메뉴 건너뛰기




Volumn 6, Issue 6, 2011, Pages

Reduced expression of fumarate hydratase in clear cell renal cancer mediates HIF-2α accumulation and promotes migration and invasion

Author keywords

[No Author keywords available]

Indexed keywords

FUMARATE HYDRATASE; HYPOXIA INDUCIBLE FACTOR 2ALPHA; MESSENGER RNA; PROTEIN KINASE B; BASIC HELIX LOOP HELIX TRANSCRIPTION FACTOR; ENDOTHELIAL PAS DOMAIN CONTAINING PROTEIN 1; ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1;

EID: 79958795339     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0021037     Document Type: Article
Times cited : (39)

References (42)
  • 2
    • 0027954044 scopus 로고
    • Mutations of the VHL tumour suppressor gene in renal carcinoma
    • Gnarra JR, Tory K, Weng Y, Schmidt L, Wei MH, et al. (1994) Mutations of the VHL tumour suppressor gene in renal carcinoma. Nat Genet 7: 85-90.
    • (1994) Nat Genet , vol.7 , pp. 85-90
    • Gnarra, J.R.1    Tory, K.2    Weng, Y.3    Schmidt, L.4    Wei, M.H.5
  • 4
    • 18544365990 scopus 로고    scopus 로고
    • Germline mutations in FH predispose to dominantly inherited uterine fibroids, skin leiomyomata and papillary renal cell cancer
    • Tomlinson IP, Alam NA, Rowan AJ, Barclay E, Jaeger EE, et al. (2002) Germline mutations in FH predispose to dominantly inherited uterine fibroids, skin leiomyomata and papillary renal cell cancer. Nat Genet 30: 406-410.
    • (2002) Nat Genet , vol.30 , pp. 406-410
    • Tomlinson, I.P.1    Alam, N.A.2    Rowan, A.J.3    Barclay, E.4    Jaeger, E.E.5
  • 5
    • 23644448721 scopus 로고    scopus 로고
    • HIF overexpression correlates with biallelic loss of fumarate hydratase in renal cancer: novel role of fumarate in regulation of HIF stability
    • Isaacs JS, Jung YJ, Mole DR, Lee S, Torres-Cabala C, et al. (2005) HIF overexpression correlates with biallelic loss of fumarate hydratase in renal cancer: novel role of fumarate in regulation of HIF stability. Cancer Cell 8: 143-153.
    • (2005) Cancer Cell , vol.8 , pp. 143-153
    • Isaacs, J.S.1    Jung, Y.J.2    Mole, D.R.3    Lee, S.4    Torres-Cabala, C.5
  • 6
    • 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, Hewitson KS, O'Rourke J, 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    Hewitson, K.S.4    O'Rourke, J.5
  • 7
    • 0035917313 scopus 로고    scopus 로고
    • HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing
    • Ivan M, Kondo K, Yang H, Kim W, Valiando J, et al. (2001) HIFalpha targeted for VHL-mediated destruction by proline 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    Kim, W.4    Valiando, J.5
  • 8
    • 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, Wilson MI, Gielbert J, 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    Wilson, M.I.4    Gielbert, J.5
  • 9
    • 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
  • 10
    • 33846199233 scopus 로고    scopus 로고
    • Hypoxia-inducible factors: central regulators of the tumor phenotype
    • Gordan JD, Simon MC, (2007) Hypoxia-inducible factors: central regulators of the tumor phenotype. Curr Opin Genet Dev 17: 71-77.
    • (2007) Curr Opin Genet Dev , vol.17 , pp. 71-77
    • Gordan, J.D.1    Simon, M.C.2
  • 12
    • 0035394516 scopus 로고    scopus 로고
    • Constitutive activation of hypoxia-inducible genes related to overexpression of hypoxia-inducible factor-1alpha in clear cell renal carcinomas
    • Wiesener MS, Munchenhagen PM, Berger I, Morgan NV, Roigas J, et al. (2001) Constitutive activation of hypoxia-inducible genes related to overexpression of hypoxia-inducible factor-1alpha in clear cell renal carcinomas. Cancer Res 61: 5215-5222.
    • (2001) Cancer Res , vol.61 , pp. 5215-5222
    • Wiesener, M.S.1    Munchenhagen, P.M.2    Berger, I.3    Morgan, N.V.4    Roigas, J.5
