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Volumn 338, Issue 1, 2005, Pages 639-647

Dioxygenases as O2-dependent regulators of the hypoxic response pathway

Author keywords

Asparaginyl hydroxylase; Dioxygenase; FIH 1; HIF; Hypoxia; Oxygen sensing; Prolyl hydroxylase

Indexed keywords

2 OXOGLUTARIC ACID; ASPARAGINE; HYPOXIA INDUCIBLE FACTOR 1; IRON; NITRIC OXIDE; OXYGEN; OXYGENASE; PROLINE; PROTEIN INHIBITOR; DIOXYGENASE;

EID: 27544495625     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.140     Document Type: Review
Times cited : (49)

References (83)
  • 1
    • 0027461553 scopus 로고
    • Inducible operation of the erthropoietin 3′ enhancer in multiple cell lines: Evidence for a widespread oxygen sensing mechanism
    • P.H. Maxwell, C.W. Pugh, and P.J. Ratcliffe Inducible operation of the erthropoietin 3′ enhancer in multiple cell lines: evidence for a widespread oxygen sensing mechanism Proc. Natl. Acad. Sci. USA 90 1993 2423 2427
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2423-2427
    • Maxwell, P.H.1    Pugh, C.W.2    Ratcliffe, P.J.3
  • 3
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • G.L. Semenza Targeting HIF-1 for cancer therapy Nat. Rev. Cancer 3 2003 721 732
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 5
    • 0033593219 scopus 로고    scopus 로고
    • Oxygen-regulated and transactivating domains in endothelial PAS protein 1: Comparison with hypoxia-inducible factor-1alpha
    • J.F. O'Rourke, Y.M. Tian, P.J. Ratcliffe, and C.W. Pugh Oxygen-regulated and transactivating domains in endothelial PAS protein 1: comparison with hypoxia-inducible factor-1alpha J. Biol. Chem. 274 1999 2060 2071
    • (1999) J. Biol. Chem. , vol.274 , pp. 2060-2071
    • O'Rourke, J.F.1    Tian, Y.M.2    Ratcliffe, P.J.3    Pugh, C.W.4
  • 6
  • 7
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit
    • L.E. Huang, Z. Arany, D.M. Livingston, and H.F. Bunn Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit J. Biol. Chem. 271 1996 32253 32259
    • (1996) J. Biol. Chem. , vol.271 , pp. 32253-32259
    • Huang, L.E.1    Arany, Z.2    Livingston, D.M.3    Bunn, H.F.4
  • 8
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
    • S. Salceda, and J. Caro Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes J. Biol. Chem. 272 1997 22642 22647
    • (1997) J. Biol. Chem. , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 9
    • 0032493368 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway
    • L.E. Huang, J. Gu, M. Schau, and H.F. Bunn Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway Proc. Natl. Acad. Sci. USA 95 1998 7987 7992
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7987-7992
    • Huang, L.E.1    Gu, J.2    Schau, M.3    Bunn, H.F.4
  • 10
    • 0033525830 scopus 로고    scopus 로고
    • Regulation of the hypoxia-inducible transcription factor 1alpha by the ubiquitin-proteasome pathway
    • P.J. Kallio, W.J. Wilson, S. O'Brien, Y. Makino, and L. Poellinger Regulation of the hypoxia-inducible transcription factor 1alpha by the ubiquitin-proteasome pathway J. Biol. Chem. 274 1999 6519 6525
    • (1999) J. Biol. Chem. , vol.274 , pp. 6519-6525
    • Kallio, P.J.1    Wilson, W.J.2    O'Brien, S.3    Makino, Y.4    Poellinger, L.5
  • 12
  • 17
    • 0033986948 scopus 로고    scopus 로고
    • Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1α
    • P. Carrero, K. Okamato, P. Coumailleau, S. O'Brien, H. Tanaka, and L. Poellinger Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1α Mol. Cell. Biol. 20 2000 402 415
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 402-415
    • Carrero, P.1    Okamato, K.2    Coumailleau, P.3    O'Brien, S.4    Tanaka, H.5    Poellinger, L.6
  • 18
    • 0033118983 scopus 로고    scopus 로고
    • Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: Their stabilization and redox signal-induced interaction with CBP/p300
    • M. Ema, K. Hirota, J. Mimura, H. Abe, J. Yodoi, K. Sogawa, L. Poellinger, and Y. Fujii-Kuriyama Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300 EMBO J. 18 1999 1905 1914
    • (1999) EMBO J. , vol.18 , pp. 1905-1914
    • Ema, M.1    Hirota, K.2    Mimura, J.3    Abe, H.4    Yodoi, J.5    Sogawa, K.6    Poellinger, L.7    Fujii-Kuriyama, Y.8
  • 19
    • 0035793584 scopus 로고    scopus 로고
    • Molecular mechanism of hypoxia-inducible factor 1-p300 interaction
    • J. Gu, J. Milligan, and L.E. Huang Molecular mechanism of hypoxia-inducible factor 1-p300 interaction J. Biol. Chem. 276 2001 3550 3554
    • (2001) J. Biol. Chem. , vol.276 , pp. 3550-3554
    • Gu, J.1    Milligan, J.2    Huang, L.E.3
  • 20
    • 0034529914 scopus 로고    scopus 로고
    • Suppression of tumor growth through disruption of hypoxia-inducible transcription
    • A.L. Kung, S. Wang, J.M. Klco, W.G. Kaelin, and D.M. Livingston Suppression of tumor growth through disruption of hypoxia-inducible transcription Nat. Med. 6 2000 1335
    • (2000) Nat. Med. , vol.6 , pp. 1335
    • Kung, A.L.1    Wang, S.2    Klco, J.M.3    Kaelin, W.G.4    Livingston, D.M.5
  • 21
    • 0035313697 scopus 로고    scopus 로고
    • HIF-1 and mechanisms of hypoxia sensing
    • G.L. Semenza HIF-1 and mechanisms of hypoxia sensing Curr. Opin. Cell Biol. 13 2001 167 171
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 167-171
    • Semenza, G.L.1
  • 22
    • 0024273450 scopus 로고
    • Regulation of the erythropoietin gene: Evidence that the oxygen sensor is a heme protein
    • M.A. Goldberg, S.P. Dunning, and H.F. Bunn Regulation of the erythropoietin gene: evidence that the oxygen sensor is a heme protein Science 242 1988 1412 1415
    • (1988) Science , vol.242 , pp. 1412-1415
    • Goldberg, M.A.1    Dunning, S.P.2    Bunn, H.F.3
  • 23
    • 0035859692 scopus 로고    scopus 로고
    • HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation
    • F. Yu, S.B. White, and F.S. Lee HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation Proc. Natl. Acad. Sci. USA 98 2001 9630 9635
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9630-9635
    • Yu, F.1    White, S.B.2    Lee, F.S.3
  • 25
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1α-pVHL complex: Hydroxyproline recognition in signaling
    • J.-H. Min, H. Yang, M. Ivan, F. Gertler, W.G. Kaelin Jr., and N. Pavletich Structure of an HIF-1α-pVHL complex: hydroxyproline recognition in signaling Science 296 2002 1886 1889
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.-H.1    Yang, H.2    Ivan, M.3    Gertler, F.4    Kaelin Jr., W.G.5    Pavletich, N.6
  • 26
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain: A hypoxic switch
    • D. Lando, D.J. Peet, D.A. Whelan, J.J. Gorman, and M.L. Whitelaw Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch Science 295 2002 858 861
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 27
    • 0031616949 scopus 로고    scopus 로고
    • Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases
    • D.L. Purich Wiley New York
    • K.I. Kivirikko, and T. Pihlajaniemi Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases D.L. Purich Advances in Enzymology and Related Areas of Molecular Biology 1998 Wiley New York 325 398
    • (1998) Advances in Enzymology and Related Areas of Molecular Biology , pp. 325-398
    • Kivirikko, K.I.1    Pihlajaniemi, T.2
  • 28
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • R.K. Bruick, and S.L. McKnight A conserved family of prolyl-4- hydroxylases that modify HIF Science 294 2001 1337 1340
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 31
