alpha promotes hypoxic cell proliferation by enhancing c-Myc transcriptional activity. Cancer Cell 11:335-347
    • (2007) Cancer Cell , vol.11 , pp. 335-347
    • Gordan, J.D.1    Bertout, J.A.2    Hu, C.J.3
  • 108
    • 23644435597 scopus 로고    scopus 로고
    • Genetic evidence for a tumor suppressor role of HIF-2alpha
    • Acker T, Diez-Juan A, Aragones J et al (2005) Genetic evidence for a tumor suppressor role of HIF-2alpha. Cancer Cell 8:131-141
    • (2005) Cancer Cell , vol.8 , pp. 131-141
    • Acker, T.1    Diez-Juan, A.2    Aragones, J.3
  • 109
    • 0035860147 scopus 로고    scopus 로고
    • Relation of hypoxia inducible factor 1 alpha and 2 alpha in operable non-small cell lung cancer to angiogenic/molecular profile of tumours and survival
    • Giatromanolaki A, Koukourakis MI, Sivridis E et al (2001) Relation of hypoxia inducible factor 1 alpha and 2 alpha in operable non-small cell lung cancer to angiogenic/molecular profile of tumours and survival. Br J Cancer 85:881-890
    • (2001) Br J Cancer , vol.85 , pp. 881-890
    • Giatromanolaki, A.1    Koukourakis, M.I.2    Sivridis, E.3
  • 110
    • 11144222884 scopus 로고    scopus 로고
    • Prognostic impact of hypoxia-inducible factors 1alpha and 2alpha in colorectal cancer patients: Correlation with tumor angiogenesis and cyclooxygenase-2 expression
    • Yoshimura H, Dhar DK, Kohno H et al (2004) Prognostic impact of hypoxia-inducible factors 1alpha and 2alpha in colorectal cancer patients: Correlation with tumor angiogenesis and cyclooxygenase-2 expression. Clin Cancer Res 10:8554-8560
    • (2004) Clin Cancer Res , vol.10 , pp. 8554-8560
    • Yoshimura, H.1    Dhar, D.K.2    Kohno, H.3
  • 111
    • 33750630119 scopus 로고    scopus 로고
    • Recruitment of HIF-1alpha and HIF-2alpha to common target genes is differentially regulated in neuroblastoma: HIF-2alpha promotes an aggressive phenotype
    • Holmquist-Mengelbier L, Fredlund E, Lofstedt T et al (2006) Recruitment of HIF-1alpha and HIF-2alpha to common target genes is differentially regulated in neuroblastoma: HIF-2alpha promotes an aggressive phenotype. Cancer Cell 10:413-423
    • (2006) Cancer Cell , vol.10 , pp. 413-423
    • Holmquist-Mengelbier, L.1    Fredlund, E.2    Lofstedt, T.3
  • 112
    • 0036721256 scopus 로고    scopus 로고
    • Association of hypoxia-inducible factors 1alpha and 2alpha with activated angiogenic pathways and prognosis in patients with endometrial carcinoma
    • Sivridis E, Giatromanolaki A, Gatter KC et al (2002) Association of hypoxia-inducible factors 1alpha and 2alpha with activated angiogenic pathways and prognosis in patients with endometrial carcinoma. Cancer 95:1055-1063
    • (2002) Cancer , vol.95 , pp. 1055-1063
    • Sivridis, E.1    Giatromanolaki, A.2    Gatter, K.C.3
  • 113
    • 33645026059 scopus 로고    scopus 로고
    • Overexpression of von Hippel-Lindau tumor suppressor protein and antisense HIF-1alpha eradicates gliomas
    • Sun X, Liu M, Wei Y et al (2006) Overexpression of von Hippel-Lindau tumor suppressor protein and antisense HIF-1alpha eradicates gliomas Cancer Gene Ther 13:428-435
    • (2006) Cancer Gene Ther , vol.13 , pp. 428-435
    • Sun, X.1    Liu, M.2    Wei, Y.3
  • 114
    • 33747366672 scopus 로고    scopus 로고
    • Cell-specific regulation of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha stabilization and transactivation in a graded oxygen environment
    • Bracken C.P, Fedele AO, Linke S et al (2006) Cell-specific regulation of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha stabilization and transactivation in a graded oxygen environment. J Biol Chem 281:22575-22585
    • (2006) J Biol Chem , vol.281 , pp. 22575-22585
    • Bracken, C.P.1    Fedele, A.O.2    Linke, S.3
  • 115
    • 33745685879 scopus 로고    scopus 로고
