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Volumn 23, Issue 1, 2013, Pages 18-25

The VHL/HIF axis in clear cell renal carcinoma

Author keywords

Angiogenesis; Hypoxia; Kidney cancer; VEGF; Von Hippel Lindau

Indexed keywords

CYCLIN D1; DNA BINDING PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; HISTONE DEMETHYLASE; HYPOXIA INDUCIBLE FACTOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; OCTAMER TRANSCRIPTION FACTOR 4; ONCOPROTEIN; SCATTER FACTOR RECEPTOR; TUMOR SUPPRESSOR PROTEIN; UBIQUITIN PROTEIN LIGASE; VASCULOTROPIN; VASCULOTROPIN INHIBITOR; VON HIPPEL LINDAU PROTEIN;

EID: 84873091765     PISSN: 1044579X     EISSN: 10963650     Source Type: Journal    
DOI: 10.1016/j.semcancer.2012.06.001     Document Type: Review
Times cited : (311)

References (143)
  • 1
    • 0031445126 scopus 로고    scopus 로고
    • Von Hippel-Lindau disease
    • Maher E., Kaelin W.G. von Hippel-Lindau disease. Medicine 1997, 76:381-391.
    • (1997) Medicine , vol.76 , pp. 381-391
    • Maher, E.1    Kaelin, W.G.2
  • 2
    • 16644373473 scopus 로고    scopus 로고
    • Role of VHL gene mutation in human cancer
    • Kim W.Y., Kaelin W.G. Role of VHL gene mutation in human cancer. Journal of Clinical Oncology 2004, 22:4991-5004.
    • (2004) Journal of Clinical Oncology , vol.22 , pp. 4991-5004
    • Kim, W.Y.1    Kaelin, W.G.2
  • 3
    • 66349100709 scopus 로고    scopus 로고
    • Patterns of gene expression and copy-number alterations in von Hippel-Lindau disease-associated and sporadic clear cell carcinoma of the kidney
    • Beroukhim R., Brunet J.P., Di Napoli A., Mertz K.D., Seeley A., Pires M.M., et al. Patterns of gene expression and copy-number alterations in von Hippel-Lindau disease-associated and sporadic clear cell carcinoma of the kidney. Cancer Research 2009, 69:4674-4681.
    • (2009) Cancer Research , vol.69 , pp. 4674-4681
    • Beroukhim, R.1    Brunet, J.P.2    Di Napoli, A.3    Mertz, K.D.4    Seeley, A.5    Pires, M.M.6
  • 4
    • 33847250856 scopus 로고    scopus 로고
    • Identification of deregulated oncogenic pathways in renal cell carcinoma: an integrated oncogenomic approach based on gene expression profiling
    • Furge K.A., Tan M.H., Dykema K., Kort E., Stadler W., Yao X., et al. Identification of deregulated oncogenic pathways in renal cell carcinoma: an integrated oncogenomic approach based on gene expression profiling. Oncogene 2007, 26:1346-1350.
    • (2007) Oncogene , vol.26 , pp. 1346-1350
    • Furge, K.A.1    Tan, M.H.2    Dykema, K.3    Kort, E.4    Stadler, W.5    Yao, X.6
  • 5
    • 17044452288 scopus 로고    scopus 로고
    • HIF activation identifies early lesions in VHL kidneys: evidence for site-specific tumor suppressor function in the nephron
    • Mandriota S.J., Turner K.J., Davies D.R., Murray P.G., Morgan N.V., Sowter H.M., et al. HIF activation identifies early lesions in VHL kidneys: evidence for site-specific tumor suppressor function in the nephron. Cancer Cells 2002, 1:459-468.
    • (2002) Cancer Cells , vol.1 , pp. 459-468
    • Mandriota, S.J.1    Turner, K.J.2    Davies, D.R.3    Murray, P.G.4    Morgan, N.V.5    Sowter, H.M.6
  • 6
    • 77951727246 scopus 로고    scopus 로고
    • VHL-gene deletion in single renal tubular epithelial cells and renal tubular cysts: further evidence for a cyst-dependent progression pathway of clear cell renal carcinoma in von Hippel-Lindau disease
    • Montani M., Heinimann K., von Teichman A., Rudolph T., Perren A., Moch H. VHL-gene deletion in single renal tubular epithelial cells and renal tubular cysts: further evidence for a cyst-dependent progression pathway of clear cell renal carcinoma in von Hippel-Lindau disease. American Journal of Surgical Pathology 2010, 34:806-815.
    • (2010) American Journal of Surgical Pathology , vol.34 , pp. 806-815
    • Montani, M.1    Heinimann, K.2    von Teichman, A.3    Rudolph, T.4    Perren, A.5    Moch, H.6
  • 7
    • 79251635938 scopus 로고    scopus 로고
    • Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma
    • Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., et al. Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma. Nature 2011, 469:539-542.
    • (2011) Nature , vol.469 , pp. 539-542
    • Varela, I.1    Tarpey, P.2    Raine, K.3    Huang, D.4    Ong, C.K.5    Stephens, P.6
  • 8
    • 75149188170 scopus 로고    scopus 로고
    • Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes
    • Dalgliesh G.L., Furge K., Greenman C., Chen L., Bignell G., Butler A., et al. Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes. Nature 2010, 463:360-363.
    • (2010) Nature , vol.463 , pp. 360-363
    • Dalgliesh, G.L.1    Furge, K.2    Greenman, C.3    Chen, L.4    Bignell, G.5    Butler, A.6
  • 9
    • 77956271441 scopus 로고    scopus 로고
    • Polybromo-associated BRG1-associated factor components BRD7 and BAF180 are critical regulators of p53 required for induction of replicative senescence
    • Burrows A.E., Smogorzewska A., Elledge S.J. Polybromo-associated BRG1-associated factor components BRD7 and BAF180 are critical regulators of p53 required for induction of replicative senescence. Proceedings of the National Academy of Sciences of the United States of America 2010, 107:14280-14285.
    • (2010) Proceedings of the National Academy of Sciences of the United States of America , vol.107 , pp. 14280-14285
    • Burrows, A.E.1    Smogorzewska, A.2    Elledge, S.J.3
  • 10
    • 40949111565 scopus 로고    scopus 로고
    • BAF180 is a critical regulator of p21 induction and a tumor suppressor mutated in breast cancer
    • Xia W., Nagase S., Montia A.G., Kalachikov S.M., Keniry M., Su T., et al. BAF180 is a critical regulator of p21 induction and a tumor suppressor mutated in breast cancer. Cancer Research 2008, 68:1667-1674.
    • (2008) Cancer Research , vol.68 , pp. 1667-1674
    • Xia, W.1    Nagase, S.2    Montia, A.G.3    Kalachikov, S.M.4    Keniry, M.5    Su, T.6
  • 11
    • 78049286684 scopus 로고    scopus 로고
    • Histone demethylases in development and disease
    • Pedersen M.T., Helin K. Histone demethylases in development and disease. Trends in Cell Biology 2010, 20:662-671.
    • (2010) Trends in Cell Biology , vol.20 , pp. 662-671
    • Pedersen, M.T.1    Helin, K.2
  • 12
    • 78650582970 scopus 로고    scopus 로고
    • Histone lysine methylation and demethylation pathways in cancer
    • Varier R.A., Timmers H.T. Histone lysine methylation and demethylation pathways in cancer. Biochimica et Biophysica Acta 2011, 1815:75-89.
    • (2011) Biochimica et Biophysica Acta , vol.1815 , pp. 75-89
    • Varier, R.A.1    Timmers, H.T.2
  • 14
    • 77956690871 scopus 로고    scopus 로고
    • Renal oxygenation suppresses VHL loss-induced senescence that is caused by increased sensitivity to oxidative stress
    • Welford S.M., Dorie M.J., Li X., Haase V.H., Giaccia A.J. Renal oxygenation suppresses VHL loss-induced senescence that is caused by increased sensitivity to oxidative stress. Molecular and Cellular Biology 2010, 30:4595-4603.