  • 13
    • 33748302779 scopus 로고    scopus 로고
    • Expression of hypoxia-inducible factor-1-alpha, hypoxia-inducible factor-2alpha and vascular endothelial growth factor in sporadic clear cell renal cell renal cell carcinoma and their significance in the pathogenesis thereof
    • Zhang N, Gong K, Yang XY, Xin DQ, Na YQ, (2006) [Expression of hypoxia-inducible factor-1-alpha, hypoxia-inducible factor-2alpha and vascular endothelial growth factor in sporadic clear cell renal cell renal cell carcinoma and their significance in the pathogenesis thereof]. Zhonghua Yi Xue Za Zhi 86: 1526-1529.
    • (2006) Zhonghua Yi Xue Za Zhi , vol.86 , pp. 1526-1529
    • Zhang, N.1    Gong, K.2    Yang, X.Y.3    Xin, D.Q.4    Na, Y.Q.5
  • 14
    • 0029090338 scopus 로고
    • Tumour suppression by the human von Hippel-Lindau gene product
    • Iliopoulos O, Kibel A, Gray S, Kaelin WG Jr, (1995) Tumour suppression by the human von Hippel-Lindau gene product. Nat Med 1: 822-826.
    • (1995) Nat Med , vol.1 , pp. 822-826
    • Iliopoulos, O.1    Kibel, A.2    Gray, S.3    Kaelin Jr., W.G.4
  • 15
    • 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 WG Jr, (2002) Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein. Cancer Cell 1: 237-246.
    • (2002) Cancer Cell , vol.1 , pp. 237-246
    • Kondo, K.1    Klco, J.2    Nakamura, E.3    Lechpammer, M.4    Kaelin Jr., W.G.5
  • 16
    • 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 JK, Vasselli JR, Riss J, Bonifacino JS, Linehan WM, et al. (2002) The contribution of VHL substrate binding and HIF1-alpha to the phenotype of VHL loss in renal cell carcinoma. Cancer Cell 1: 247-255.
    • (2002) Cancer Cell , vol.1 , pp. 247-255
    • Maranchie, J.K.1    Vasselli, J.R.2    Riss, J.3    Bonifacino, J.S.4    Linehan, W.M.5
  • 17
    • 34247250752 scopus 로고    scopus 로고
    • NAD(P)H oxidases regulate HIF-2alpha protein expression
    • Block K, Gorin Y, Hoover P, Williams P, Chelmicki T, et al. (2007) NAD(P)H oxidases regulate HIF-2alpha protein expression. J Biol Chem 282: 8019-8026.
    • (2007) J Biol Chem , vol.282 , pp. 8019-8026
    • Block, K.1    Gorin, Y.2    Hoover, P.3    Williams, P.4    Chelmicki, T.5
  • 18
    • 58049216350 scopus 로고    scopus 로고
    • Differential dependence of hypoxia-inducible factors 1 alpha and 2 alpha on mTORC1 and mTORC2
    • Toschi A, Lee E, Gadir N, Ohh M, Foster DA, (2008) Differential dependence of hypoxia-inducible factors 1 alpha and 2 alpha on mTORC1 and mTORC2. J Biol Chem 283: 34495-34499.
    • (2008) J Biol Chem , vol.283 , pp. 34495-34499
    • Toschi, A.1    Lee, E.2    Gadir, N.3    Ohh, M.4    Foster, D.A.5
  • 19
    • 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 DC, Cohen MB, Panka DJ, Collins M, Ghebremichael M, et al. (2010) The efficacy of the novel dual PI3-kinase/mTOR inhibitor NVP-BEZ235 compared with rapamycin in renal cell carcinoma. Clin Cancer Res 16: 3628-3638.
    • (2010) Clin Cancer Res , vol.16 , pp. 3628-3638
    • Cho, D.C.1    Cohen, M.B.2    Panka, D.J.3    Collins, M.4    Ghebremichael, M.5
  • 20
    • 34248336258 scopus 로고    scopus 로고
    • Hereditary leiomyomatosis and renal cell cancer: a syndrome associated with an aggressive form of inherited renal cancer
    • discussion 2079-2080
    • Grubb RL 3rd, Franks ME, Toro J, Middelton L, Choyke L, et al. (2007) Hereditary leiomyomatosis and renal cell cancer: a syndrome associated with an aggressive form of inherited renal cancer. J Urol 177: 2074-2079; discussion 2079-2080.
    • (2007) J Urol , vol.177 , pp. 2074-2079
    • Grubb 3rd, R.L.1    Franks, M.E.2    Toro, J.3    Middelton, L.4    Choyke, L.5
  • 21
    • 34147117259 scopus 로고    scopus 로고
    • Conventional renal cancer in a patient with fumarate hydratase mutation
