Oxygen sensing

Haematologica

Volumn 90, Issue 1, 2005, Pages 8-12

  Cockman, Matthew E ^a   Pugh, Christopher W ^a  

^a H Wellcome Bldg Molec Physiol ^*  (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ERYTHROPOIETIN; HYPOXIA INDUCIBLE FACTOR 1; OXYGEN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; VON HIPPEL LINDAU PROTEIN;

ALLELE; EDITORIAL; GENE MUTATION; GENETIC DISORDER; HUMAN; HUMAN CELL; HYPOXIA; KIDNEY CELL; LIVER CELL; NONHUMAN; OXYGEN SENSING; PROTEIN DEGRADATION; PROTEIN DOMAIN; SIGNAL TRANSDUCTION; TISSUE OXYGENATION; VON HIPPEL LINDAU DISEASE;

ANAEROBIOSIS; ANOXIA; DIOXYGENASES; GENE EXPRESSION; HUMANS; OXYGEN CONSUMPTION; PROTEIN BINDING;

EID: 13244249909     PISSN: 03906078     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Editorial

References (79)

1. Pugh CW, Ratcliffe PJ. The von Hippel-Lindau tumor suppressor, hypoxia-inducible factor-1 (HIF-1) degradation, and cancer pathogenesis. Semin Cancer Biol 2003; 13:83-9.
2. Jelkmann W. Erythropoietin: structure, control of production, and function. Physiol Rev 1992;72:449-89.
3. Goldberg MA, Glass GA, Cunningham JM, Bunn HF. The regulated expression of erythropoietin by two human hepatoma cell lines. Proc Natl Acad Sci USA 1987;84:7972-6.
4. Beck I, Ramirez S, Weinmann R, Caro J. Enhancer element at the 3′-flanking region controls transcriptional response to hypoxia in the human erythropoietin gene. J Biol Chem 1991;266:15563-6.
5. Pugh CW, Tan CC, Jones RW, Ratcliffe PJ. Functional analysis of an oxygen-regulated transcriptional enhancer lying 3′ to the mouse erythropoietin gene. Proc Natl Acad Sci USA 1991;88:10553-7.
6. Semenza GL, Nejfelt MK, Chi SM, Antonarakis SE. Hypoxia-inducible nuclear factors bind to an enhancer element located 3′ to the human erythropoietin gene. Proc Natl Acad Sci USA 1991;88:5680-4.
7. Wang GL, Jiang BH, Rue EA, Semenza GL. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc Natl Acad Sci USA 1995;92:5510-4.
8. Maxwell PH, Pugh CW, Ratcliffe PJ. Inducible operation of die erythropoietin 3′ enhancer in multiple cell lines: evidence for a widespread oxygen sensing mechanism. Proc Natl Acad Sci USA 1993;90:2423-7.
9. Wang GL, Semenza GL. General involvement of hypoxia-inducible factor 1 in transcriptional response to hypoxia. Proc Natl Acad Sci USA 1993;90:4304-8.
10. Firth JD, Ebert BL, Pugh CW, Ratcliffe PJ. Oxygen-regulated control elements in the phosphoglycerate kinase 1 and lactate dehydrogenase A genes: similarities with the erythropoeitin 3′ enhancer. Proc Natl Acad Sci USA 1994;91:6496-500.
11. Semenza GL. Hypoxia-inducible factor 1: master regulator of O2 homeostasis. Curr Opin Genet Dev 1998;8: 588-94.
12. Wenger RH. Cellular adaptation to hypoxia: O2-sensing protein hydroxylases, hypoxia-inducible transcription factors, and O2-regulated gene expression. FASEB J 2002;16:1151-62.
13. Arany Z, Huang LE, Eckner R, Bhattacharya S, Jiang C, Goldberg MA, et al. An essential role for p300/CBP in die cellular response to hypoxia. Proc Natl Acad Sci USA 1996;93:12969-73.
14. Tian H, McKnight SL, Russell DW. Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev 1997; 11:72-82.
15. Gu YZ, Moran SM, Hogenesch JB, Wartman L, Bradfield CA. Molecular characterization and chromosomal localization of a third α-class hypoxia inducible factor subunit, HIF3α. Gene Expression 1998;7:205-13.