    • Role of hypoxiainducible factor (HIF)-1alpha versus HIF-2alpha in the regulation of HIF target genes in response to hypoxia, insulin-like growth factor-I, or loss of von Hippel-Lindau function: Implications for targeting the HIF pathway
    • Carroll VA, Ashcroft M (2006) Role of hypoxiainducible factor (HIF)-1alpha versus HIF-2alpha in the regulation of HIF target genes in response to hypoxia, insulin-like growth factor-I, or loss of von Hippel-Lindau function: Implications for targeting the HIF pathway. Cancer Res 66:6264-6270
    • (2006) Cancer Res , vol.66 , pp. 6264-6270
    • Carroll, V.A.1    Ashcroft, M.2
  • 116
    • 0037699955 scopus 로고    scopus 로고
    • Angiogenesis in health and disease
    • Carmeliet P (2003) Angiogenesis in health and disease. Nat Med 9:653-660
    • (2003) Nat Med , vol.9 , pp. 653-660
    • Carmeliet, P.1
  • 117
    • 0034671706 scopus 로고    scopus 로고
    • Placental cell fates are regulated in vivo by HIF-mediated hypoxia responses
    • [In Process Citation]
    • Adelman DM, Gertsenstein M, Nagy A et al (2000) Placental cell fates are regulated in vivo by HIF-mediated hypoxia responses [In Process Citation]. Genes Dev 14:3191-3203
    • (2000) Genes Dev , vol.14 , pp. 3191-3203
    • Adelman, D.M.1    Gertsenstein, M.2    Nagy, A.3
  • 118
    • 0030943461 scopus 로고    scopus 로고
    • Abnormal angiogenesis and responses to glucose and oxygen deprivation in mice lacking the protein ARNT
    • Maltepe E, Schmidt JV, Baunoch D et al (1997) Abnormal angiogenesis and responses to glucose and oxygen deprivation in mice lacking the protein ARNT. Nature 386:403-407
    • (1997) Nature , vol.386 , pp. 403-407
    • Maltepe, E.1    Schmidt, J.V.2    Baunoch, D.3
  • 119
    • 30444442692 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor activity in endothelial cells disrupts embryonic cardiovascular development
    • Licht AH, Muller-Holtkamp F, Flamme I, Breier G (2006) Inhibition of hypoxia-inducible factor activity in endothelial cells disrupts embryonic cardiovascular development. Blood 107:584-590
    • (2006) Blood , vol.107 , pp. 584-590
    • Licht, A.H.1    Muller-Holtkamp, F.2    Flamme, I.3    Breier, G.4
  • 120
    • 11244315697 scopus 로고    scopus 로고
    • Transcriptional regulation of vascular endothelial cell responses to hypoxia by HIF-1
    • Manalo DJ, Rowan A, Lavoie T et al (2005) Transcriptional regulation of vascular endothelial cell responses to hypoxia by HIF-1. Blood 105:659-669
    • (2005) Blood , vol.105 , pp. 659-669
    • Manalo, D.J.1    Rowan, A.2    Lavoie, T.3
  • 121
    • 7944224442 scopus 로고    scopus 로고
    • Loss of HIF-1alpha in endothelial cells disrupts a hypoxia-driven VEGF autocrine loop necessary for tumorigenesis
    • Tang N, Wang L, Esko J et al (2004) Loss of HIF-1alpha in endothelial cells disrupts a hypoxia-driven VEGF autocrine loop necessary for tumorigenesis. Cancer Cell 6:485-495
    • (2004) Cancer Cell , vol.6 , pp. 485-495
    • Tang, N.1    Wang, L.2    Esko, J.3
  • 122
    • 0029761644 scopus 로고    scopus 로고
    • Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1
    • Forsythe JA, Jiang BH, Iyer NV et al (1996) Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1. Mol Cell Biol 16:4604-4613
    • (1996) Mol Cell Biol , vol.16 , pp. 4604-4613
    • Forsythe, J.A.1    Jiang, B.H.2    Iyer, N.V.3
  • 123
    • 0030751493 scopus 로고    scopus 로고
    • Differential transcriptional regulation of the two vascular endothelial growth factor receptor genes. Flt-1, but not Flk-1/KDR, is upregulated by hypoxia
    • Gerber HP, Condorelli F, Park J, Ferrara N (1997) Differential transcriptional regulation of the two vascular endothelial growth factor receptor genes. Flt-1, but not Flk-1/KDR, is upregulated by hypoxia. J Biol Chem 272:23659-23667