    • (2010) Molecular and Cellular Biology , vol.30 , pp. 4595-4603
    • Welford, S.M.1    Dorie, M.J.2    Li, X.3    Haase, V.H.4    Giaccia, A.J.5
  • 15
    • 84856955226 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein regulates gene expression and tumor growth through histone demethylase JARID1C
    • Niu X., Zhang T., Liao L., Zhou L., Lindner D.J., Zhou M., et al. The von Hippel-Lindau tumor suppressor protein regulates gene expression and tumor growth through histone demethylase JARID1C. Oncogene 2012, 31:776-786.
    • (2012) Oncogene , vol.31 , pp. 776-786
    • Niu, X.1    Zhang, T.2    Liao, L.3    Zhou, L.4    Lindner, D.J.5    Zhou, M.6
  • 17
    • 80051625243 scopus 로고    scopus 로고
    • Oxygen sensing, homeostasis, and disease
    • Semenza G.L. Oxygen sensing, homeostasis, and disease. New England Journal of Medicine 2011, 365:537-547.
    • (2011) New England Journal of Medicine , vol.365 , pp. 537-547
    • Semenza, G.L.1
  • 18
    • 0036718539 scopus 로고    scopus 로고
    • Molecular basis of the VHL hereditary cancer syndrome
    • Kaelin W.G. Molecular basis of the VHL hereditary cancer syndrome. Nature Reviews Cancer 2002, 2:673-682.
    • (2002) Nature Reviews Cancer , vol.2 , pp. 673-682
    • Kaelin, W.G.1
  • 19
    • 34547174217 scopus 로고    scopus 로고
    • Hypoxia-inducible factor linked to differential kidney cancer risk seen with type 2A and type 2B VHL mutations
    • Li L., Zhang L., Zhang X., Yan Q., Minamishima Y.A., Olumi A.F., et al. Hypoxia-inducible factor linked to differential kidney cancer risk seen with type 2A and type 2B VHL mutations. Molecular and Cellular Biology 2007, 27:5381-5392.
    • (2007) Molecular and Cellular Biology , vol.27 , pp. 5381-5392
    • Li, L.1    Zhang, L.2    Zhang, X.3    Yan, Q.4    Minamishima, Y.A.5    Olumi, A.F.6
  • 20
    • 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 S., Cockman M., Smallwood A., Mole D., Woodward E., Maxwell P., et al. Contrasting effects on HIF-1alpha regulation by disease-causing pVHL mutations correlate with patterns of tumourigenesis in von Hippel-Lindau disease. Human Molecular Genetics 2001, 10:1029-1038.
    • (2001) Human Molecular Genetics , vol.10 , pp. 1029-1038
    • Clifford, S.1    Cockman, M.2    Smallwood, A.3    Mole, D.4    Woodward, E.5    Maxwell, P.6
  • 21
    • 0035336706 scopus 로고    scopus 로고
    • Von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF
    • Hoffman M.A., Ohh M., Yang H., Klco J.M., Ivan M., Kaelin W.G. von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF. Human Molecular Genetics 2001, 10:1019-1027.
    • (2001) Human Molecular Genetics , vol.10 , pp. 1019-1027
    • Hoffman, M.A.1    Ohh, M.2    Yang, H.3    Klco, J.M.4    Ivan, M.5    Kaelin, W.G.6
  • 22
    • 43649093915 scopus 로고    scopus 로고
    • Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway
    • Kaelin W.G., Ratcliffe P.J. Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. Molecular Cell 2008, 30:393-402.
    • (2008) Molecular Cell , vol.30 , pp. 393-402
    • Kaelin, W.G.1    Ratcliffe, P.J.2
  • 23
    • 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 W.J., Tanaka H., Poellinger L. Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus. Journal of Biological Chemistry 2002, 277:32405-32408.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 32405-32408
    • Makino, Y.1    Kanopka, A.2    Wilson, W.J.3    Tanaka, H.4    Poellinger, L.5
  • 24
    • 0035969508 scopus 로고    scopus 로고
    • Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression
    • Makino Y., Cao R., Svensson K., Bertilsson G., Asman M., Tanaka H., et al. Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression. Nature 2001, 414:550-554.
    • (2001) Nature , vol.414 , pp. 550-554
    • Makino, Y.1    Cao, R.2    Svensson, K.3    Bertilsson, G.4    Asman, M.5    Tanaka, H.6
  • 25
    • 24644484730 scopus 로고    scopus 로고
    • Human HIF-3alpha4 is a dominant-negative regulator of HIF-1 and is down-regulated in renal cell carcinoma
    • Maynard M.A., Evans A.J., Hosomi T., Hara S., Jewett M.A., Ohh M. Human HIF-3alpha4 is a dominant-negative regulator of HIF-1 and is down-regulated in renal cell carcinoma. FASEB Journal 2005, 19:1396-1406.
    • (2005) FASEB Journal , vol.19 , pp. 1396-1406
    • Maynard, M.A.1    Evans, A.J.2    Hosomi, T.3    Hara, S.4    Jewett, M.A.5    Ohh, M.6
  • 26
    • 0037837724 scopus 로고    scopus 로고
    • Multiple splice variants of the human HIF-3 alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex
    • Maynard M.A., Qi H., Chung J., Lee E.H., Kondo Y., Hara S., et al. Multiple splice variants of the human HIF-3 alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex. Journal of Biological Chemistry 2003, 278:11032-11040.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 11032-11040
    • Maynard, M.A.1    Qi, H.2    Chung, J.3    Lee, E.H.4    Kondo, Y.5    Hara, S.6
  • 30
    • 17944375360 scopus 로고    scopus 로고
    • C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
    • Epstein A., Gleadle J., McNeill L., Hewitson K., O'Rourke J., Mole D., et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 2001, 107:43-54.
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.1    Gleadle, J.2    McNeill, L.3    Hewitson, K.4    O'Rourke, J.5    Mole, D.6
  • 31
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick R., McKnight S. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 2001, 294:1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.1    McKnight, S.2
  • 33
    • 33749344471 scopus 로고    scopus 로고
    • Failure to prolyl hydroxylate hypoxia-inducible factor alpha phenocopies VHL inactivation in vivo
    • Kim W.Y., Safran M., Buckley M.R., Ebert B.L., Glickman J., Bosenberg M., et al. Failure to prolyl hydroxylate hypoxia-inducible factor alpha phenocopies VHL inactivation in vivo. EMBO Journal 2006, 25:4650-4662.
    • (2006) EMBO Journal , vol.25 , pp. 4650-4662
    • Kim, W.Y.1    Safran, M.2    Buckley, M.R.3    Ebert, B.L.4    Glickman, J.5    Bosenberg, M.6
  • 34
    • 33846254999 scopus 로고    scopus 로고
    • RACK1 competes with HSP90 for binding to HIF-1α and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha
    • Liu Y.V., Baek J.H., Zhang H., Diez R., Cole R.N., Semenza G.L. RACK1 competes with HSP90 for binding to HIF-1α and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha. Molecular Cell 2007, 25:207-217.
    • (2007) Molecular Cell , vol.25 , pp. 207-217
    • Liu, Y.V.1    Baek, J.H.2    Zhang, H.3    Diez, R.4    Cole, R.N.5    Semenza, G.L.6
  • 35
    • 57349136768 scopus 로고    scopus 로고
    • Hypoxia-associated factor, a novel E3-ubiquitin ligase, binds and ubiquitinates hypoxia-inducible factor 1alpha, leading to its oxygen-independent degradation
    • Koh M.Y., Darnay B.G., Powis G. Hypoxia-associated factor, a novel E3-ubiquitin ligase, binds and ubiquitinates hypoxia-inducible factor 1alpha, leading to its oxygen-independent degradation. Molecular and Cellular Biology 2008, 28:7081-7095.
    • (2008) Molecular and Cellular Biology , vol.28 , pp. 7081-7095
    • Koh, M.Y.1    Darnay, B.G.2    Powis, G.3
  • 36
    • 78649753203 scopus 로고    scopus 로고
    • The chaperone-dependent ubiquitin ligase CHIP targets HIF-1alpha for degradation in the presence of methylglyoxal
    • Bento C.F., Fernandes R., Ramalho J., Marques C., Shang F., Taylor A., et al. The chaperone-dependent ubiquitin ligase CHIP targets HIF-1alpha for degradation in the presence of methylglyoxal. PLoS One 2010, 5:e15062.
