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Volumn 436, Issue 2, 2011, Pages 363-369

Biochemical characterization of human HIF hydroxylases using HIF protein substrates that contain all three hydroxylation sites

Author keywords

C terminal transactivation domain (CAD); Hypoxia response element; Hypoxia inducible factor (HIF); Prolyl hydroxylase domain (PHD); Substrate selectivity

Indexed keywords

HYPOXIA INDUCIBLE FACTOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; HYPOXIA INDUCIBLE FACTOR HYDROXYLASE; OXYGENASE; PROLINE; UNCLASSIFIED DRUG;

EID: 79955990630     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101201     Document Type: Article
Times cited : (31)

References (28)
  • 1
    • 45749089370 scopus 로고    scopus 로고
    • The human oxygen sensing machinery and its manipulation
    • Chowdhury, R., Hardy, A. and Schofield, C. J. (2008) The human oxygen sensing machinery and its manipulation. Chem. Soc. Rev. 37, 1308-1319
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1308-1319
    • Chowdhury, R.1    Hardy, A.2    Schofield, C.J.3
  • 2
    • 24344488419 scopus 로고    scopus 로고
    • The HIF pathway in cancer
    • Maxwell, P. H. (2005) The HIF pathway in cancer. Semin. Cell Dev. Biol. 16, 523-530
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 523-530
    • Maxwell, P.H.1
  • 3
    • 0035812772 scopus 로고    scopus 로고
    • 2, and the 3 PHDs: How animal cells signal hypoxia to the nucleus
    • 2, and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell 107, 1-3
    • (2001) Cell , vol.107 , pp. 1-3
    • Semenza, G.L.1
  • 4
    • 33846883294 scopus 로고    scopus 로고
    • New agents that stimulate erythropoiesis
    • Bunn, H. F. (2007) New agents that stimulate erythropoiesis. Blood 109, 868-873
    • (2007) Blood , vol.109 , pp. 868-873
    • Bunn, H.F.1
  • 5
    • 20844431565 scopus 로고    scopus 로고
    • Targeting hypoxia-inducible factor (HIF) as a therapeutic strategy for CNS disorders
    • Freeman, R. S. and Barone, M. C. (2005) Targeting hypoxia-inducible factor (HIF) as a therapeutic strategy for CNS disorders. Curr. Drug Targets CNS Neurol. Disord. 4, 85-92
    • (2005) Curr. Drug Targets CNS Neurol. Disord. , vol.4 , pp. 85-92
    • Freeman, R.S.1    Barone, M.C.2
  • 6
    • 4043119692 scopus 로고    scopus 로고
    • The HIF pathway as a therapeutic target
    • DOI 10.1016/S1359-6446(04)03202-7, PII S1359644604032027
    • Hewitson, K. S. and Schofield, C. J. (2004) The HIF pathway as a therapeutic target. Drug Discovery Today 9, 704-711 (Pubitemid 39070283)
    • (2004) Drug Discovery Today , vol.9 , Issue.16 , pp. 704-711
    • Hewitson, K.S.1    Schofield, C.J.2
  • 7
    • 70649104691 scopus 로고    scopus 로고
    • The hypoxia-inducible factor (HIF) pathway as a target for prevention and treatment of clinical manifestations
    • Kietzmann, T. (2009) The hypoxia-inducible factor (HIF) pathway as a target for prevention and treatment of clinical manifestations. Curr. Pharm. Des 15, 3837-3838
    • (2009) Curr. Pharm. Des , vol.15 , pp. 3837-3838
    • Kietzmann, T.1
  • 8
    • 59749096845 scopus 로고    scopus 로고
    • Prolyl hydroxylases as regulators of cell metabolism
    • Boulahbel, H., Duran, R. V. and Gottlieb, E. (2009) Prolyl hydroxylases as regulators of cell metabolism. Biochem. Soc. Trans. 37, 291-294
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 291-294
    • Boulahbel, H.1    Duran, R.V.2    Gottlieb, E.3
  • 9
    • 50649120554 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets
    • Myllyharju, J. (2008) Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets. Ann. Med. 40, 402-417
    • (2008) Ann. Med. , vol.40 , pp. 402-417
    • Myllyharju, J.1
  • 10
    • 33847050240 scopus 로고    scopus 로고
    • Non-heme dioxygenases: Cellular sensors and regulators jelly rolled into one?
