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Volumn 70, Issue 8, 2010, Pages 3071-3079

The connectivity map links iron regulatory protein-1-mediated inhibition of hypoxia-inducible factor-2a translation to the anti-inflammatory 15-deoxy-△12,14-prostaglandin J2

Author keywords

[No Author keywords available]

Indexed keywords

15 DEOXY DELTA12,14 PROSTAGLANDIN J2; CYTOKINE; HYPOXIA INDUCIBLE FACTOR 1; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 1BETA; HYPOXIA INDUCIBLE FACTOR 2; HYPOXIA INDUCIBLE FACTOR 2ALPHA; HYPOXIA INDUCIBLE FACTOR 2BETA; IRON REGULATORY PROTEIN 1; MAMMALIAN TARGET OF RAPAMYCIN; UNCLASSIFIED DRUG;

EID: 77951082053     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-09-2877     Document Type: Article
Times cited : (35)

References (38)
  • 1
    • 34247385849 scopus 로고    scopus 로고
    • Molecular biology of renal cell cancer and the identification of therapeutic targets
    • DOI 10.1200/JCO.2006.08.8948
    • Iliopoulos O. Molecular biology of renal cell cancer and the identification of therapeutic targets. J Clin Oncol 2006;24:5593-5600 (Pubitemid 46631340)
    • (2006) Journal of Clinical Oncology , vol.24 , Issue.35 , pp. 5593-5600
    • Iliopoulos, O.1
  • 2
    • 0036528246 scopus 로고    scopus 로고
    • Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein
    • DOI 10.1016/S1535-6108(02)00043-0
    • Kondo K, Klco J, Nakamura E, Lechpammer M, Kaelin WG. Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein. Cancer Cell 2002;1:237-246 (Pubitemid 41039148)
    • (2002) Cancer Cell , vol.1 , Issue.3 , pp. 237-246
    • Kondo, K.1    Klco, J.2    Nakamura, E.3    Lechpammer, M.4    Kaelin Jr., W.G.5
  • 3
    • 2342597973 scopus 로고    scopus 로고
    • Inhibition of HIF2α is sufficient to suppress pVHL-defective tumor growth
    • DOI 10.1371/journal.pbio.0000083
    • Kondo K, KimWY, LechpammerM, Kaelin WG. Inhibition of HIF2α is sufficient to suppress pVHL-defective tumor growth. PLoS Biol 2003;1:83. (Pubitemid 39112142)
    • (2003) PLoS Biology , vol.1 , Issue.3
    • Kondo, K.1    Kim, W.Y.2    Lechpammer, M.3    Kaelin Jr., W.G.4
  • 4
    • 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. Mol Cancer Res 2004;2:89-95. (Pubitemid 38250425)
    • (2004) Molecular Cancer Research , vol.2 , Issue.2 , pp. 89-95
    • Zimmer, M.1    Doucette, D.2    Siddiqui, N.3    Iliopoulos, O.4
  • 5
    • 35349001759 scopus 로고    scopus 로고
    • Inhibition of VEGF expression by targeting HIF-1α with small interference RNA in human RPE cells
    • DOI 10.1159/000107502
    • Zhang P, Wang Y, Hui Y, et al. Inhibition of VEGF expression by targeting HIF-1α with small interference RNA in human RPE cells. Ophthalmologica 2007;221:411-417 (Pubitemid 47608868)
    • (2007) Ophthalmologica , vol.221 , Issue.6 , pp. 411-417
    • Zhang, P.1    Wang, Y.2    Hui, Y.3    Hu, D.4    Wang, H.5    Zhou, J.6    Du, H.7
  • 9
    • 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 BL, Neil C, et al. Small-molecule inhibitors of HIF-2a translation link its 5′UTR iron-responsive element to oxygen sensing. Mol Cell 2008;32:838-848
    • (2008) Mol Cell , vol.32 , pp. 838-848
    • Zimmer, M.1    Ebert, B.L.2    Neil, C.3
  • 10
    • 34247628002 scopus 로고    scopus 로고
    • Iron-regulatory proteins limit hypoxia-inducible factor-2α expression in iron deficiency
    • DOI 10.1038/nsmb1222, PII NSMB1222
    • Sanchez M, Galy B, Muckenthaler MU, Hentze MW. Iron-regulatory proteins limit hypoxia-inducible factor-2α expression in iron deficiency. Nat Struct Mol Biol 2007;14:420-426 (Pubitemid 46685876)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.5 , pp. 420-426
    • Sanchez, M.1    Galy, B.2    Muckenthaler, M.U.3    Hentze, M.W.4
  • 11
    • 33750530167 scopus 로고    scopus 로고
    • 2 as a potential endogenous regulator of redox-sensitive transcription factors
    • 2 as a potential endogenous regulator of redox-sensitive transcription factors. Biochem Pharmacol 2006;72:1516-1528
    • (2006) Biochem Pharmacol , vol.72 , pp. 1516-1528
    • Kim, E.H.1    Surh, Y.J.2
  • 15
    • 0004136246 scopus 로고
    • Sambrook J, Fritsch EF, Maniatis T, editors. CSHL Press