    • (2010) PLoS One , vol.5
    • Bento, C.F.1    Fernandes, R.2    Ramalho, J.3    Marques, C.4    Shang, F.5    Taylor, A.6
  • 37
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is a an asparaginyl hydroxylase that regulates the transcriptional activity of hypoxia inducible factor
    • Lando D., Peet D., Gorman J., Whelan D., Whitelaw M., Bruick R. FIH-1 is a an asparaginyl hydroxylase that regulates the transcriptional activity of hypoxia inducible factor. Genes and Development 2002, 16:1466-1471.
    • (2002) Genes and Development , vol.16 , pp. 1466-1471
    • Lando, D.1    Peet, D.2    Gorman, J.3    Whelan, D.4    Whitelaw, M.5    Bruick, R.6
  • 38
    • 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 K.S., McNeill L.A., Riordan M.V., Tian Y.M., Bullock A.N., Welford R.W., et al. Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family. Journal of Biological Chemistry 2002, 277:26351-26355.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 26351-26355
    • Hewitson, K.S.1    McNeill, L.A.2    Riordan, M.V.3    Tian, Y.M.4    Bullock, A.N.5    Welford, R.W.6
  • 39
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: a novel protein that interacts with HIF-1 a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity
    • Mahon P., Hirota K., Semenza G. FIH-1: a novel protein that interacts with HIF-1 a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity. Genes and Development 2001, 15:2675-2686.
    • (2001) Genes and Development , vol.15 , pp. 2675-2686
    • Mahon, P.1    Hirota, K.2    Semenza, G.3
  • 40
    • 1642315195 scopus 로고    scopus 로고
    • Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases
    • Koivunen P., Hirsila M., Gunzler V., Kivirikko K.I., Myllyharju J. Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases. Journal of Biological Chemistry 2004, 279:9899-9904.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 9899-9904
    • Koivunen, P.1    Hirsila, M.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 41
    • 5644240828 scopus 로고    scopus 로고
    • Genetic analysis of the role of the asparaginyl hydroxylase FIH in regulating HIF transcriptional target genes
    • Stolze I.P., Tian Y.M., Appelhoff R.J., Turley H., Wykoff C.C., Gleadle J.M., et al. Genetic analysis of the role of the asparaginyl hydroxylase FIH in regulating HIF transcriptional target genes. Journal of Biological Chemistry 2004, 279:42719-42725.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 42719-42725
    • Stolze, I.P.1    Tian, Y.M.2    Appelhoff, R.J.3    Turley, H.4    Wykoff, C.C.5    Gleadle, J.M.6
  • 42
    • 33645735151 scopus 로고    scopus 로고
    • The oxygen sensor factor-inhibiting hypoxia-inducible factor-1 controls expression of distinct genes through the bifunctional transcriptional character of hypoxia-inducible factor-1alpha
    • Dayan F., Roux D., Brahimi-Horn M.C., Pouyssegur J., Mazure N.M. The oxygen sensor factor-inhibiting hypoxia-inducible factor-1 controls expression of distinct genes through the bifunctional transcriptional character of hypoxia-inducible factor-1alpha. Cancer Research 2006, 66:3688-3698.
    • (2006) Cancer Research , vol.66 , pp. 3688-3698
    • Dayan, F.1    Roux, D.2    Brahimi-Horn, M.C.3    Pouyssegur, J.4    Mazure, N.M.5
  • 43
    • 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 A.O., Linke S., Balrak W., Lisy K., Whitelaw M.L., et al. Cell-specific regulation of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha stabilization and transactivation in a graded oxygen environment. Journal of Biological Chemistry 2006, 281:22575-22585.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 22575-22585
    • Bracken, C.P.1    Fedele, A.O.2    Linke, S.3    Balrak, W.4    Lisy, K.5    Whitelaw, M.L.6
  • 44
    • 33947250323 scopus 로고    scopus 로고
    • The hypoxia-inducible factor 2{alpha} N-terminal and C-terminal transactivation domains cooperate to promote renal tumorigenesis in vivo
    • Yan Q., Bartz S., Mao M., Li L., Kaelin W.G. The hypoxia-inducible factor 2{alpha} N-terminal and C-terminal transactivation domains cooperate to promote renal tumorigenesis in vivo. Molecular and Cellular Biology 2007, 27:2092-2102.
    • (2007) Molecular and Cellular Biology , vol.27 , pp. 2092-2102
    • Yan, Q.1    Bartz, S.2    Mao, M.3    Li, L.4    Kaelin, W.G.5
  • 45
    • 33745685879 scopus 로고    scopus 로고
    • Role of hypoxia-inducible 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 V.A., Ashcroft M. Role of hypoxia-inducible 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 Research 2006, 66:6264-6270.
    • (2006) Cancer Research , vol.66 , pp. 6264-6270
    • Carroll, V.A.1    Ashcroft, M.2
  • 46
    • 35848938945 scopus 로고    scopus 로고
    • The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1alpha and HIF-2alpha
    • Hu C.J., Sataur A., Wang L., Chen H., Simon M.C. The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1alpha and HIF-2alpha. Molecular Biology of the Cell 2007, 18:4528-4542.
    • (2007) Molecular Biology of the Cell , vol.18 , pp. 4528-4542
    • Hu, C.J.1    Sataur, A.2    Wang, L.3    Chen, H.4    Simon, M.C.5
  • 47
    • 33644747418 scopus 로고    scopus 로고
    • HIF-2alpha regulates Oct-4: effects of hypoxia on stem cell function, embryonic development, and tumor growth
    • Covello K.L., Kehler J., Yu H., Gordan J.D., Arsham A.M., Hu C.J., et al. HIF-2alpha regulates Oct-4: effects of hypoxia on stem cell function, embryonic development, and tumor growth. Genes and Development 2006, 20:557-570.
    • (2006) Genes and Development , vol.20 , pp. 557-570
    • Covello, K.L.1    Kehler, J.2    Yu, H.3    Gordan, J.D.4    Arsham, A.M.5    Hu, C.J.6
  • 48
    • 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 R.R., Lau K.W., Tran M.G., Sowter H.M., Mandriota S.J., Li J.L., et al. Contrasting properties of hypoxia-inducible factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-associated renal cell carcinoma. Molecular and Cellular Biology 2005, 25:5675-5686.
    • (2005) Molecular and Cellular Biology , vol.25 , pp. 5675-5686
    • Raval, R.R.1    Lau, K.W.2    Tran, M.G.3    Sowter, H.M.4    Mandriota, S.J.5    Li, J.L.6
  • 49
    • 0037617447 scopus 로고    scopus 로고
    • Loss of von Hippel-Lindau protein causes cell density dependent deregulation of CyclinD1 expression through hypoxia-inducible factor
    • Baba M., Hirai S., Yamada-Okabe H., Hamada K., Tabuchi H., Kobayashi K., et al. Loss of von Hippel-Lindau protein causes cell density dependent deregulation of CyclinD1 expression through hypoxia-inducible factor. Oncogene 2003, 22:2728-2738.
    • (2003) Oncogene , vol.22 , pp. 2728-2738
    • Baba, M.1    Hirai, S.2    Yamada-Okabe, H.3    Hamada, K.4    Tabuchi, H.5    Kobayashi, K.6
  • 50
    • 0036645091 scopus 로고    scopus 로고
    • Identification of cyclin D1 and other novel targets for the von Hippel-Lindau tumor suppressor gene by expression array analysis and investigation of cyclin D1 genotype as a modifier in von Hippel-Lindau disease
    • Zatyka M., da Silva N.F., Clifford S.C., Morris M.R., Wiesener M.S., Eckardt K.U., et al. Identification of cyclin D1 and other novel targets for the von Hippel-Lindau tumor suppressor gene by expression array analysis and investigation of cyclin D1 genotype as a modifier in von Hippel-Lindau disease. Cancer Research 2002, 62:3803-3811.