    • Lehtonen HJ, Blanco I, Piulats JM, Herva R, Launonen V, et al. (2007) Conventional renal cancer in a patient with fumarate hydratase mutation. Hum Pathol 38: 793-796.
    • (2007) Hum Pathol , vol.38 , pp. 793-796
    • Lehtonen, H.J.1    Blanco, I.2    Piulats, J.M.3    Herva, R.4    Launonen, V.5
  • 22
    • 77952079054 scopus 로고    scopus 로고
    • The NADPH oxidase subunit p22phox inhibits the function of the tumor suppressor protein tuberin
    • Block K, Gorin Y, New DD, Eid A, Chelmicki T, et al. (2010) The NADPH oxidase subunit p22phox inhibits the function of the tumor suppressor protein tuberin. The American journal of pathology 176: 2447-2455.
    • (2010) The American Journal of Pathology , vol.176 , pp. 2447-2455
    • Block, K.1    Gorin, Y.2    New, D.D.3    Eid, A.4    Chelmicki, T.5
  • 24
    • 3142626559 scopus 로고    scopus 로고
    • Molecular genetic analysis of FIH-1, FH, and SDHB candidate tumour suppressor genes in renal cell carcinoma
    • Morris MR, Maina E, Morgan NV, Gentle D, Astuti D, et al. (2004) Molecular genetic analysis of FIH-1, FH, and SDHB candidate tumour suppressor genes in renal cell carcinoma. J Clin Pathol 57: 706-711.
    • (2004) J Clin Pathol , vol.57 , pp. 706-711
    • Morris, M.R.1    Maina, E.2    Morgan, N.V.3    Gentle, D.4    Astuti, D.5
  • 26
    • 77955170881 scopus 로고    scopus 로고
    • Hypoxia-regulated microRNA-210 modulates mitochondrial function and decreases ISCU and COX10 expression
    • Chen Z, Li Y, Zhang H, Huang P, Luthra R, (2010) Hypoxia-regulated microRNA-210 modulates mitochondrial function and decreases ISCU and COX10 expression. Oncogene 29: 4362-4368.
    • (2010) Oncogene , vol.29 , pp. 4362-4368
    • Chen, Z.1    Li, Y.2    Zhang, H.3    Huang, P.4    Luthra, R.5
  • 27
    • 67651204610 scopus 로고    scopus 로고
    • Fumarate hydratase deficiency in renal cancer induces glycolytic addiction and hypoxia-inducible transcription factor 1alpha stabilization by glucose-dependent generation of reactive oxygen species
    • Sudarshan S, Sourbier C, Kong HS, Block K, Valera Romero VA, et al. (2009) Fumarate hydratase deficiency in renal cancer induces glycolytic addiction and hypoxia-inducible transcription factor 1alpha stabilization by glucose-dependent generation of reactive oxygen species. Mol Cell Biol 29: 4080-4090.
    • (2009) Mol Cell Biol , vol.29 , pp. 4080-4090
    • Sudarshan, S.1    Sourbier, C.2    Kong, H.S.3    Block, K.4    Valera Romero, V.A.5
  • 28
    • 33846254999 scopus 로고    scopus 로고
    • RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha
    • Liu YV, Baek JH, Zhang H, Diez R, Cole RN, et al. (2007) RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha. Molecular cell 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
  • 29
    • 77956503391 scopus 로고    scopus 로고
    • Dysregulation of hypoxia pathways in fumarate hydratase-deficient cells is independent of defective mitochondrial metabolism
    • O'Flaherty L, Adam J, Heather LC, Zhdanov AV, Chung YL, et al. (2010) Dysregulation of hypoxia pathways in fumarate hydratase-deficient cells is independent of defective mitochondrial metabolism. Hum Mol Genet 19: 3844-3851.
    • (2010) Hum Mol Genet , vol.19 , pp. 3844-3851
    • O'Flaherty, L.1    Adam, J.2    Heather, L.C.3    Zhdanov, A.V.4    Chung, Y.L.5
  • 30
    • 77950553262 scopus 로고    scopus 로고
    • Fumarase: a mitochondrial metabolic enzyme and a cytosolic/nuclear component of the DNA damage response
    • Yogev O, Singer E, Shaulian E, Goldberg M, Fox TD, et al. (2010) Fumarase: a mitochondrial metabolic enzyme and a cytosolic/nuclear component of the DNA damage response. PLoS Biol 8: e1000328.
    • (2010) PLoS Biol , vol.8
