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Volumn 66, Issue 13, 2009, Pages 2167-2180

15-Deoxy-Δ12,14-prostaglandin-J2 reveals a new pVHL-independent, lysosomal-dependent mechanism of HIF-1α degradation

Author keywords

15 Deoxy 12,14 prostaglandin J2; Calpain; Heat shock protein 90; Hypoxia inducible factor; Lysosome; Proximal tubular cells

Indexed keywords

15 DEOXY DELTA12,14 PROSTAGLANDIN J2; CATHEPSIN B; HYPOXIA INDUCIBLE FACTOR 1ALPHA; VON HIPPEL LINDAU PROTEIN;

EID: 67649933387     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-009-0039-x     Document Type: Article
Times cited : (17)

References (45)
  • 3
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation
    • DOI 10.1093/emboj/20.18.5197
    • N Masson C Willam PH Maxwell CW Pugh PJ Ratcliffe 2001 Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation EMBO J 20 5197 5206 (Pubitemid 32910914)
    • (2001) EMBO Journal , vol.20 , Issue.18 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 4
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • DOI 10.1074/jbc.M304982200
    • M Hirsila P Koivunen V Gunzler KI Kivirikko J Myllyharju 2003 Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor J Biol Chem 278 33 30772 30780 (Pubitemid 36994584)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 30772-30780
    • Hirsila, M.1    Koivunen, P.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 6
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain: A hypoxic switch
    • DOI 10.1126/science.1068592
    • D Lando DJ Peet DA Whelan JJ Gorman ML Whitelaw 2002 Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch Science 295 5556 858 861 (Pubitemid 34118367)
    • (2002) Science , vol.295 , Issue.5556 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 8
    • 27944506308 scopus 로고    scopus 로고
    • Improvement of kidney function in a rat model of renal ischemia-reperfusion injury by treatment with a novel HIF prolyl-hydroxylase inhibitor. ASN annual meeting, St Louis MO
    • G Guo 2004 Improvement of kidney function in a rat model of renal ischemia-reperfusion injury by treatment with a novel HIF prolyl-hydroxylase inhibitor. ASN annual meeting, St Louis MO J Am Soc Nephrol 15 460A
    • (2004) J Am Soc Nephrol , vol.15
    • Guo, G.1
  • 10
    • 34548418008 scopus 로고    scopus 로고
    • Accumulation of hypoxia-inducible factor-1α through a novel electrophilic, thiol antioxidant-sensitive mechanism
    • DOI 10.1016/j.cellsig.2007.06.004, PII S0898656807001799
    • G Olmos I Conde MI Arenas L Del Peso C Castellanos MO Landazuri FJ Lucio-Cazana 2007 Accumulation of hypoxia-inducible factor-1α through a novel electrophilic, thiol antioxidant-sensitive mechanism Cell Signal 19 2098 2105 (Pubitemid 47353813)
    • (2007) Cellular Signalling , vol.19 , Issue.10 , pp. 2098-2105
    • Olmos, G.1    Conde, I.2    Arenas, I.3    Del Peso, L.4    Castellanos, C.5    Landazuri, M.O.6    Lucio-Cazana, J.7
  • 11
    • 34247583794 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates hypoxia-inducible factor 1α and mediates its destabilization in a VHL-independent manner
    • DOI 10.1128/MCB.00015-07
    • D Flügel A Görlach C Michiels T Kietzmann 2007 Glycogen synthase kinase 3 phosphorylates hypoxia-inducible factor 1α and mediates its destabilization in a VHL-independent manner Mol Cell Biol 27 3253 3265 (Pubitemid 46685205)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.9 , pp. 3253-3265
    • Flugel, D.1    Gorlach, A.2    Michiels, C.3    Kietzmann, T.4
  • 12
    • 33846254999 scopus 로고    scopus 로고
    • 2-Independent and HSP90 Inhibitor-Induced Degradation of HIF-1α
    • DOI 10.1016/j.molcel.2007.01.001, PII S1097276507000020