    • (2002) Cancer Research , vol.62 , pp. 3803-3811
    • Zatyka, M.1    da Silva, N.F.2    Clifford, S.C.3    Morris, M.R.4    Wiesener, M.S.5    Eckardt, K.U.6
  • 52
    • 80054771537 scopus 로고    scopus 로고
    • Genetic and functional studies implicate HIF1α as a 14q kidney cancer suppressor gene
    • Shen C., Beroukhim R., Schumacher S.E., Zhou J., Chang M., Signoretti S., et al. Genetic and functional studies implicate HIF1α as a 14q kidney cancer suppressor gene. Cancer Discovery 2011, 1:222-235.
    • (2011) Cancer Discovery , vol.1 , pp. 222-235
    • Shen, C.1    Beroukhim, R.2    Schumacher, S.E.3    Zhou, J.4    Chang, M.5    Signoretti, S.6
  • 53
    • 56849096837 scopus 로고    scopus 로고
    • HIF-alpha effects on c-Myc distinguish two subtypes of sporadic VHL-deficient clear cell renal carcinoma
    • Gordan J.D., Lal P., Dondeti V.R., Letrero R., Parekh K.N., Oquendo C.E., et al. HIF-alpha effects on c-Myc distinguish two subtypes of sporadic VHL-deficient clear cell renal carcinoma. Cancer Cells 2008, 14:435-446.
    • (2008) Cancer Cells , vol.14 , pp. 435-446
    • Gordan, J.D.1    Lal, P.2    Dondeti, V.R.3    Letrero, R.4    Parekh, K.N.5    Oquendo, C.E.6
  • 54
    • 0033587146 scopus 로고    scopus 로고
    • The von Hippel-Lindau gene product is necessary for oxgyen-dependent proteolysis of hypoxia-inducible factor α subunits
    • Maxwell P., Weisner M., Chang G-W., Clifford S., Vaux E., Pugh C., et al. The von Hippel-Lindau gene product is necessary for oxgyen-dependent proteolysis of hypoxia-inducible factor α subunits. Nature 1999, 399:271-275.
    • (1999) Nature , vol.399 , pp. 271-275
    • Maxwell, P.1    Weisner, M.2    Chang, G.-W.3    Clifford, S.4    Vaux, E.5    Pugh, C.6
  • 55
    • 2342597973 scopus 로고    scopus 로고
    • Inhibition of HIF2alpha is sufficient to suppress pVHL-defective tumor growth
    • Kondo K., Kim W.Y., Lechpammer M., Kaelin W.G. Inhibition of HIF2alpha is sufficient to suppress pVHL-defective tumor growth. PLoS Biology 2003, 1:439-444.
    • (2003) PLoS Biology , vol.1 , pp. 439-444
    • Kondo, K.1    Kim, W.Y.2    Lechpammer, M.3    Kaelin, W.G.4
  • 56
    • 1342280515 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor is sufficient for growth suppression of VHL-/- tumors
    • Zimmer M., Doucette D., Siddiqui N., Iliopoulos O. Inhibition of hypoxia-inducible factor is sufficient for growth suppression of VHL-/- tumors. Molecular Cancer Research 2004, 2:89-95.
    • (2004) Molecular Cancer Research , vol.2 , pp. 89-95
    • Zimmer, M.1    Doucette, D.2    Siddiqui, N.3    Iliopoulos, O.4
  • 57
    • 0036528246 scopus 로고    scopus 로고
    • Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein
    • Kondo K., Klco J., Nakamura E., Lechpammer M., Kaelin W.G. Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein. Cancer Cells 2002, 1:237-246.
    • (2002) Cancer Cells , vol.1 , pp. 237-246
    • Kondo, K.1    Klco, J.2    Nakamura, E.3    Lechpammer, M.4    Kaelin, W.G.5
  • 58
    • 0036527785 scopus 로고    scopus 로고
    • The contribution of VHL substrate binding and HIF1-alpha to the phenotype of VHL loss in renal cell carcinoma
    • Maranchie J.K., Vasselli J.R., Riss J., Bonifacino J.S., Linehan W.M., Klausner R.D. The contribution of VHL substrate binding and HIF1-alpha to the phenotype of VHL loss in renal cell carcinoma. Cancer Cells 2002, 1:247-255.
    • (2002) Cancer Cells , vol.1 , pp. 247-255
    • Maranchie, J.K.1    Vasselli, J.R.2    Riss, J.3    Bonifacino, J.S.4    Linehan, W.M.5    Klausner, R.D.6
  • 59
    • 16244381736 scopus 로고    scopus 로고
    • Inactivation of the arylhydrocarbon receptor nuclear translocator (Arnt) suppresses von Hippel-Lindau disease-associated vascular tumors in mice
    • Rankin E.B., Higgins D.F., Walisser J.A., Johnson R.S., Bradfield C.A., Haase V.H. Inactivation of the arylhydrocarbon receptor nuclear translocator (Arnt) suppresses von Hippel-Lindau disease-associated vascular tumors in mice. Molecular and Cellular Biology 2005, 25:3163-3172.
    • (2005) Molecular and Cellular Biology , vol.25 , pp. 3163-3172
    • Rankin, E.B.1    Higgins, D.F.2    Walisser, J.A.3    Johnson, R.S.4    Bradfield, C.A.5    Haase, V.H.6
  • 61
    • 51649090078 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-2 regulates vascular tumorigenesis in mice
    • Rankin E.B., Rha J., Unger T.L., Wu C.H., Shutt H.P., Johnson R.S., et al. Hypoxia-inducible factor-2 regulates vascular tumorigenesis in mice. Oncogene 2008, 27:5354-5358.
    • (2008) Oncogene , vol.27 , pp. 5354-5358
    • Rankin, E.B.1    Rha, J.2    Unger, T.L.3    Wu, C.H.4    Shutt, H.P.5    Johnson, R.S.6
  • 63
    • 78651257523 scopus 로고    scopus 로고
    • Genome-wide association study of renal cell carcinoma identifies two susceptibility loci on 2p21 and 11q13.3
    • Purdue M.P., Johansson M., Zelenika D., Toro J.R., Scelo G., Moore L.E., et al. Genome-wide association study of renal cell carcinoma identifies two susceptibility loci on 2p21 and 11q13.3. Nature Genetics 2011, 43:60-65.
    • (2011) Nature Genetics , vol.43 , pp. 60-65
    • Purdue, M.P.1    Johansson, M.2    Zelenika, D.3    Toro, J.R.4    Scelo, G.5    Moore, L.E.6
  • 65
    • 80455174760 scopus 로고    scopus 로고
    • Chromosome 14q loss defines a molecular subtype of clear-cell renal cell carcinoma associated with poor prognosis
    • Monzon F.A., Alvarez K., Peterson L., Truong L., Amato R.J., Hernandez-McClain J., et al. Chromosome 14q loss defines a molecular subtype of clear-cell renal cell carcinoma associated with poor prognosis. Modern Pathology 2011, 24:1470-1479.
    • (2011) Modern Pathology , vol.24 , pp. 1470-1479
    • Monzon, F.A.1    Alvarez, K.2    Peterson, L.3    Truong, L.4    Amato, R.J.5    Hernandez-McClain, J.6
  • 66
    • 75149174239 scopus 로고    scopus 로고
    • Mutation analysis of hypoxia-inducible factors HIF1A and HIF2A in renal cell carcinoma
    • Morris M.R., Hughes D.J., Tian Y.M., Ricketts C.J., Lau K.W., Gentle D., et al. Mutation analysis of hypoxia-inducible factors HIF1A and HIF2A in renal cell carcinoma. Anticancer Research 2009, 29:4337-4343.
    • (2009) Anticancer Research , vol.29 , pp. 4337-4343
    • Morris, M.R.1    Hughes, D.J.2    Tian, Y.M.3    Ricketts, C.J.4    Lau, K.W.5    Gentle, D.6
  • 67
    • 0032581277 scopus 로고    scopus 로고
    • Role of HIF-1alpha in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis
    • Carmeliet P., Dor Y., Herbert J.M., Fukumura D., Brusselmans K., Dewerchin M., et al. Role of HIF-1alpha in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis. Nature 1998, 394:485-490.