    • (1997) J Biol Chem , vol.272 , pp. 23659-23667
    • Gerber, H.P.1    Condorelli, F.2    Park, J.3    Ferrara, N.4
  • 124
    • 18244372452 scopus 로고    scopus 로고
    • Endothelium-intrinsic requirement for Hif-2alpha during vascular development
    • Duan LJ, Zhang-Benoit Y, Fong GH (2005) Endothelium-intrinsic requirement for Hif-2alpha during vascular development. Circulation 111:2227-2232
    • (2005) Circulation , vol.111 , pp. 2227-2232
    • Duan, L.J.1    Zhang-Benoit, Y.2    Fong, G.H.3
  • 125
    • 0037470245 scopus 로고    scopus 로고
    • Cooperative interaction of hypoxia-inducible factor-2alpha (HIF-2alpha) and Ets-1 in the transcriptional activation of vascular endothelial growth factor receptor-2 (Flk-1)
    • Elvert G, Kappel A, Heidenreich R et al (2003) Cooperative interaction of hypoxia-inducible factor-2alpha (HIF-2alpha) and Ets-1 in the transcriptional activation of vascular endothelial growth factor receptor-2 (Flk-1). J Biol Chem 278:7520-7530
    • (2003) J Biol Chem , vol.278 , pp. 7520-7530
    • Elvert, G.1    Kappel, A.2    Heidenreich, R.3
  • 126
    • 0344436031 scopus 로고    scopus 로고
    • Identification of vascular endothelial growth factor (VEGF) receptor-2 (Flk-1) promoter/enhancer sequences sufficient for angioblast and endothelial cell-specific transcription in transgenic mice
    • Kappel A, Ronicke V, Damert A et al (1999) Identification of vascular endothelial growth factor (VEGF) receptor-2 (Flk-1) promoter/enhancer sequences sufficient for angioblast and endothelial cell-specific transcription in transgenic mice. Blood 93:4284-4292
    • (1999) Blood , vol.93 , pp. 4284-4292
    • Kappel, A.1    Ronicke, V.2    Damert, A.3
  • 127
    • 3343013829 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 gene promotes angiogenesis through the transactivation of both vascular endothelial growth factor and its receptor, Flt-1
    • Takeda N, Maemura K, Imai Y et al (2004) Endothelial PAS domain protein 1 gene promotes angiogenesis through the transactivation of both vascular endothelial growth factor and its receptor, Flt-1. Circ Res 95:146-153
    • (2004) Circ Res , vol.95 , pp. 146-153
    • Takeda, N.1    Maemura, K.2    Imai, Y.3
  • 128
    • 33645504221 scopus 로고    scopus 로고
    • Hypoxic induction of an HIF-1alpha-dependent bFGF autocrine loop drives angiogenesis in human endothelial cells
    • Calvani M, Rapisarda A, Uranchimeg B et al (2006) Hypoxic induction of an HIF-1alpha-dependent bFGF autocrine loop drives angiogenesis in human endothelial cells. Blood 107:2705-2712
    • (2006) Blood , vol.107 , pp. 2705-2712
    • Calvani, M.1    Rapisarda, A.2    Uranchimeg, B.3
  • 129
    • 0032387693 scopus 로고    scopus 로고
    • Hypoxia increases thrombospondin-1 transcript and protein in cultured endothelial cells
    • Phelan MW, Forman LW, Perrine SP, Faller DV (1998) Hypoxia increases thrombospondin-1 transcript and protein in cultured endothelial cells. J Lab Clin Med 132:519-529
    • (1998) J Lab Clin Med , vol.132 , pp. 519-529
    • Phelan, M.W.1    Forman, L.W.2    Perrine, S.P.3    Faller, D.V.4
  • 130
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • Warburg O (1956) On the origin of cancer cells. Science 123:309-314
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 131
    • 33744783432 scopus 로고    scopus 로고
    • Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance
    • Fantin VR, St-Pierre J, Leder P (2006) Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance. Cancer Cell 9:425-434
    • (2006) Cancer Cell , vol.9 , pp. 425-434
    • Fantin, V.R.1    St-Pierre, J.2    Leder, P.3
  • 132
    • 33646917296 scopus 로고    scopus 로고
    • The plasma membrane lactate transporter MCT4, but not MCT1, is up-regulated by hypoxia through a HIF-1α-dependent mechanism