    • YV Liu JH Baek H Zhang R Diez RN Cole GL Semenza 2007 RACK1 Competes with HSP90 for Binding to HIF-1α and is Required for O2-independent and HSP90 Inhibitor-induced Degradation of HIF-1α Mol Cell 25 207 217 (Pubitemid 46109612)
    • (2007) Molecular Cell , vol.25 , Issue.2 , 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
  • 13
    • 33749006252 scopus 로고    scopus 로고
    • Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1α
    • DOI 10.1158/0008-5472.CAN-05-4598
    • Qian DZ, Kachhap SK, Collis SJ, Verheul HMW, Carducci MA, Atadja P, Pili R (2006) Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1A. Cancer Res 66:8814-8821 (Pubitemid 44449199)
    • (2006) Cancer Research , vol.66 , Issue.17 , pp. 8814-8821
    • Qian, D.Z.1    Kachhap, S.K.2    Collis, S.J.3    Verheul, H.M.W.4    Carducci, M.A.5    Atadja, P.6    Pili, R.7
  • 14
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α-degradative pathway
    • JS Isaacs Y Jung EG Mimnaugh ZA Martine F Cuttitta LM Neckers 2002 Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α- degradative pathway J Biol Chem 277 29936 29944
    • (2002) J Biol Chem , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1    Jung, Y.2    Mimnaugh, E.G.3    Martine, Z.A.4    Cuttitta, F.5    Neckers, L.M.6
  • 15
    • 33745398366 scopus 로고    scopus 로고
    • Calpain mediates a von Hippel-Lindau protein-independent destruction of hypoxia-inducible factor-1α
    • DOI 10.1091/mbc.E05-08-0770
    • J Zhou R Köhl B Herr R Frank B Brüne 2006 Calpain mediates a von hippel-lindau protein-independent destruction of hypoxia-inducible factor-1α Mol Cell Biol 17 1549 1558 (Pubitemid 44011575)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.4 , pp. 1549-1558
    • Zhou, J.1    Kohl, R.2    Herr, B.3    Frank, R.4    Brune, B.5
  • 16
    • 23044432584 scopus 로고    scopus 로고
    • Cathepsin B regulates the intrinsic angiogenic threshold of endothelial cells
    • DOI 10.1091/mbc.E04-11-1029
    • E Im A Venkatakrishan A Kazlauskas 2005 Cathepsin B regulates the intrinsic angiogenic threshold of endotelial cells Mol Biol Cell 16 3488 3500 (Pubitemid 41077063)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.8 , pp. 3488-3500
    • Im, E.1    Venkatakrishnan, A.2    Kazlauskas, A.3
  • 19
    • 34447522124 scopus 로고    scopus 로고
    • Constitutive/hypoxic degradation of HIF-α proteins by the proteasome is independent of von Hippel Lindau protein ubiquitylation and the transactivation activity of the protein
    • DOI 10.1074/jbc.M700704200
    • W Kong B Alvarez-Castelao ZJ Lin JG Castano J Caro 2007 Constitutive/Hypoxic Degradation of HIF-α Proteins by the Proteasome Is Independent of von Hippel Lindau Protein Ubiquitylation and the Transactivation Activity of the Protein J Biol Chem 282 15498 15505 (Pubitemid 47093272)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.21 , pp. 15498-15505
    • Kong, X.1    Alvarez-Castelao, B.2    Lin, Z.3    Castano, J.G.4    Caro, J.5
  • 20
    • 33645459848 scopus 로고    scopus 로고
    • Identification of novel protein targets for modification by 15-deoxy-Δ12, 14-prostaglandin-J2 in mesangial cells reveals multiple interactions with the cytoskeleton
    • K Stamatakis FJ Sanchez-Gomez D Perez-Sala 2006 Identification of novel protein targets for modification by 15-deoxy-Δ12, 14-prostaglandin-J2 in mesangial cells reveals multiple interactions with the cytoskeleton J Am Soc Nephrol 17 89 98
    • (2006) J Am Soc Nephrol , vol.17 , pp. 89-98
    • Stamatakis, K.1    Sanchez-Gomez, F.J.2    Perez-Sala, D.3
  • 21
    • 0035877804 scopus 로고    scopus 로고
    • The cathepsin B inhibitor z-FA.fmk inhibits cytokine production in macrophages stimulated by lipopolysaccharide
    • P Schotte R Schauvliege S Janssens R Beyaert 2001 The cathepsin B inhibitor z-FA.fmk inhibits cytokine production in macrophages stimulated by lipopolysaccharide J Biol Chem 276 21153 21157