    • (1998) Nature , vol.394 , pp. 485-490
    • Carmeliet, P.1    Dor, Y.2    Herbert, J.M.3    Fukumura, D.4    Brusselmans, K.5    Dewerchin, M.6
  • 68
    • 0041382820 scopus 로고    scopus 로고
    • The hypoxic response of tumors is dependent on their microenvironment
    • Blouw B., Song H., Tihan T., Bosze J., Ferrara N., Gerber H.P., et al. The hypoxic response of tumors is dependent on their microenvironment. Cancer Cells 2003, 4:133-146.
    • (2003) Cancer Cells , vol.4 , pp. 133-146
    • Blouw, B.1    Song, H.2    Tihan, T.3    Bosze, J.4    Ferrara, N.5    Gerber, H.P.6
  • 69
    • 69349102011 scopus 로고    scopus 로고
    • Hypoxia-HIF-1alpha-C/EBPalpha/Runx1 signaling in leukemic cell differentiation
    • Zhang J., Chen G.Q. Hypoxia-HIF-1alpha-C/EBPalpha/Runx1 signaling in leukemic cell differentiation. Pathophysiology 2009, 16:297-303.
    • (2009) Pathophysiology , vol.16 , pp. 297-303
    • Zhang, J.1    Chen, G.Q.2
  • 70
    • 54349102038 scopus 로고    scopus 로고
    • Accumulation of hypoxia-inducible factor-1 alpha protein and its role in the differentiation of myeloid leukemic cells induced by all-trans retinoic acid
    • Zhang J., Song L.P., Huang Y., Zhao Q., Zhao K.W., Chen G.Q. Accumulation of hypoxia-inducible factor-1 alpha protein and its role in the differentiation of myeloid leukemic cells induced by all-trans retinoic acid. Haematologica 2008, 93:1480-1487.
    • (2008) Haematologica , vol.93 , pp. 1480-1487
    • Zhang, J.1    Song, L.P.2    Huang, Y.3    Zhao, Q.4    Zhao, K.W.5    Chen, G.Q.6
  • 71
    • 38349000624 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha-induced differentiation of myeloid leukemic cells is its transcriptional activity independent
    • Song L.P., Zhang J., Wu S.F., Huang Y., Zhao Q., Cao J.P., et al. Hypoxia-inducible factor-1alpha-induced differentiation of myeloid leukemic cells is its transcriptional activity independent. Oncogene 2008, 27:519-527.
    • (2008) Oncogene , vol.27 , pp. 519-527
    • Song, L.P.1    Zhang, J.2    Wu, S.F.3    Huang, Y.4    Zhao, Q.5    Cao, J.P.6
  • 72
    • 33845447175 scopus 로고    scopus 로고
    • LOT1 (ZAC1/PLAGL1) and its family members: mechanisms and functions
    • Abdollahi A. LOT1 (ZAC1/PLAGL1) and its family members: mechanisms and functions. Journal of Cellular Physiology 2007, 210:16-25.
    • (2007) Journal of Cellular Physiology , vol.210 , pp. 16-25
    • Abdollahi, A.1
  • 74
    • 84655161946 scopus 로고    scopus 로고
    • HIF1α and HIF2α: sibling rivalry in hypoxic umor growth and progression
    • Keith B., Johnson R.S., Simon M.C. HIF1α and HIF2α: sibling rivalry in hypoxic umor growth and progression. Nature Reviews Cancer 2011, 12:9-22.
    • (2011) Nature Reviews Cancer , vol.12 , pp. 9-22
    • Keith, B.1    Johnson, R.S.2    Simon, M.C.3
  • 76
    • 71549151624 scopus 로고    scopus 로고
    • Suppression of hypoxia-inducible factor 2alpha restores p53 activity via Hdm2 and reverses chemoresistance of renal carcinoma cells
    • Roberts A.M., Watson I.R., Evans A.J., Foster D.A., Irwin M.S., Ohh M. Suppression of hypoxia-inducible factor 2alpha restores p53 activity via Hdm2 and reverses chemoresistance of renal carcinoma cells. Cancer Research 2009, 69:9056-9064.
    • (2009) Cancer Research , vol.69 , pp. 9056-9064
    • Roberts, A.M.1    Watson, I.R.2    Evans, A.J.3    Foster, D.A.4    Irwin, M.S.5    Ohh, M.6
  • 77
    • 34548581017 scopus 로고    scopus 로고
    • Modulating hypoxia-inducible transcription by disrupting the HIF-1-DNA interface
    • Nickols N.G., Jacobs C.S., Farkas M.E., Dervan P.B. Modulating hypoxia-inducible transcription by disrupting the HIF-1-DNA interface. ACS Chemical Biology 2007, 2:561-571.
    • (2007) ACS Chemical Biology , vol.2 , pp. 561-571
    • Nickols, N.G.1    Jacobs, C.S.2    Farkas, M.E.3    Dervan, P.B.4
  • 78
    • 33750503786 scopus 로고    scopus 로고
    • Exploring the limits of benzimidazole DNA-binding oligomers for the hypoxia inducible factor (HIF) site
    • Viger A., Dervan P.B. Exploring the limits of benzimidazole DNA-binding oligomers for the hypoxia inducible factor (HIF) site. Bioorganic and Medicinal Chemistry 2006, 14:8539-8549.
    • (2006) Bioorganic and Medicinal Chemistry , vol.14 , pp. 8539-8549
    • Viger, A.1    Dervan, P.B.2
  • 79
    • 33645821109 scopus 로고    scopus 로고
    • A rationally designed small molecule that inhibits the HIF-1alpha-ARNT heterodimer from binding to DNA in vivo
    • Vinson C. A rationally designed small molecule that inhibits the HIF-1alpha-ARNT heterodimer from binding to DNA in vivo. Science's STKE 2005, 2005:pe23.
    • (2005) Science's STKE , vol.2005
    • Vinson, C.1
  • 82
    • 57849147670 scopus 로고    scopus 로고
    • Small-molecule inhibitors of HIF-2a translation link its 5'UTR iron-responsive element to oxygen sensing
    • Zimmer M., Ebert B.L., Neil C., Brenner K., Papaioannou I., Melas A., et al. Small-molecule inhibitors of HIF-2a translation link its 5'UTR iron-responsive element to oxygen sensing. Molecular Cell 2008, 32:838-848.
    • (2008) Molecular Cell , vol.32 , pp. 838-848
    • Zimmer, M.1    Ebert, B.L.2    Neil, C.3    Brenner, K.4    Papaioannou, I.5    Melas, A.6
  • 86
    • 77951082053 scopus 로고    scopus 로고
    • The connectivity map links iron regulatory protein-1-mediated inhibition of hypoxia-inducible factor-2a translation to the anti-inflammatory 15-deoxy-delta12,14-prostaglandin J2
    • Zimmer M., Lamb J., Ebert B.L., Lynch M., Neil C., Schmidt E., et al. The connectivity map links iron regulatory protein-1-mediated inhibition of hypoxia-inducible factor-2a translation to the anti-inflammatory 15-deoxy-delta12,14-prostaglandin J2. Cancer Research 2010, 70:3071-3079.
    • (2010) Cancer Research , vol.70 , pp. 3071-3079
    • Zimmer, M.1    Lamb, J.2    Ebert, B.L.3    Lynch, M.4    Neil, C.5    Schmidt, E.6
  • 87
    • 33749451610 scopus 로고    scopus 로고
    • Molecular pathways in renal cell carcinoma-rationale for targeted treatment
    • Kim W.Y., Kaelin W.G. Molecular pathways in renal cell carcinoma-rationale for targeted treatment. Seminars in Oncology 2006, 33:588-595.
    • (2006) Seminars in Oncology , vol.33 , pp. 588-595
    • Kim, W.Y.1    Kaelin, W.G.2
  • 88
    • 48649107474 scopus 로고    scopus 로고
    • Efficacy of everolimus in advanced renal cell carcinoma: a double-blind, randomised, placebo-controlled phase III trial
    • Motzer R.J., Escudier B., Oudard S., Hutson T.E., Porta C., Bracarda S., et al. Efficacy of everolimus in advanced renal cell carcinoma: a double-blind, randomised, placebo-controlled phase III trial. Lancet 2008, 372:449-456.