    • Ullah MS, Davies AJ, Halestrap AP (2006) The plasma membrane lactate transporter MCT4, but not MCT1, is up-regulated by hypoxia through a HIF-1α-dependent mechanism. J Biol Chem 281:9030-9037
    • (2006) J Biol Chem , vol.281 , pp. 9030-9037
    • Ullah, M.S.1    Davies, A.J.2    Halestrap, A.P.3
  • 133
    • 33644614520 scopus 로고    scopus 로고
    • HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia
    • Kim J-W, Tchernyshyov I, Semenza GL, Dang CV (2006) HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia. Cell Metabolism 3:177-185
    • (2006) Cell Metabolism , vol.3 , pp. 177-185
    • Kim, J.-W.1    Tchernyshyov, I.2    Semenza, G.L.3    Dang, C.V.4
  • 134
    • 33644622570 scopus 로고    scopus 로고
    • HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
    • Papandreou I, Cairns RA, Fontana L et al (2006) HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. Cell Metabolism 3:187-197
    • (2006) Cell Metabolism , vol.3 , pp. 187-197
    • Papandreou, I.1    Cairns, R.A.2    Fontana, L.3
  • 135
    • 2942724235 scopus 로고    scopus 로고
    • mTOR inhibition reverses Akt-dependent prostate intraepithelial neoplasia through regulation of apoptotic and HIF-1-dependent pathways
    • Majumder PK, Febbo PG, Bikoff R et al (2004) mTOR inhibition reverses Akt-dependent prostate intraepithelial neoplasia through regulation of apoptotic and HIF-1-dependent pathways. Nat Med 10:594-601
    • (2004) Nat Med , vol.10 , pp. 594-601
    • Majumder, P.K.1    Febbo, P.G.2    Bikoff, R.3
  • 136
    • 26444570010 scopus 로고    scopus 로고
    • Accumulation of Krebs cycle intermediates and over-expression of HIF1{alpha} in tumours which result from germline FH and SDH mutations
    • Pollard PJ, Briere JJ, Alam NA et al (2005) Accumulation of Krebs cycle intermediates and over-expression of HIF1{alpha} in tumours which result from germline FH and SDH mutations. Hum Mol Genet 14:2231-2239
    • (2005) Hum Mol Genet , vol.14 , pp. 2231-2239
    • Pollard, P.J.1    Briere, J.J.2    Alam, N.A.3
  • 137
    • 33745918951 scopus 로고    scopus 로고
    • TIGAR, a p53-inducible regulator of glycolysis and apoptosis
    • Bensaad K, Tsuruta A, Selak MA et al (2006) TIGAR, a p53-inducible regulator of glycolysis and apoptosis. Cell 126:107-120
    • (2006) Cell , vol.126 , pp. 107-120
    • Bensaad, K.1    Tsuruta, A.2    Selak, M.A.3
  • 138
    • 0038037735 scopus 로고    scopus 로고
    • Regulation of angiogenesis by hypoxia: Role of the HIF system
    • Pugh CW, Ratcliffe PJ (2003) Regulation of angiogenesis by hypoxia: Role of the HIF system. Nat Med 9:677-684
    • (2003) Nat Med , vol.9 , pp. 677-684
    • Pugh, C.W.1    Ratcliffe, P.J.2
  • 139
    • 33750619348 scopus 로고    scopus 로고
    • Glucose metabolism and cancer
    • Shaw RJ (2006) Glucose metabolism and cancer. Curr Opin Cell Biol 18:598-608
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 598-608
    • Shaw, R.J.1
  • 140
    • 25444432052 scopus 로고    scopus 로고
    • Genetic instability: The dark side of the hypoxic response
    • To KK, Koshiji M, Hammer S, Huang LE (2005) Genetic instability: The dark side of the hypoxic response. Cell Cycle 4:881-882
    • (2005) Cell Cycle , vol.4 , pp. 881-882
    • To, K.K.1    Koshiji, M.2    Hammer, S.3    Huang, L.E.4
  • 141
    • 4444311880 scopus 로고    scopus 로고
    • Hypoxia inducible factor-1α as a cancer drug target
    • Powis G, Kirkpatrick L (2004) Hypoxia inducible factor-1α as a cancer drug target. Mol Cancer Ther 3:647-654
    • (2004) Mol Cancer Ther , vol.3 , pp. 647-654
    • Powis, G.1    Kirkpatrick, L.2
  • 142
    • 3142622930 scopus 로고    scopus 로고
    • Small molecule blockade of transcriptional coactivation of the hypoxia-inducible factor pathway