    • 0242330181 scopus 로고    scopus 로고
    • Oxygen sensing in the hypoxic response pathway: Regulation of the hypoxia-inducible transcription factor
    • R.K. Bruick Oxygen sensing in the hypoxic response pathway: regulation of the hypoxia-inducible transcription factor Genes Dev. 17 2003 2614 2623
    • (2003) Genes Dev. , vol.17 , pp. 2614-2623
    • Bruick, R.K.1
  • 33
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • D. Lando, D.J. Peet, J.J. Gorman, D.A. Whelan, M.L. Whitelaw, and R.K. Bruick FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor Genes Dev. 16 2002 1466 1471
    • (2002) Genes Dev. , vol.16 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3    Whelan, D.A.4    Whitelaw, M.L.5    Bruick, R.K.6
  • 34
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity
    • P.C. Mahon, K. Hirota, and G.L. Semenza FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity Genes Dev. 15 2001 2675 2686
    • (2001) Genes Dev. , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 35
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia
    • E. Berra, E. Benizri, A. Ginouvès, V. Volmat, D. Roux, and J. Pouysségur HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia EMBO J. 22 2003 4082 4090
    • (2003) EMBO J. , vol.22 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouvès, A.3    Volmat, V.4    Roux, D.5    Pouysségur, J.6
  • 36
    • 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
    • P. Koivunen, M. Hirsila, V. Gunzler, K.I. Kivirikko, and J. Myllyharju Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases J. Biol. Chem. 279 2004 9899 9904
    • (2004) J. Biol. Chem. , vol.279 , pp. 9899-9904
    • Koivunen, P.1    Hirsila, M.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 37
    • 5644240828 scopus 로고    scopus 로고
    • Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (HIF) in regulating HIF transcriptional target genes
    • I.P. Stolze, Y.M. Tian, R.J. Appelhoff, H. Turley, C.C. Wykoff, J.M. Gleadle, and P.J. Ratcliffe Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (HIF) in regulating HIF transcriptional target genes J. Biol. Chem. 279 2004 42719 42725
    • (2004) J. Biol. Chem. , 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    Ratcliffe, P.J.7
  • 40
    • 0037180452 scopus 로고    scopus 로고
    • Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway
    • C.E. Dann 3rd, R.K. Bruick, and J. Deisenhofer Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway Proc. Natl. Acad. Sci. USA 99 2002 15351 15356
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15351-15356
    • Dann III, C.E.1    Bruick, R.K.2    Deisenhofer, J.3
  • 42
    • 0037470162 scopus 로고    scopus 로고
    • Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau
    • C. Lee, S.J. Kim, D.G. Jeong, S.M. Lee, and S.E. Ryu Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau J. Biol. Chem. 278 2003 7558 7563
    • (2003) J. Biol. Chem. , vol.278 , pp. 7558-7563
    • Lee, C.1    Kim, S.J.2    Jeong, D.G.3    Lee, S.M.4    Ryu, S.E.5
  • 43
    • 0032760945 scopus 로고    scopus 로고
    • Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
    • C.J. Schofield, and Z. Zhang Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes Curr. Opin. Struct. Biol. 9 1999 722 731
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 722-731
    • Schofield, C.J.1    Zhang, Z.2
  • 44
    • 0043022281 scopus 로고    scopus 로고
    • Dioxygenase enzymes: Catalytic mechanisms and chemical models
    • T.D.H. Bugg Dioxygenase enzymes: catalytic mechanisms and chemical models Tetrahedron 59 2003 7075 7101
    • (2003) Tetrahedron , vol.59 , pp. 7075-7101
    • Bugg, T.D.H.1
  • 45
    • 2442628211 scopus 로고    scopus 로고
    • Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes
    • R.P. Hausinger Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes Crit. Rev. Biochem. Mol. Biol. 39 2004 21 68
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 21-68
    • Hausinger, R.P.1
  • 46
    • 0036846033 scopus 로고    scopus 로고
    • Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803
    • L.A. McNeill, K.S. Hewitson, T.D. Claridge, J.F. Seibel, L.E. Horsfall, and C.J. Schofield Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803 Biochem. J. 367 2002 571 575
    • (2002) Biochem. J. , vol.367 , pp. 571-575
    • McNeill, L.A.1    Hewitson, K.S.2    Claridge, T.D.3    Seibel, J.F.4    Horsfall, L.E.5    Schofield, C.J.6
  • 47
    • 0033608080 scopus 로고    scopus 로고
    • Mechanism-based inactivation of the human prolyl-4-hydroxylase by 5-oxaproline-containing peptides: Evidence for a prolyl radical intermediate
    • M. Wu, H.-S. Moon, T.P. Begley, J. Myllyharju, and K.I. Kivirikko Mechanism-based inactivation of the human prolyl-4-hydroxylase by 5-oxaproline-containing peptides: evidence for a prolyl radical intermediate J. Am. Chem. Soc. 121 1999 587 588
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 587-588
    • Wu, M.1    Moon, H.-S.2    Begley, T.P.3    Myllyharju, J.4    Kivirikko, K.I.5
  • 48
    • 0032583527 scopus 로고    scopus 로고
    • Substrate binding to the α-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: Coupling mechanism of oxidative decarboxylation and hydroxylation
    • J. Zhou, M. Gunsior, B.O. Bachman, C. Townsend, and E.I. Solomon Substrate binding to the α-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: coupling mechanism of oxidative decarboxylation and hydroxylation J. Am. Chem. Soc. 120 1998 13539 13540
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 13539-13540
    • Zhou, J.1    Gunsior, M.2    Bachman, B.O.3    Townsend, C.4    Solomon, E.I.5
  • 50
    • 0037131159 scopus 로고    scopus 로고
    • Sequence determinants in hypoxia inducible factor-1a for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3
    • J. Huang, Q. Zhao, S.M. Mooney, and F.S. Lee Sequence determinants in hypoxia inducible factor-1a for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3 J. Biol. Chem. 277 2002 39792 39800
    • (2002) J. Biol. Chem. , vol.277 , pp. 39792-39800
    • Huang, J.1    Zhao, Q.2    Mooney, S.M.3    Lee, F.S.4
  • 51
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • M. Hirsila, P. Koivunen, V. Gunzler, K.I. Kivirikko, and J. Myllyharju Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor J. Biol. Chem. 278 2003 30772 30780
    • (2003) J. Biol. Chem. , vol.278 , pp. 30772-30780
    • Hirsila, M.1    Koivunen, P.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 52
    • 1842639126 scopus 로고    scopus 로고
    • Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor
    • S. Linke, C. Stojkoski, R.J. Kewley, G.W. Booker, M.L. Whitelaw, and D.J. Peet Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor J. Biol. Chem. 279 2004 14391 14397
    • (2004) J. Biol. Chem. , vol.279 , pp. 14391-14397
    • Linke, S.1    Stojkoski, C.2    Kewley, R.J.3    Booker, G.W.4    Whitelaw, M.L.5    Peet, D.J.6
  • 55
    • 0442278330 scopus 로고    scopus 로고
    • Drosophila cyclin D/Cdk4 requires Hif-1 prolyl hydroxylase to drive cell growth
    • C. Frei, and B.A. Edgar Drosophila cyclin D/Cdk4 requires Hif-1 prolyl hydroxylase to drive cell growth Dev. Cell 6 2004 241 251
    • (2004) Dev. Cell , vol.6 , pp. 241-251
    • Frei, C.1    Edgar, B.A.2
  • 61
    • 24144447915 scopus 로고    scopus 로고
    • Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-α activation
    • K.D. Mansfield, R.D. Guzy, Y. Pan, R.M. Young, T.P. Cash, P.T. Schumacker, and M.C. Simon Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-α activation Cell Metab. 1 2005 393 399