    • (2008) Lancet , vol.372 , pp. 449-456
    • Motzer, R.J.1    Escudier, B.2    Oudard, S.3    Hutson, T.E.4    Porta, C.5    Bracarda, S.6
  • 90
    • 39449120471 scopus 로고    scopus 로고
    • A retroinhibition approach reveals a tumor cell-autonomous response to rapamycin in head and neck cancer
    • Amornphimoltham P., Patel V., Leelahavanichkul K., Abraham R.T., Gutkind J.S. A retroinhibition approach reveals a tumor cell-autonomous response to rapamycin in head and neck cancer. Cancer Research 2008, 68:1144-1153.
    • (2008) Cancer Research , vol.68 , pp. 1144-1153
    • Amornphimoltham, P.1    Patel, V.2    Leelahavanichkul, K.3    Abraham, R.T.4    Gutkind, J.S.5
  • 91
    • 34347220473 scopus 로고    scopus 로고
    • Defining the role of mTOR in cancer
    • Guertin D.A., Sabatini D.M. Defining the role of mTOR in cancer. Cancer Cells 2007, 12:9-22.
    • (2007) Cancer Cells , vol.12 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 93
    • 32944457518 scopus 로고    scopus 로고
    • MTOR inhibition induces upstream receptor tyrosine kinase signaling and activates Akt
    • O'Reilly K.E., Rojo F., She Q.B., Solit D., Mills G.B., Smith D., et al. mTOR inhibition induces upstream receptor tyrosine kinase signaling and activates Akt. Cancer Research 2006, 66:1500-1508.
    • (2006) Cancer Research , vol.66 , pp. 1500-1508
    • O'Reilly, K.E.1    Rojo, F.2    She, Q.B.3    Solit, D.4    Mills, G.B.5    Smith, D.6
  • 94
    • 0035851205 scopus 로고    scopus 로고
    • Amino acid and insulin signaling via the mTOR/p70 S6 kinase pathway A negative feedback mechanism leading to insulin resistance in skeletal muscle cells
    • Tremblay F., Marette A. Amino acid and insulin signaling via the mTOR/p70 S6 kinase pathway A negative feedback mechanism leading to insulin resistance in skeletal muscle cells. Journal of Biological Chemistry 2001, 276:38052-38060.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 38052-38060
    • Tremblay, F.1    Marette, A.2
  • 95
    • 77954746352 scopus 로고    scopus 로고
    • The efficacy of the novel dual PI3-kinase/mTOR inhibitor NVP-BEZ235 compared with rapamycin in renal cell carcinoma
    • Cho D.C., Cohen M.B., Panka D.J., Collins M., Ghebremichael M., Atkins M.B., et al. The efficacy of the novel dual PI3-kinase/mTOR inhibitor NVP-BEZ235 compared with rapamycin in renal cell carcinoma. Clinical Cancer Research 2010, 16:3628-3638.
    • (2010) Clinical Cancer Research , vol.16 , pp. 3628-3638
    • Cho, D.C.1    Cohen, M.B.2    Panka, D.J.3    Collins, M.4    Ghebremichael, M.5    Atkins, M.B.6
  • 96
    • 37349080670 scopus 로고    scopus 로고
    • Bevacizumab plus interferon alfa-2a for treatment of metastatic renal cell carcinoma: a randomised, double-blind phase III trial
    • Escudier B., Pluzanska A., Koralewski P., Ravaud A., Bracarda S., Szczylik C., et al. Bevacizumab plus interferon alfa-2a for treatment of metastatic renal cell carcinoma: a randomised, double-blind phase III trial. Lancet 2007, 370:2103-2111.
    • (2007) Lancet , vol.370 , pp. 2103-2111
    • Escudier, B.1    Pluzanska, A.2    Koralewski, P.3    Ravaud, A.4    Bracarda, S.5    Szczylik, C.6
  • 99
    • 77949890945 scopus 로고    scopus 로고
    • Pazopanib in locally advanced or metastatic renal cell carcinoma: results of a randomized phase III trial
    • Sternberg C.N., Davis I.D., Mardiak J., Szczylik C., Lee E., Wagstaff J., et al. Pazopanib in locally advanced or metastatic renal cell carcinoma: results of a randomized phase III trial. Journal of Clinical Oncology 2010, 28:1061-1068.
    • (2010) Journal of Clinical Oncology , vol.28 , pp. 1061-1068
    • Sternberg, C.N.1    Davis, I.D.2    Mardiak, J.3    Szczylik, C.4    Lee, E.5    Wagstaff, J.6
  • 101
    • 65949118243 scopus 로고    scopus 로고
    • Combination targeted therapy in advanced renal cell carcinoma
    • Sosman J., Puzanov I. Combination targeted therapy in advanced renal cell carcinoma. Cancer 2009, 115:2368-2375.
    • (2009) Cancer , vol.115 , pp. 2368-2375
    • Sosman, J.1    Puzanov, I.2
  • 102
    • 63049093371 scopus 로고    scopus 로고
    • Phase I trial of bevacizumab plus escalated doses of sunitinib in patients with metastatic renal cell carcinoma
    • Feldman D.R., Baum M.S., Ginsberg M.S., Hassoun H., Flombaum C.D., Velasco S., et al. Phase I trial of bevacizumab plus escalated doses of sunitinib in patients with metastatic renal cell carcinoma. Journal of Clinical Oncology 2009, 27:1432-1439.
    • (2009) Journal of Clinical Oncology , vol.27 , pp. 1432-1439
    • Feldman, D.R.1    Baum, M.S.2    Ginsberg, M.S.3    Hassoun, H.4    Flombaum, C.D.5    Velasco, S.6
  • 104
    • 0031834239 scopus 로고    scopus 로고
    • A plasticity window for blood vessel remodelling is defined by pericyte coverage of the preformed endothelial network and is regulated by PDGF-B and VEGF
    • Benjamin L.E., Hemo I., Keshet E. A plasticity window for blood vessel remodelling is defined by pericyte coverage of the preformed endothelial network and is regulated by PDGF-B and VEGF. Development 1998, 125:1591-1598.
    • (1998) Development , vol.125 , pp. 1591-1598
    • Benjamin, L.E.1    Hemo, I.2    Keshet, E.3
  • 105
    • 0032952010 scopus 로고    scopus 로고
    • Selective ablation of immature blood vessels in established human tumors follows vascular endothelial growth factor withdrawal
    • Benjamin L.E., Golijanin D., Itin A., Pode D., Keshet E. Selective ablation of immature blood vessels in established human tumors follows vascular endothelial growth factor withdrawal. Journal of Clinical Investigation 1999, 103:159-165.
    • (1999) Journal of Clinical Investigation , vol.103 , pp. 159-165
    • Benjamin, L.E.1    Golijanin, D.2    Itin, A.3    Pode, D.4    Keshet, E.5
  • 106
    • 0038476608 scopus 로고    scopus 로고
    • Benefits of targeting both pericytes and endothelial cells in the tumor vasculature with kinase inhibitors
    • Bergers G., Song S., Meyer-Morse N., Bergsland E., Hanahan D. Benefits of targeting both pericytes and endothelial cells in the tumor vasculature with kinase inhibitors. Journal of Clinical Investigation 2003, 111:1287-1295.
    • (2003) Journal of Clinical Investigation , vol.111 , pp. 1287-1295
    • Bergers, G.1    Song, S.2    Meyer-Morse, N.3    Bergsland, E.4    Hanahan, D.5
  • 108
    • 33646883733 scopus 로고    scopus 로고
    • Combination therapy of imatinib mesylate and interferon-alpha demonstrates minimal activity and significant toxicity in metastatic renal cell carcinoma: results of a single-institution phase II trial
    • Polite B.N., Desai A.A., Manchen B., Stadler W.M. Combination therapy of imatinib mesylate and interferon-alpha demonstrates minimal activity and significant toxicity in metastatic renal cell carcinoma: results of a single-institution phase II trial. Clinical Genitourinary Cancer 2006, 4:275-280.