    • Kung AL, Zabludoff SD, France DS et al (2004) Small molecule blockade of transcriptional coactivation of the hypoxia-inducible factor pathway. Cancer Cell 6:33-43
    • (2004) Cancer Cell , vol.6 , pp. 33-43
    • Kung, A.L.1    Zabludoff, S.D.2    France, D.S.3
  • 143
    • 30944442431 scopus 로고    scopus 로고
    • Small interfering RNA expression vector targeting hypoxia-inducible factor 1 alpha inhibits tumor growth in hepatobiliary and pancreatic cancers
    • Mizuno T, Nagao M, Yamada Y et al (2005) Small interfering RNA expression vector targeting hypoxia-inducible factor 1 alpha inhibits tumor growth in hepatobiliary and pancreatic cancers. Cancer Gene Ther 13:131-140
    • (2005) Cancer Gene Ther , vol.13 , pp. 131-140
    • Mizuno, T.1    Nagao, M.2    Yamada, Y.3
  • 144
    • 33845351323 scopus 로고    scopus 로고
    • Hypoxia-targeting drugs as new cancer chemotherapeutics
    • Nagasawa H, Uto Y, Kirk KL, Hori H (2006) Hypoxia-targeting drugs as new cancer chemotherapeutics. Biol Pharm Bull 29:2335-2342
    • (2006) Biol Pharm Bull , vol.29 , pp. 2335-2342
    • Nagasawa, H.1    Uto, Y.2    Kirk, K.L.3    Hori, H.4
  • 145
    • 0036007293 scopus 로고    scopus 로고
    • Expression of HIF-1α by human macrophages: Implications for the use of macrophages in hypoxiaregulated cancer gene therapy
    • Burke B, Tang N, Corke KP et al (2002) Expression of HIF-1α by human macrophages: Implications for the use of macrophages in hypoxiaregulated cancer gene therapy. J Pathol 196:204-212
    • (2002) J Pathol , vol.196 , pp. 204-212
    • Burke, B.1    Tang, N.2    Corke, K.P.3
  • 146
    • 85047697737 scopus 로고    scopus 로고
    • Anticancer efficacy of systemically delivered anaerobic bacteria as gene therapy vectors targeting tumor hypoxia/necrosis
    • Liu S-C, Minton NP, Giaccia AJ, Brown JM (2002) Anticancer efficacy of systemically delivered anaerobic bacteria as gene therapy vectors targeting tumor hypoxia/necrosis. Gene Ther 9:291-296
    • (2002) Gene Ther , vol.9 , pp. 291-296
    • Liu, S.-C.1    Minton, N.P.2    Giaccia, A.J.3    Brown, J.M.4
  • 147
    • 0036399291 scopus 로고    scopus 로고
    • New oncolytic adenovirus with hypoxia-and estrogen receptor-regulated replication
    • Hernandez-Alcoceba R, Pihalja M, Qian D, Clarke MF (2002) New oncolytic adenovirus with hypoxia-and estrogen receptor-regulated replication. Hum Gene Ther 13:1737-1750
    • (2002) Hum Gene Ther , vol.13 , pp. 1737-1750
    • Hernandez-Alcoceba, R.1    Pihalja, M.2    Qian, D.3    Clarke, M.F.4
  • 148
    • 0142157670 scopus 로고    scopus 로고
    • Specific oncolytic effect of a new hypoxia-inducible factor-dependent replicative adenovirus on von Hippel-Lindau-defective renal cell carcinomas
    • Cuevas Y, Hernandez-Alcoceba R, Aragones J et al (2003) Specific oncolytic effect of a new hypoxia-inducible factor-dependent replicative adenovirus on von Hippel-Lindau-defective renal cell carcinomas. Cancer Res 63:6877-6884
    • (2003) Cancer Res , vol.63 , pp. 6877-6884
    • Cuevas, Y.1    Hernandez-Alcoceba, R.2    Aragones, J.3
  • 149
    • 0037509944 scopus 로고    scopus 로고
    • A novel hypoxia-inducible factor (HIF) activated oncolytic adenovirus for cancer therapy
    • Post DE, Van Meir EG (2003) A novel hypoxia-inducible factor (HIF) activated oncolytic adenovirus for cancer therapy. Oncogene 22:2065-2072
    • (2003) Oncogene , vol.22 , pp. 2065-2072
    • Post, D.E.1    Van Meir, E.G.2
  • 150
    • 33744969828 scopus 로고    scopus 로고
    • Energy deregulation: Licensing tumors to grow
    • Garber K (2006) Energy deregulation: Licensing tumors to grow. Science 312:1158-1159
    • (2006) Science , vol.312 , pp. 1158-1159
    • Garber, K.1


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