    • In: Sambrook J, Fritsch EF, Maniatis T, editors. Molecular cloning: a laboratory manual: CSHL Press; 1989.
    • (1989) Molecular Cloning: A Laboratory Manual
  • 17
    • 22544464680 scopus 로고    scopus 로고
    • HnRNP K binds a core polypyrimidine element in the eukaryotic translation initiation factor 4E (eIF4E) promoter, and its regulation of eIF4E contributes to neoplastic transformation
    • DOI 10.1128/MCB.25.15.6436-6453.2005
    • Lynch M, Chen L, Ravitz MJ, et al. hnRNP K binds a core polypyrimidine element in the eukaryotic translation initiation factor 4E (eIF4E) promoter, and its regulation of eIF4E contributes to neoplastic transformation. Mol Cell Biol 2005;25:6436-6453 (Pubitemid 41023220)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.15 , pp. 6436-6453
    • Lynch, M.1    Chen, L.2    Ravitz, M.J.3    Mehtani, S.4    Korenblat, K.5    Pazin, M.J.6    Schmidt, E.V.7
  • 18
    • 0037048648 scopus 로고    scopus 로고
    • The prolyl 4-hydroxylase inhibitor ethyl-3,4-dihydroxybenzoate generates effective iron deficiency in cultured cells
    • Wang J, Buss JL, Chen G, Ponka P, Pantopoulos K. The prolyl 4-hydroxylase inhibitor ethyl-3,4-dihydroxybenzoate generates effective iron deficiency in cultured cells. FEBS Lett 2002;529:309-312
    • (2002) FEBS Lett , vol.529 , pp. 309-312
    • Wang, J.1    Buss, J.L.2    Chen, G.3    Ponka, P.4    Pantopoulos, K.5
  • 19
    • 0036789574 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 1α expression and function by the mammalian target of rapamycin
    • Hudson CC, Liu M, Chiang GG, et al. Regulation of hypoxia-inducible factor 1α expression and function by the mammalian target of rapamycin. Mol Cell Biol 2002;22:7004-7014
    • (2002) Mol Cell Biol , vol.22 , pp. 7004-7014
    • Hudson, C.C.1    Liu, M.2    Chiang, G.G.3
  • 22
    • 1942453838 scopus 로고    scopus 로고
    • A Novel Function of the MA-3 Domains in Transformation and Translation Suppressor Pdcd4 Is Essential for Its Binding to Eukaryotic Translation Initiation Factor 4A
    • DOI 10.1128/MCB.24.9.3894-3906.2004
    • Yang HS, Cho MH, Zakowicz H, Hegamyer G, Sonenberg N, Colburn NH. A novel function of the MA-3 domains in transformation and translation suppressor Pdcd4 is essential for its binding to eukaryotic translation initiation factor 4A. Mol Cell Biol 2004;24:3894-3906 (Pubitemid 38496167)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.9 , pp. 3894-3906
    • Yang, H.-S.1    Cho, M.-H.2    Zakowicz, H.3    Hegamyer, G.4    Sonenberg, N.5    Colburn, N.H.6
  • 23
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • DOI 10.1038/nchembio807, PII NCHEMBIO807
    • Rouault TA. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat Chem Biol 2006;2:406-414 (Pubitemid 44114917)
    • (2006) Nature Chemical Biology , vol.2 , Issue.8 , pp. 406-414
    • Rouault, T.A.1
  • 24
    • 0032508548 scopus 로고    scopus 로고
    • Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding. Fine-tuning of mRNA regulation?
    • Ke Y, Wu J, Leibold EA, Walden WE, Theil EC. Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding. Fine-tuning of mRNA regulation? J Biol Chem 1998;273:23637-23640
    • (1998) J Biol Chem , vol.273 , pp. 23637-23640
    • Ke, Y.1    Wu, J.2    Leibold, E.A.3    Walden, W.E.4    Theil, E.C.5
  • 25
    • 58049216350 scopus 로고    scopus 로고
    • Differential dependence of hypoxia-inducible factors 1α and 2α on mTORC1 and mTORC2
    • Toschi A, Lee E, Gadir N, Ohh M, Foster DA. Differential dependence of hypoxia-inducible factors 1α and 2α on mTORC1 and mTORC2. J Biol Chem 2008;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
  • 26
    • 0037146555 scopus 로고    scopus 로고
    • 2 induces hypoxia-inducible factor-1α stabilization and nuclear localization in a human prostate cancer cell line
    • 2 induces hypoxia-inducible factor-1α stabilization and nuclear localization in a human prostate cancer cell line. J Biol Chem 2002;277:50081-50086
    • (2002) J Biol Chem , vol.277 , pp. 50081-50086
    • Liu, X.H.1    Kirschenbaum, A.2    Lu, M.3
  • 28
    • 0036006453 scopus 로고    scopus 로고
    • 2, transactivates EGF receptor: A novel mechanism for promoting colon cancer growth and gastrointestinal hypertrophy