    • (2006) Clinical Genitourinary Cancer , vol.4 , pp. 275-280
    • Polite, B.N.1    Desai, A.A.2    Manchen, B.3    Stadler, W.M.4
  • 109
    • 0034055006 scopus 로고    scopus 로고
    • Differential response to transforming growth factor (TGF)-alpha and fibroblast growth factor (FGF) in human renal cell carcinomas of the clear cell and papillary types
    • Ramp U., Reinecke P., Gabbert H., Gerharz C. Differential response to transforming growth factor (TGF)-alpha and fibroblast growth factor (FGF) in human renal cell carcinomas of the clear cell and papillary types. European Journal of Cancer 2000, 36:932-941.
    • (2000) European Journal of Cancer , vol.36 , pp. 932-941
    • Ramp, U.1    Reinecke, P.2    Gabbert, H.3    Gerharz, C.4
  • 110
    • 0030900916 scopus 로고    scopus 로고
    • Functional intactness of stimulatory and inhibitory autocrine loops in human renal carcinoma cell lines of the clear cell type
    • Ramp U., Jaquet K., Reinecke P., Schardt C., Friebe U., Nitsch T., et al. Functional intactness of stimulatory and inhibitory autocrine loops in human renal carcinoma cell lines of the clear cell type. Journal of Urology 1997, 157:2345-2350.
    • (1997) Journal of Urology , vol.157 , pp. 2345-2350
    • Ramp, U.1    Jaquet, K.2    Reinecke, P.3    Schardt, C.4    Friebe, U.5    Nitsch, T.6
  • 111
    • 21344463784 scopus 로고    scopus 로고
    • Membranous expression and prognostic implications of epidermal growth factor receptor protein in human renal cell cancer
    • Merseburger A.S., Hennenlotter J., Simon P., Kruck S., Koch E., Horstmann M., et al. Membranous expression and prognostic implications of epidermal growth factor receptor protein in human renal cell cancer. Anticancer Research 2005, 25:1901-1907.
    • (2005) Anticancer Research , vol.25 , pp. 1901-1907
    • Merseburger, A.S.1    Hennenlotter, J.2    Simon, P.3    Kruck, S.4    Koch, E.5    Horstmann, M.6
  • 112
    • 0030786030 scopus 로고    scopus 로고
    • Epidermal growth factor receptor expression is associated with rapid tumor cell proliferation in renal cell carcinoma
    • Moch H., Sauter G., Buchholz N., Gasser T.C., Bubendorf L., Waldman F.M., et al. Epidermal growth factor receptor expression is associated with rapid tumor cell proliferation in renal cell carcinoma. Human Pathology 1997, 28:1255-1259.
    • (1997) Human Pathology , vol.28 , pp. 1255-1259
    • Moch, H.1    Sauter, G.2    Buchholz, N.3    Gasser, T.C.4    Bubendorf, L.5    Waldman, F.M.6
  • 113
    • 0029146750 scopus 로고
    • Epidermal growth factor receptor and transforming growth factor alpha expression in papillary and nonpapillary renal cell carcinoma: correlation with metastatic behavior and prognosis
    • Uhlman D.L., Nguyen P., Manivel J.C., Zhang G., Hagen K., Fraley E., et al. Epidermal growth factor receptor and transforming growth factor alpha expression in papillary and nonpapillary renal cell carcinoma: correlation with metastatic behavior and prognosis. Clinical Cancer Research 1995, 1:913-920.
    • (1995) Clinical Cancer Research , vol.1 , pp. 913-920
    • Uhlman, D.L.1    Nguyen, P.2    Manivel, J.C.3    Zhang, G.4    Hagen, K.5    Fraley, E.6
  • 114
    • 0024328825 scopus 로고
    • Expression of transforming growth factor alpha and epidermal growth factor receptor messenger RNA in neoplastic and nonneoplastic human kidney tissue
    • Mydlo J., Michaeli J., Cordon-Cardo C., Goldenberg A., Heston W., Fair W. Expression of transforming growth factor alpha and epidermal growth factor receptor messenger RNA in neoplastic and nonneoplastic human kidney tissue. Cancer Research 1989, 49:3407-3411.
    • (1989) Cancer Research , vol.49 , pp. 3407-3411
    • Mydlo, J.1    Michaeli, J.2    Cordon-Cardo, C.3    Goldenberg, A.4    Heston, W.5    Fair, W.6
  • 115
    • 0023877293 scopus 로고
    • Epidermal growth factor in the normal and neoplastic kidney and bladder
    • Lau J., Fowler J.J., Ghosh L. Epidermal growth factor in the normal and neoplastic kidney and bladder. Journal of Urology 1988, 139:170-175.
    • (1988) Journal of Urology , vol.139 , pp. 170-175
    • Lau, J.1    Fowler, J.J.2    Ghosh, L.3
  • 116
    • 0025323946 scopus 로고
    • Modulation of pro-epidermal growth factor, pro-transforming growth factor alpha and epidermal growth factor receptor gene expression in human renal carcinomas
    • Petrides P., Bock S., Bovens J., Hofmann R., Jakse G. Modulation of pro-epidermal growth factor, pro-transforming growth factor alpha and epidermal growth factor receptor gene expression in human renal carcinomas. Cancer Research 1990, 50:3934-3939.
    • (1990) Cancer Research , vol.50 , pp. 3934-3939
    • Petrides, P.1    Bock, S.2    Bovens, J.3    Hofmann, R.4    Jakse, G.5
  • 117
    • 0031964099 scopus 로고    scopus 로고
    • Transforming growth factor alpha is a target for the von Hippel-Lindau tumor suppressor
    • Knebelmann B., Ananth S., Cohen H., Sukhatme V. Transforming growth factor alpha is a target for the von Hippel-Lindau tumor suppressor. Cancer Research 1998, 58:226-231.
    • (1998) Cancer Research , vol.58 , pp. 226-231
    • Knebelmann, B.1    Ananth, S.2    Cohen, H.3    Sukhatme, V.4
  • 121
    • 20444485232 scopus 로고    scopus 로고
    • Silencing of epidermal growth factor receptor suppresses hypoxia-inducible factor-2-driven VHL-/- renal cancer
    • Smith K., Gunaratnam L., Morley M., Franovic A., Mekhail K., Lee S. Silencing of epidermal growth factor receptor suppresses hypoxia-inducible factor-2-driven VHL-/- renal cancer. Cancer Research 2005, 65:5221-5230.
    • (2005) Cancer Research , vol.65 , pp. 5221-5230
    • Smith, K.1    Gunaratnam, L.2    Morley, M.3    Franovic, A.4    Mekhail, K.5    Lee, S.6
  • 122
    • 9744240281 scopus 로고    scopus 로고
    • A phase II trial of gefitinib (Iressa, ZD1839) in stage IV and recurrent renal cell carcinoma
    • Dawson N.A., Guo C., Zak R., Dorsey B., Smoot J., Wong J., et al. A phase II trial of gefitinib (Iressa, ZD1839) in stage IV and recurrent renal cell carcinoma. Clinical Cancer Research 2004, 10:7812-7819.
    • (2004) Clinical Cancer Research , vol.10 , pp. 7812-7819
    • Dawson, N.A.1    Guo, C.2    Zak, R.3    Dorsey, B.4    Smoot, J.5    Wong, J.6
  • 124
    • 35648938219 scopus 로고    scopus 로고
    • Randomized phase II study of erlotinib combined with bevacizumab compared with bevacizumab alone in metastatic renal cell cancer
    • Bukowski R.M., Kabbinavar F.F., Figlin R.A., Flaherty K., Srinivas S., Vaishampayan U., et al. Randomized phase II study of erlotinib combined with bevacizumab compared with bevacizumab alone in metastatic renal cell cancer. Journal of Clinical Oncology 2007, 25:4536-4541.