    • Yogev, O.1    Singer, E.2    Shaulian, E.3    Goldberg, M.4    Fox, T.D.5
  • 31
    • 33747042840 scopus 로고    scopus 로고
    • AKT can be activated in the nucleus
    • Wang R, Brattain MG, (2006) AKT can be activated in the nucleus. Cell Signal 18: 1722-1731.
    • (2006) Cell Signal , vol.18 , pp. 1722-1731
    • Wang, R.1    Brattain, M.G.2
  • 32
    • 0034964421 scopus 로고    scopus 로고
    • Gene mutations in the succinate dehydrogenase subunit SDHB cause susceptibility to familial pheochromocytoma and to familial paraganglioma
    • Astuti D, Latif F, Dallol A, Dahia PL, Douglas F, et al. (2001) Gene mutations in the succinate dehydrogenase subunit SDHB cause susceptibility to familial pheochromocytoma and to familial paraganglioma. Am J Hum Genet 69: 49-54.
    • (2001) Am J Hum Genet , vol.69 , pp. 49-54
    • Astuti, D.1    Latif, F.2    Dallol, A.3    Dahia, P.L.4    Douglas, F.5
  • 34
    • 0033767445 scopus 로고    scopus 로고
    • Mutations in SDHC cause autosomal dominant paraganglioma, type 3
    • Niemann S, Muller U, (2000) Mutations in SDHC cause autosomal dominant paraganglioma, type 3. Nat Genet 26: 268-270.
    • (2000) Nat Genet , vol.26 , pp. 268-270
    • Niemann, S.1    Muller, U.2
  • 35
    • 79958842198 scopus 로고    scopus 로고
    • Defects in succinate dehydrogenase in gastrointestinal stromal tumors lacking KIT and PDGFRA mutations
    • Janeway KA, Kim SY, Lodish M, Nose V, Rustin P, et al. (2010) Defects in succinate dehydrogenase in gastrointestinal stromal tumors lacking KIT and PDGFRA mutations. Proc Natl Acad Sci U S A.
    • (2010) Proc Natl Acad Sci U S A
    • Janeway, K.A.1    Kim, S.Y.2    Lodish, M.3    Nose, V.4    Rustin, P.5
  • 36
    • 77955594623 scopus 로고    scopus 로고
    • A HIF1alpha regulatory loop links hypoxia and mitochondrial signals in pheochromocytomas
    • Dahia PL, Ross KN, Wright ME, Hayashida CY, Santagata S, et al. (2005) A HIF1alpha regulatory loop links hypoxia and mitochondrial signals in pheochromocytomas. PLoS Genet 1: 72-80.
    • (2005) PLoS Genet , vol.1 , pp. 72-80
    • Dahia, P.L.1    Ross, K.N.2    Wright, M.E.3    Hayashida, C.Y.4    Santagata, S.5
  • 37
    • 70349266564 scopus 로고    scopus 로고
    • Oxygen consumption can regulate the growth of tumors, a new perspective on the Warburg effect
    • Chen Y, Cairns R, Papandreou I, Koong A, Denko NC, (2009) Oxygen consumption can regulate the growth of tumors, a new perspective on the Warburg effect. PLoS One 4: e7033.
    • (2009) PLoS One , vol.4
    • Chen, Y.1    Cairns, R.2    Papandreou, I.3    Koong, A.4    Denko, N.C.5
  • 38
    • 77955815630 scopus 로고    scopus 로고
    • Fumarase tumor suppressor gene and MET oncogene cooperate in upholding transformation and tumorigenesis
    • Costa B, Dettori D, Lorenzato A, Bardella C, Coltella N, et al. (2010) Fumarase tumor suppressor gene and MET oncogene cooperate in upholding transformation and tumorigenesis. FASEB J 24: 2680-2688.
    • (2010) FASEB J , vol.24 , pp. 2680-2688
    • Costa, B.1    Dettori, D.2    Lorenzato, A.3    Bardella, C.4    Coltella, N.5
  • 39
  • 40
    • 33846675525 scopus 로고    scopus 로고
    • Tumor cell invasion of von Hippel Lindau renal cell carcinoma cells is mediated by membrane type-1 matrix metalloproteinase
    • Petrella BL, Brinckerhoff CE, (2006) Tumor cell invasion of von Hippel Lindau renal cell carcinoma cells is mediated by membrane type-1 matrix metalloproteinase. Molecular cancer 5: 66.
    • (2006) Molecular Cancer , vol.5 , pp. 66
    • Petrella, B.L.1    Brinckerhoff, C.E.2
  • 41
    • 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, Sowter HM, Mandriota SJ, 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    Sowter, H.M.4    Mandriota, S.J.5
  • 42
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.