    • (2001) J Biol Chem , vol.276 , pp. 21153-21157
    • Schotte, P.1    Schauvliege, R.2    Janssens, S.3    Beyaert, R.4
  • 23
    • 0035862167 scopus 로고    scopus 로고
    • Nuclear localization of cystatin B, the cathepsin inhibitor implicated in myoclonus epilepsy (EPM1)
    • DOI 10.1006/excr.2000.5085
    • M Riccio R Di Giaimo S Pianetti PP Palmieri M Melli S Santi 2001 Nuclear localization of cystatin B, the cathepsin inhibitor implicated in myoclonus epilepsy (EPM1) Exp Cell Res 262 84 94 (Pubitemid 32980247)
    • (2001) Experimental Cell Research , vol.262 , Issue.2 , pp. 84-94
    • Riccio, M.1    Di Giaimo, R.2    Pianetti, S.3    Palmieri, P.P.4    Melli, M.5    Santi, S.6
  • 24
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • DOI 10.1016/S0962-8924(98)01346-4
    • DH Lee AL Goldberg 1998 Proteasome inhibitors: valuable new tools for cell biologists Trends Cell Biol 8 397 403 (Pubitemid 28458705)
    • (1998) Trends in Cell Biology , vol.8 , Issue.10 , pp. 397-403
    • Lee, D.H.1
  • 25
    • 0142009674 scopus 로고    scopus 로고
    • Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions
    • G Fuertes JJ Martín de Llano A Villarroya A Rivett E Knecht 2003 Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions Biochem J 375 75 80
    • (2003) Biochem J , vol.375 , pp. 75-80
    • Fuertes, G.1    De Martín, J.J.L.2    Villarroya, A.3    Rivett, A.4    Knecht, E.5
  • 26
    • 33646841837 scopus 로고    scopus 로고
    • Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate
    • DOI 10.1074/jbc.M509043200
    • AF Kisselev A Callard AL Goldberg 2006 Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate J Biol Chem 281 8582 8590 (Pubitemid 43847961)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.13 , pp. 8582-8590
    • Kisselev, A.F.1    Callard, A.2    Goldberg, A.L.3
  • 30
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signalling: Role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products
    • DOI 10.1042/BJ20031049
    • AL Levonen A Landar A Ramachandran EK Ceaser DA Dickinson G Zanoni JD Morrow VM Darley-Usmar 2004 Cellular mechanisms of redox cell signaling: the role of cysteine modification in controlling antioxidant defenses in response to electrophilic lipid oxidation products Biochem J 378 373 382 (Pubitemid 38367228)
    • (2004) Biochemical Journal , vol.378 , Issue.2 , pp. 373-382
    • Levonen, A.-L.1    Landar, A.2    Ramachandran, A.3    Ceaser, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8
  • 31
    • 6944250291 scopus 로고    scopus 로고
    • 2 addition in mesangial cells: Role in the inhibition of pro-inflammatory genes
    • DOI 10.1124/mol.104.002824
    • FJ Sanchez-Gomez E Cernuda-Morollon K Stamatakis D Perez-Sala 2004 Protein thiol modification by 15-deoxy-Δ12, 14-prostaglandin J2 addition in mesangial cells: role in the inhibition of pro-inflammatory genes Mol Pharmacol 66 5 1349 1358 (Pubitemid 39411076)
    • (2004) Molecular Pharmacology , vol.66 , Issue.5 , pp. 1349-1358
    • Sanchez-Gomez, F.J.1    Cernuda-Morollon, E.2    Stamatakis, K.3    Perez-Sala, D.4
  • 33
    • 0034472510 scopus 로고    scopus 로고
    • Experimental hypoxia of STZ-diabetic rat myocardium and protective effects of Ginkgo biloba extract: II. Ultrastructural investigation of microvascular endothelium
    • K Welt G Fitzl A Schepper 2001 Experimental hypoxia of STZ-diabetic rat myocardium and protective effects of Ginkgo biloba extrac. II. Ultrastructura investigation of microvascular endothelium Exp Toxicol Pathol 52 6 503 512 (Pubitemid 33791860)
    • (2001) Experimental and Toxicologic Pathology , vol.52 , Issue.6 , pp. 503-512
    • Welt, K.1    Fitzl, G.2    Schepper, A.3
  • 35
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • F Agarraberes J Dice 2001 A molecular chaperone complex at the lysosomal membrane is required for protein translocation J Cell Sci 114 2491 2499 (Pubitemid 32684803)