    • (2007) Journal of Clinical Oncology , vol.25 , pp. 4536-4541
    • Bukowski, R.M.1    Kabbinavar, F.F.2    Figlin, R.A.3    Flaherty, K.4    Srinivas, S.5    Vaishampayan, U.6
  • 125
    • 4143050397 scopus 로고    scopus 로고
    • Safety, pharmacokinetics, and activity of ABX-EGF, a fully human anti-epidermal growth factor receptor monoclonal antibody in patients with metastatic renal cell cancer
    • Rowinsky E.K., Schwartz G.H., Gollob J.A., Thompson J.A., Vogelzang N.J., Figlin R., et al. Safety, pharmacokinetics, and activity of ABX-EGF, a fully human anti-epidermal growth factor receptor monoclonal antibody in patients with metastatic renal cell cancer. Journal of Clinical Oncology 2004, 22:3003-3015.
    • (2004) Journal of Clinical Oncology , vol.22 , pp. 3003-3015
    • Rowinsky, E.K.1    Schwartz, G.H.2    Gollob, J.A.3    Thompson, J.A.4    Vogelzang, N.J.5    Figlin, R.6
  • 126
    • 34249075147 scopus 로고    scopus 로고
    • MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling
    • Engelman J.A., Zejnullahu K., Mitsudomi T., Song Y., Hyland C., Park J.O., et al. MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling. Science 2007, 316:1039-1043.
    • (2007) Science , vol.316 , pp. 1039-1043
    • Engelman, J.A.1    Zejnullahu, K.2    Mitsudomi, T.3    Song, Y.4    Hyland, C.5    Park, J.O.6
  • 128
    • 35348822482 scopus 로고    scopus 로고
    • Coactivation of receptor tyrosine kinases affects the response of tumor cells to targeted therapies
    • Stommel J.M., Kimmelman A.C., Ying H., Nabioullin R., Ponugoti A.H., Wiedemeyer R., et al. Coactivation of receptor tyrosine kinases affects the response of tumor cells to targeted therapies. Science 2007, 318:287-290.
    • (2007) Science , vol.318 , pp. 287-290
    • Stommel, J.M.1    Kimmelman, A.C.2    Ying, H.3    Nabioullin, R.4    Ponugoti, A.H.5    Wiedemeyer, R.6
  • 129
    • 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 P., Gong C., Taylor G., Roessler L., et al. The von Hippel-Lindau tumor suppressor gene inhibits hepatocyte growth factor/scatter factor-induced invasion and branching morphogenesis in renal carcinoma cells. Molecular and Cellular Biology 1999, 19:5902-5912.
    • (1999) Molecular and Cellular Biology , vol.19 , pp. 5902-5912
    • Koochekpour, S.1    Jeffers, M.2    Wang, P.3    Gong, C.4    Taylor, G.5    Roessler, L.6
  • 130
    • 33645731190 scopus 로고    scopus 로고
    • Inactivation of von Hippel-Lindau gene induces constitutive phosphorylation of MET protein in clear cell renal carcinoma
    • Nakaigawa N., Yao M., Baba M., Kato S., Kishida T., Hattori K., et al. Inactivation of von Hippel-Lindau gene induces constitutive phosphorylation of MET protein in clear cell renal carcinoma. Cancer Research 2006, 66:3699-3705.
    • (2006) Cancer Research , vol.66 , pp. 3699-3705
    • Nakaigawa, N.1    Yao, M.2    Baba, M.3    Kato, S.4    Kishida, T.5    Hattori, K.6
  • 133
    • 77956296140 scopus 로고    scopus 로고
    • MET kinase inhibitor SGX523 synergizes with epidermal growth factor receptor inhibitor erlotinib in a hepatocyte growth factor-dependent fashion to suppress carcinoma growth
    • Zhang Y.W., Staal B., Essenburg C., Su Y., Kang L., West R., et al. MET kinase inhibitor SGX523 synergizes with epidermal growth factor receptor inhibitor erlotinib in a hepatocyte growth factor-dependent fashion to suppress carcinoma growth. Cancer Research 2010, 70:6880-6890.
    • (2010) Cancer Research , vol.70 , pp. 6880-6890
    • Zhang, Y.W.1    Staal, B.2    Essenburg, C.3    Su, Y.4    Kang, L.5    West, R.6
  • 134
    • 0034879988 scopus 로고    scopus 로고
    • Frequently deleted loci on chromosome 9 may harbor several tumor suppressor genes in human renal cell carcinoma
    • Grady B., Goharderakhshan R., Chang J., Ribeiro-Filho L.A., Perinchery G., Franks J., et al. Frequently deleted loci on chromosome 9 may harbor several tumor suppressor genes in human renal cell carcinoma. Journal of Urology 2001, 166:1088-1092.
    • (2001) Journal of Urology , vol.166 , pp. 1088-1092
    • Grady, B.1    Goharderakhshan, R.2    Chang, J.3    Ribeiro-Filho, L.A.4    Perinchery, G.5    Franks, J.6
  • 136
    • 0034746254 scopus 로고    scopus 로고
    • CDKNA2A mutation analysis, protein expression, and deletion mapping of chromosome 9p in conventional clear-cell renal carcinomas: evidence for a second tumor suppressor gene proximal to CDKN2A
    • Schraml P., Struckmann K., Bednar R., Fu W., Gasser T., Wilber K., et al. CDKNA2A mutation analysis, protein expression, and deletion mapping of chromosome 9p in conventional clear-cell renal carcinomas: evidence for a second tumor suppressor gene proximal to CDKN2A. American Journal of Pathology 2001, 158:593-601.
    • (2001) American Journal of Pathology , vol.158 , pp. 593-601
    • Schraml, P.1    Struckmann, K.2    Bednar, R.3    Fu, W.4    Gasser, T.5    Wilber, K.6
  • 137
    • 0033955395 scopus 로고    scopus 로고
    • Flavopiridol, a novel cyclin-dependent kinase inhibitor, in metastatic renal cancer: a University of Chicago Phase II Consortium study
    • Stadler W.M., Vogelzang N.J., Amato R., Sosman J., Taber D., Liebowitz D., et al. Flavopiridol, a novel cyclin-dependent kinase inhibitor, in metastatic renal cancer: a University of Chicago Phase II Consortium study. Journal of Clinical Oncology 2000, 18:371-375.
    • (2000) Journal of Clinical Oncology , vol.18 , pp. 371-375
    • Stadler, W.M.1    Vogelzang, N.J.2    Amato, R.3    Sosman, J.4    Taber, D.5    Liebowitz, D.6
  • 138
    • 73549088729 scopus 로고    scopus 로고
    • Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth
    • Krieg A.J., Rankin E.B., Chan D., Razorenova O., Fernandez S., Giaccia A.J. Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth. Molecular and Cellular Biology 2010, 30:344-353.
    • (2010) Molecular and Cellular Biology , vol.30 , pp. 344-353
    • Krieg, A.J.1    Rankin, E.B.2    Chan, D.3    Razorenova, O.4    Fernandez, S.5    Giaccia, A.J.6
  • 140
    • 68449090024 scopus 로고    scopus 로고
    • Identification and characterization of demethylase JMJD1A as a gene upregulated in the human cellular response to hypoxia
    • Sar A., Ponjevic D., Nguyen M., Box A.H., Demetrick D.J. Identification and characterization of demethylase JMJD1A as a gene upregulated in the human cellular response to hypoxia. Cell and Tissue Research 2009, 337:223-234.
    • (2009) Cell and Tissue Research , vol.337 , pp. 223-234
    • Sar, A.1    Ponjevic, D.2    Nguyen, M.3    Box, A.H.4    Demetrick, D.J.5
  • 142
    • 58949097017 scopus 로고    scopus 로고
    • Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1alpha
    • Pollard P., Loenarz C., Mole D., McDonough M., Gleadle J., Schofield C., et al. Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1alpha. Biochemical Journal 2008, 416:387-394.
    • (2008) Biochemical Journal , vol.416 , pp. 387-394
    • Pollard, P.1    Loenarz, C.2    Mole, D.3    McDonough, M.4    Gleadle, J.5    Schofield, C.6
  • 143
    • 61349088682 scopus 로고    scopus 로고
    • The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF
    • Beyer S., Kristensen M.M., Jensen K.S., Johansen J.V., Staller P. The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF. Journal of Biological Chemistry 2008, 283:36542-36552.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 36542-36552
    • Beyer, S.1    Kristensen, M.M.2    Jensen, K.S.3    Johansen, J.V.4    Staller, P.5


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