    • DOI 10.1038/nm0302-289
    • Pai R, Soreghan B, Szabo IL, Pavelka M, Baatar D, Tarnawski AS. Prostaglandin E2 transactivates EGF receptor: a novel mechanism for promoting colon cancer growth and gastrointestinal hypertrophy. Nat Med 2002;8:289-293 (Pubitemid 34250108)
    • (2002) Nature Medicine , vol.8 , Issue.3 , pp. 289-293
    • Pai, R.1    Soreghan, B.2    Szabo, I.L.3    Pavelka, M.4    Baatar, D.5    Tarnawski, A.S.6
  • 29
    • 16444385003 scopus 로고
    • 2 enhances intestinal adenoma growth via activation of the Rasmitogen-activated protein kinase cascade
    • 2 enhances intestinal adenoma growth via activation of the Rasmitogen-activated protein kinase cascade. Cancer Res 2005;65:1822-1829.
    • (1822) Cancer Res , vol.2005 , pp. 65
    • Wang, D.1    Buchanan, F.G.2    Wang, H.3    Dey, S.K.4    DuBois, R.N.5
  • 30
    • 4544320012 scopus 로고    scopus 로고
    • 2 promotes colorectal adenoma growth via transactivation of the nuclear peroxisome proliferator-activated receptor δ
    • DOI 10.1016/j.ccr.2004.08.011, PII S1535610804002168
    • Wang D, Wang H, Shi Q, et al. Prostaglandin E2 promotes colorectal adenoma growth via transactivation of the nuclear peroxisome proliferator-activated receptor δ. Cancer Cell 2004;6:285-295 (Pubitemid 39222041)
    • (2004) Cancer Cell , vol.6 , Issue.3 , pp. 285-295
    • Wang, D.1    Wang, H.2    Shi, Q.3    Katkuri, S.4    Walhi, W.5    Desvergne, B.6    Das, S.K.7    Dey, S.K.8    Dubois, R.N.9
  • 32
    • 67649933387 scopus 로고    scopus 로고
    • 2 reveals a new pVHL-independent, lysosomal-dependent mechanism of HIF-1α degradation
    • 2 reveals a new pVHL-independent, lysosomal-dependent mechanism of HIF-1α degradation. Cell Mol Life Sci 2009;66:2167-2180
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2167-2180
    • Olmos, G.1    Arenas, M.I.2    Bienes, R.3
  • 33
    • 31544470131 scopus 로고    scopus 로고
    • Activation of RhoB by hypoxia controls hypoxia-inducible factor-1α stabilization through glycogen synthase kinase-3 in U87 glioblastoma cells
    • DOI 10.1158/0008-5472.CAN-05-2299
    • Skuli N, Monferran S, Delmas C, et al. Activation of RhoB by hypoxia controls hypoxia-inducible factor-1α stabilization through glycogen synthase kinase-3 in U87 glioblastoma cells. Cancer Res 2006;66:482-489 (Pubitemid 43166057)
    • (2006) Cancer Research , vol.66 , Issue.1 , pp. 482-489
    • Skuli, N.1    Monferran, S.2    Delmas, C.3    Lajoie-Mazenc, I.4    Favre, G.5    Toulas, C.6    Cohen-Jonathan-Moyal, E.7
  • 35
    • 37149023303 scopus 로고    scopus 로고
    • 2 inhibits translation through inactivation of eIF4A
    • 2 inhibits translation through inactivation of eIF4A. EMBO J 2007;26:5020-5032
    • (2007) EMBO J , vol.26 , pp. 5020-5032
    • Kim, W.J.1    Kim, J.H.2    Jang, S.K.3
  • 36
    • 0023226442 scopus 로고
    • Iron deficiency and neutrophil function: Different rates of correction of the depressions in oxidative burst and myeloperoxidase activity after iron treatment
    • Murakawa H, Bland CE, Willis WT, Dallman PR. Iron deficiency and neutrophil function: different rates of correction of the depressions in oxidative burst and myeloperoxidase activity after iron treatment. Blood 1987;69:1464-1468 (Pubitemid 17088909)
    • (1987) Blood , vol.69 , Issue.5 , pp. 1464-1468
    • Murakawa, H.1    Bland, C.E.2    Willis, W.T.3    Dallman, P.R.4
  • 37
    • 43049124745 scopus 로고    scopus 로고
    • Iron and inflammation: Cross-talk between pathways regulating hepcidin
    • Fleming RE. Iron and inflammation: cross-talk between pathways regulating hepcidin. J Mol Med 2008;86:491-494
    • (2008) J Mol Med , vol.86 , pp. 491-494
    • Fleming, R.E.1
  • 38
    • 1842608845 scopus 로고    scopus 로고
    • Iron metabolism and the IRE/IRP regulatory system: An update
    • DOI 10.1196/annals.1306.001
    • Pantopoulos K. Iron metabolism and the IRE/IRP regulatory system: an update. Ann N Y Acad Sci 2004;1012:1-13. (Pubitemid 38453511)
    • (2004) Annals of the New York Academy of Sciences , vol.1012 , pp. 1-13
    • Pantopoulos, K.1


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