    • Ozer, A. and Bruick, R. K. (2007) Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one? Nat. Chem. Biol. 3, 144-153
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 144-153
    • Ozer, A.1    Bruick, R.K.2
  • 11
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick, R. K. and McKnight, S. L. (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
  • 12
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • Hirsila, M., Koivunen, P., Gunzler, V., Kivirikko, K. I. and Myllyharju, J. (2003) Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor. J. Biol. Chem. 278, 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
  • 13
    • 0037131159 scopus 로고    scopus 로고
    • Sequence determinants in hypoxia-inducible factor-1α for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3
    • DOI 10.1074/jbc.M206955200
    • Huang, J., Zhao, Q., Mooney, S. M. and Lee, F. S. (2002) Sequence determinants in hypoxia-inducible factor-1α for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3. J. Biol. Chem. 277, 39792-39800 (Pubitemid 35190963)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39792-39800
    • Huang, J.1    Zhao, Q.2    Mooney, S.M.3    Lee, F.S.4
  • 14
    • 33846315497 scopus 로고    scopus 로고
    • Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay
    • DOI 10.1042/BJ20061151
    • Ehrismann, D., Flashman, E., Genn, D. N., Mathioudakis, N., Hewitson, K. S., Ratcliffe, P. J. and Schofield, C. J. (2007) Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay. Biochem. J. 401, 227-234 (Pubitemid 46114616)
    • (2007) Biochemical Journal , vol.401 , Issue.1 , pp. 227-234
    • Ehrismann, D.1    Flashman, E.2    Genn, D.N.3    Mathioudakis, N.4    Hewitson, K.S.5    Ratcliffe, P.J.6    Schofield, C.J.7
  • 15
    • 42949162752 scopus 로고    scopus 로고
    • Kinetic rationale for selectivity toward N- and C-terminal oxygen-dependent degradation domain substrates mediated by a loop region of hypoxia-inducible factor prolyl hydroxylases
    • Flashman, E., Bagg, E. A., Chowdhury, R., Mecinovic, J., Loenarz, C., McDonough, M. A., Hewitson, K. S. and Schofield, C. J. (2008) Kinetic rationale for selectivity toward N- and C-terminal oxygen-dependent degradation domain substrates mediated by a loop region of hypoxia-inducible factor prolyl hydroxylases. J. Biol. Chem. 283, 3808-3815
    • (2008) J. Biol. Chem. , vol.283 , pp. 3808-3815
    • Flashman, E.1    Bagg, E.A.2    Chowdhury, R.3    Mecinovic, J.4    Loenarz, C.5    McDonough, M.A.6    Hewitson, K.S.7    Schofield, C.J.8
  • 16
    • 33749410367 scopus 로고    scopus 로고
    • The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases
    • Koivunen, P., Hirsila, M., Kivirikko, K. I. and Myllyharju, J. (2006) The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases. J. Biol. Chem. 281, 28712-28720
    • (2006) J. Biol. Chem. , vol.281 , pp. 28712-28720
    • Koivunen, P.1    Hirsila, M.2    Kivirikko, K.I.3    Myllyharju, J.4
  • 17
    • 11244279649 scopus 로고    scopus 로고
    • Many amino acid substitutions in a hypoxia-inducible transcription factor (HIF)-1α-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: Substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation
    • Li, D., Hirsila, M., Koivunen, P., Brenner, M. C., Xu, L., Yang, C., Kivirikko, K. I. and Myllyharju, J. (2004) Many amino acid substitutions in a hypoxia-inducible transcription factor (HIF)-1α-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation. J. Biol. Chem. 279, 55051-55059
    • (2004) J. Biol. Chem. , vol.279 , pp. 55051-55059
    • Li, D.1    Hirsila, M.2    Koivunen, P.3    Brenner, M.C.4    Xu, L.5    Yang, C.6    Kivirikko, K.I.7    Myllyharju, J.8
  • 18
    • 1842639126 scopus 로고    scopus 로고
    • Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor
    • Linke, S., Stojkoski, C., Kewley, R. J., Booker, G. W., Whitelaw, M. L. and Peet, D. J. (2004) Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor. J. Biol. Chem. 279, 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
  • 19
    • 38449095460 scopus 로고    scopus 로고
    • Enzyme substrate recognition in oxygen sensing: How the HIF trap snaps
    • Metzen, E. (2007) Enzyme substrate recognition in oxygen sensing: how the HIF trap snaps. Biochem. J. 408, e5-e6
    • (2007) Biochem. J. , vol.408
    • Metzen, E.1
  • 20
    • 36749095315 scopus 로고    scopus 로고
    • Identification of a region on hypoxia-inducible-factor prolyl 4-hydroxylases that determines their specificity for the oxygen degradation domains
    • Villar, D., Vara-Vega, A., Landazuri, M. O. and Del, P. L. (2007) Identification of a region on hypoxia-inducible-factor prolyl 4-hydroxylases that determines their specificity for the oxygen degradation domains. Biochem. J. 408, 231-240
    • (2007) Biochem. J. , vol.408 , pp. 231-240
    • Villar, D.1    Vara-Vega, A.2    Landazuri, M.O.3    Del, P.L.4
  • 23
    • 22544464403 scopus 로고    scopus 로고
    • Coordinate regulation of the oxygen-dependent degradation domains of hypoxia-inducible factor 1 α
    • Chan, D. A., Sutphin, P. D., Yen, S. E. and Giaccia, A. J. (2005) Coordinate regulation of the oxygen-dependent degradation domains of hypoxia-inducible factor 1 α. Mol. Cell. Biol. 25, 6415-6426
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6415-6426
    • Chan, D.A.1    Sutphin, P.D.2    Yen, S.E.3    Giaccia, A.J.4
  • 25
    • 34047255064 scopus 로고    scopus 로고
    • Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates
    • Hewitson, K. S., Lienard, B. M., McDonough, M. A., Clifton, I. J., Butler, D., Soares, A. S., Oldham, N. J., McNeill, L. A. and Schofield, C. J. (2007) Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates. J. Biol. Chem. 282, 3293-3301
    • (2007) J. Biol. Chem. , vol.282 , pp. 3293-3301
    • Hewitson, K.S.1    Lienard, B.M.2    McDonough, M.A.3    Clifton, I.J.4    Butler, D.5    Soares, A.S.6    Oldham, N.J.7    McNeill, L.A.8    Schofield, C.J.9
  • 26
    • 33947520506 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: Possible links between cell metabolism and stabilization of HIF
    • Koivunen, P., Hirsila, M., Remes, A. M., Hassinen, I. E., Kivirikko, K. I. and Myllyharju, J. (2007) Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF. J. Biol. Chem. 282, 4524-4532
    • (2007) J. Biol. Chem. , vol.282 , pp. 4524-4532
    • Koivunen, P.1    Hirsila, M.2    Remes, A.M.3    Hassinen, I.E.4    Kivirikko, K.I.5    Myllyharju, J.6
  • 27
    • 34547733023 scopus 로고    scopus 로고
    • The latest advances in kidney diseases and related disorders
    • Cases, A. (2007) The latest advances in kidney diseases and related disorders. Drug News Perspect. 20, 647-654
    • (2007) Drug News Perspect. , vol.20 , pp. 647-654
    • Cases, A.1
  • 28
    • 34548829081 scopus 로고    scopus 로고
    • HIF-prolyl hydroxylase inhibition results in endogenous erythropoietin induction, erythrocytosis, and modest fetal hemoglobin expression in rhesus macaques
    • DOI 10.1182/blood-2007-02-073254
    • Hsieh, M. M., Linde, N. S., Wynter, A., Metzger, M., Wong, C., Langsetmo, I., Lin, A., Smith, R., Rodgers, G. P., Donahue, R. E. et al. (2007) HIF prolyl hydroxylase inhibition results in endogenous erythropoietin induction, erythrocytosis, and modest fetal hemoglobin expression in rhesus macaques. Blood 110, 2140-2147 (Pubitemid 47443933)
    • (2007) Blood , vol.110 , Issue.6 , pp. 2140-2147
    • Hsieh, M.M.1    Linde, N.S.2    Wynter, A.3    Metzger, M.4    Wong, C.5    Langsetmo, I.6    Lin, A.7    Smith, R.8    Rodgers, G.P.9    Donahue, R.E.10    Klaus, S.J.11    Tisdale, J.F.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.