    • (2001) Journal of Cell Science , vol.114 , Issue.13 , pp. 2491-2499
    • Agarraberes, F.A.1    Dice, J.F.2
  • 36
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperone-mediated autophagy during oxidative stress
    • DOI 10.1091/mbc.E04-06-0477
    • R Kiffin C Christian E Knecht AM Cuervo 2004 Activation of chaperone-mediated autophagy during oxidative stress Mol Biol Cell 15 4829 4840 (Pubitemid 39392200)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.11 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.2    Knecht, E.3    Cuervo, A.M.4
  • 37
    • 4444260675 scopus 로고    scopus 로고
    • Interaction of the PAS B Domain with HSP90 Accelerates Hypoxia-Inducible Factor-1α Stabilization
    • D Katschinsk L Le S Schindler T Thomas A Voss R Wenger 2004 Interaction of the PAS B Domain with HSP90 Accelerates Hypoxia-Inducible Factor-1α Stabilization Cell Physiol Biochem 14 4 6
    • (2004) Cell Physiol Biochem , vol.14 , pp. 4-6
    • Katschinsk, D.1    Le, L.2    Schindler, S.3    Thomas, T.4    Voss, A.5    Wenger, R.6
  • 38
    • 33745022323 scopus 로고    scopus 로고
    • Cell-type-specific regulation of degradation of hypoxia-inducible factor 1α: Role of subcellular compartmentalization
    • DOI 10.1128/MCB.02236-05
    • X Zheng JL Ruas R Cao FA Salomons Y Cao L Poellinger T Pereira 2006 Cell-type-specific regulation of degradation of hypoxia-inducible factor 1 alpha: role of subcellular compartmentalization Mol Cell Biol 26 4628 4641 (Pubitemid 43877580)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.12 , pp. 4628-4641
    • Zheng, X.1    Ruas, J.L.2    Cao, R.3    Salomons, F.A.4    Cao, Y.5    Poellinger, L.6    Pereira, T.7
  • 39
    • 34548360660 scopus 로고    scopus 로고
    • Peroxisomal localization of hypoxia-inducible factors and hypoxia-inducible factor regulatory hydroxylases in primary rat hepatocytes exposed to hypoxia-reoxygenation
    • DOI 10.2353/ajpath.2006.060360
    • Z Khan GK Michalopoulos DB Stolz 2006 Peroxisomal localization of hypoxia-inducible factors and hypoxia inducible factor regulaoty hydroxylases in primary rat hepatocytes exposed to hypoxia-reoxigenation Am J Pathol 169 4 1251 1269 (Pubitemid 351194361)
    • (2006) American Journal of Pathology , vol.169 , Issue.4 , pp. 1251-1269
    • Khan, Z.1    Michalopoulos, G.K.2    Stolz, D.B.3
  • 41
    • 33748417446 scopus 로고    scopus 로고
    • Release of iron from ferritin requires lysosomal activity
    • TZ Kidane E Sauble MC Linder 2006 Release of iron from ferritin requires lysosomal activity Am J Physiol 291 C445 C455
    • (2006) Am J Physiol , vol.291
    • Kidane, T.Z.1    Sauble, E.2    Linder, M.C.3
  • 42
    • 0035929592 scopus 로고    scopus 로고
    • 15-Deoxy-Delta 12, 14-prostaglandin J2 inhibition of NF-kappaB-DNA binding through covalent modification of the p50 subunit
    • E Cernuda-Morollon E Pineda-Molina FJ Canada D Perez-Sala 2001 15-Deoxy-Delta 12, 14-prostaglandin J2 inhibition of NF-kappaB-DNA binding through covalent modification of the p50 subunit J Biol Chem 276 38 35530 35536
    • (2001) J Biol Chem , vol.276 , Issue.38 , pp. 35530-35536
    • Cernuda-Morollon, E.1    Pineda-Molina, E.2    Canada, F.J.3    Perez-Sala, D.4
  • 43
    • 0035053973 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins: New insights on biological activities and cellular targets
    • DOI 10.1002/med.1006
    • DS Strauss CK Glass 2001 Cyclopentenone prostaglandins: new insights on biological activities and cellular targets Med Res Rev 21 3 185 210 (Pubitemid 32303994)
    • (2001) Medicinal Research Reviews , vol.21 , Issue.3 , pp. 185-210
    • Straus, D.S.1    Glass, C.K.2


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