    • (2005) Cell Metab. , vol.1 , pp. 393-399
    • Mansfield, K.D.1    Guzy, R.D.2    Pan, Y.3    Young, R.M.4    Cash, T.P.5    Schumacker, P.T.6    Simon, M.C.7
  • 63
    • 0042469448 scopus 로고    scopus 로고
    • Nitric Oxide impairs normoxic degradation of HIF-1α by inhibition of prolyl hydroxylases
    • E. Metzen, J. Zhou, W. Jelkmann, J. Fandrey, and B. Brüne Nitric Oxide impairs normoxic degradation of HIF-1α by inhibition of prolyl hydroxylases Mol. Biol. Cell 14 2003 347 3481
    • (2003) Mol. Biol. Cell , vol.14 , pp. 347-3481
    • Metzen, E.1    Zhou, J.2    Jelkmann, W.3    Fandrey, J.4    Brüne, B.5
  • 64
    • 0348134741 scopus 로고    scopus 로고
    • Redistribution of intracellular oxygen in hypoxia by nitric oxide: Effect on HIF1α
    • T. Hagen, C.T. Taylor, F. Lam, and S. Moncada Redistribution of intracellular oxygen in hypoxia by nitric oxide: effect on HIF1α Science 302 2003 1975 1978
    • (2003) Science , vol.302 , pp. 1975-1978
    • Hagen, T.1    Taylor, C.T.2    Lam, F.3    Moncada, S.4
  • 66
    • 1542300383 scopus 로고    scopus 로고
    • The von Hippel Lindau/hypoxia-inducible factor (HIF) pathway regulates the transcription of the HIF-proline hydroxylase genes in response to low oxygen
    • L. del Peso, M.C. Castellanos, E. Temes, S. Martin-Puig, Y. Cuevas, G. Olmos, and M.O. Landazuri The von Hippel Lindau/hypoxia-inducible factor (HIF) pathway regulates the transcription of the HIF-proline hydroxylase genes in response to low oxygen J. Biol. Chem. 278 2003 48690 48695
    • (2003) J. Biol. Chem. , vol.278 , pp. 48690-48695
    • Del Peso, L.1    Castellanos, M.C.2    Temes, E.3    Martin-Puig, S.4    Cuevas, Y.5    Olmos, G.6    Landazuri, M.O.7
  • 70
    • 4644260710 scopus 로고    scopus 로고
    • Depletion of intracellular ascorbate by the carcinogenic metals nickel and cobalt results in the induction of hypoxic stress
    • K. Salnikow, S.P. Donald, R.K. Bruick, A. Zhitkovich, J.M. Phang, and K.S. Kasprzak Depletion of intracellular ascorbate by the carcinogenic metals nickel and cobalt results in the induction of hypoxic stress J. Biol. Chem. 279 2004 40337 40344
    • (2004) J. Biol. Chem. , vol.279 , pp. 40337-40344
    • Salnikow, K.1    Donald, S.P.2    Bruick, R.K.3    Zhitkovich, A.4    Phang, J.M.5    Kasprzak, K.S.6
  • 71
    • 19044392200 scopus 로고    scopus 로고
    • Ascorbate depletion: A critical step in nickel carcinogenesis
    • K. Salnikow, and K.S. Kasprzak Ascorbate depletion: a critical step in nickel carcinogenesis Environ. Health Perspect. 113 2005 577 584
    • (2005) Environ. Health Perspect. , vol.113 , pp. 577-584
    • Salnikow, K.1    Kasprzak, K.S.2
  • 72
    • 0037446983 scopus 로고    scopus 로고
    • Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells
    • H.J. Knowles, R.R. Raval, A.L. Harris, and P.J. Ratcliffe Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells Cancer Res. 63 2003 1764 1768
    • (2003) Cancer Res. , vol.63 , pp. 1764-1768
    • Knowles, H.J.1    Raval, R.R.2    Harris, A.L.3    Ratcliffe, P.J.4
  • 73
    • 2642542967 scopus 로고    scopus 로고
    • Endogenous 2-oxoacids differentially regulate expression of oxygen sensors
    • C.L. Dalgard, H. Lu, A. Mohyeldin, and A. Verma Endogenous 2-oxoacids differentially regulate expression of oxygen sensors Biochem. J. 380 2004 419 424
    • (2004) Biochem. J. , vol.380 , pp. 419-424
    • Dalgard, C.L.1    Lu, H.2    Mohyeldin, A.3    Verma, A.4
  • 75
    • 13944276440 scopus 로고    scopus 로고
    • OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha
    • J.H. Baek, P.C. Mahon, J. Oh, B. Kelly, B. Krishnamachary, M. Pearson, D.A. Chan, A.J. Giaccia, and G.L. Semenza OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha Mol. Cell 17 2005 503 512
    • (2005) Mol. Cell , vol.17 , pp. 503-512
    • Baek, J.H.1    Mahon, P.C.2    Oh, J.3    Kelly, B.4    Krishnamachary, B.5    Pearson, M.6    Chan, D.A.7    Giaccia, A.J.8    Semenza, G.L.9
  • 76
    • 19644376763 scopus 로고    scopus 로고
    • The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF)
    • A. Ozer, L.C. Wu, and R.K. Bruick The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF) Proc. Natl. Acad. Sci. USA 102 2005 7481 7486
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7481-7486
    • Ozer, A.1    Wu, L.C.2    Bruick, R.K.3
  • 77
    • 0037131271 scopus 로고    scopus 로고
    • Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1α
    • D.A. Chan, P.D. Sutphin, N.C. Denko, and A.J. Giaccia Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1α J. Biol. Chem. 277 2002 40112 40117
    • (2002) J. Biol. Chem. , vol.277 , pp. 40112-40117
    • Chan, D.A.1    Sutphin, P.D.2    Denko, N.C.3    Giaccia, A.J.4
  • 79
    • 0028241545 scopus 로고
    • A fully active catalytic domain of bovine aspartyl (asparaginyl) B-hydroxylase expressed in Escherichia coli: Characterization and evidence for the identification of an active-site region in vertebrate α-ketoglutarate- dependent dioxygenases
    • S. Jia, K. McGinnis, W.J. VanDusen, C.J. Burke, A. Kuo, P.R. Griffin, M.K. Sardana, K.O. Elliston, A.M. Stern, and P.A. Friedman A fully active catalytic domain of bovine aspartyl (asparaginyl) B-hydroxylase expressed in Escherichia coli: Characterization and evidence for the identification of an active-site region in vertebrate α-ketoglutarate-dependent dioxygenases Proc. Natl. Acad. Sci. USA 91 1994 7227 7231
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7227-7231
    • Jia, S.1    McGinnis, K.2    Vandusen, W.J.3    Burke, C.J.4    Kuo, A.5    Griffin, P.R.6    Sardana, M.K.7    Elliston, K.O.8    Stern, A.M.9    Friedman, P.A.10
  • 80
    • 17644414543 scopus 로고    scopus 로고
    • The Skp1 prolyl hydroxylase from Dictyostelium is related to the hypoxia-inducible factor-a class of animal prolyl 4-hydroxylases
    • H. vander Wel, A. Ercan, and C.M. West The Skp1 prolyl hydroxylase from Dictyostelium is related to the hypoxia-inducible factor-a class of animal prolyl 4-hydroxylases J. Biol. Chem. 280 2005 14645 14655
    • (2005) J. Biol. Chem. , vol.280 , pp. 14645-14655
    • Vander Wel, H.1    Ercan, A.2    West, C.M.3
  • 81
    • 0141890273 scopus 로고    scopus 로고
    • Oxygen and iron regulation of iron regulatory protein 2
    • E.S. Hanson, M.L. Rawlins, and E.A. Leibold Oxygen and iron regulation of iron regulatory protein 2 J. Biol. Chem. 278 2003 40337 40342
    • (2003) J. Biol. Chem. , vol.278 , pp. 40337-40342
    • Hanson, E.S.1    Rawlins, M.L.2    Leibold, E.A.3
  • 82
    • 1642458415 scopus 로고    scopus 로고
    • Iron-mediated degradation of IRP2, an unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity
    • J. Wang, G. Chen, M. Muckenthaler, B. Galy, M.W. Hentze, and K. Pantopoulos Iron-mediated degradation of IRP2, an unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity Mol. Cell. Biol. 24 2004 954 965
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 954-965
    • Wang, J.1    Chen, G.2    Muckenthaler, M.3    Galy, B.4    Hentze, M.W.5    Pantopoulos, K.6
  • 83
    • 0030962028 scopus 로고    scopus 로고
    • Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase
    • J. Myllyharju, and K.I. Kivirikko Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase EMBO J. 16 1997 1173 1180
    • (1997) EMBO J. , vol.16 , pp. 1173-1180
    • Myllyharju, J.1    Kivirikko, K.I.2


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