16. Makino Y, Kanopka A, Wilson WJ, Tanaka H, Poellinger L. Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3 locus. J Biol Chem 2002;277:32405-8.
17. Drutel G, Kathmann M, Heron A, Schwartz JC, Arrang JM. Cloning and selective expression in brain and kidney of ARNT2 homologous to the Ah receptor nuclear translocator (ARNT). Biochem Biophys Res Commun 1996;225:333-9.
18. Hirose K, Morita M, Ema M, Mimura J, Hamada H, Fujii H, et al. cDNA cloning and tissue-specific expression of a novel basic helix-loop-helix/PAS factor (Arnt2) with close sequence similarity to the aryl hydrocarbon receptor nuclear translocator (Arnt). Mol Cell Biol 1996;16:1706-13.
19. Ikeda M, Nomura M. cDNA cloning and tissue-specific expression of a novel basic helix-loop-helix/PAS protein (BMAL1) and identification of alternatively spliced variants with alternative translation initiation site usage. Biochem Biophys Res Commun 1997;233:258-64.
20. Reyes H, Reisz-Porszasz S, Hankinson O. Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor. Science 1992;256:1193-5.
21. Pugh CW, O'Rourke JF, Nagao M, Gleadle JM, Ratcliffe PJ. Activation of hypoxia inducible factor-1; definition of regulatory domains within the α subunit. J Biol Chem 1997;272:11205-14.
22. Huang LE, Gu J, Schau M, Bunn HF. Regulation of hypoxia-inducible factor 1a is mediated by an oxygen-dependent domain via the ubiquitin-proteasome pathway. Proc Natl Acad Sci USA 1998;95:7987-92.
23. Masson N, Willam C, Maxwell PH, Pugh CW, Ratcliffe PJ. Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation. EMBO J 2001;20:5197-206.
24. Salceda S, Caro J. Hypoxia-inducible factor 1α (HIF-1α) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. J Biol Chem 1997;272:22642-7.
25. Maxwell PH, Wiesener MS, Chang GW, Clifford SC, Vaux EC, Cockman ME, et al. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 1999;399:271-5.
26. Ivan M, Kondo K, Yang H, Kim W, Valiando J, Ohh M, et al. HIFα targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science 2001;292:464-8.
27. Jaakkola P, Mole DR, Tian YM, Wilson MI, Gielbert J, Gaskell SJ, et al. Targeting of HIF-a to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 2001;292:468-72.
28. Hon WC, Wilson MI, Harlos K, Claridge TD, Schofield CJ, Push CW, et al. Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL. Nature 2002; 417:975-8.
29. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, et al. C. elegans EGL-9 and mammalian homologues define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 2001;107:43-54.
30. Schofield CJ, Zhang Z. Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes. Curr Opin Struct Biol 1999;9:722-31.
31. Lavista-Llanos S, Centanin L, Irisarri M, Russo DM, Gleadle JM, Bocca SN, et al. Control of the hypoxic reponse in Drosophila melanogaster by the basic helix-loop-helix PAS protein similar. Mol Cel Biol 2002;22: 6842-53.
32. Mahon PC, Hirota K, Semenza GL. FIH-1: a novel protein that interacts with HIF-1a and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev 2001;5:2675-86.
33. Lando D, Peet DJ, Whelan DA, German JJ, Whitelaw ML. Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch. Science 2002;295:858-61.
34. Lando D, Peet DJ, German JJ, Whelan DA, Whitelaw ML, Bruick RK. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev 2002;16:1466-71.
35. Hewitson KS, McNeill LA, Riordan MV, Tian YM, Bullock AN, Welford RW, et al. Hypoxia inducible factor (HIF) asparagine hydroxylase is identical to Factor Inhibiting HIF (FIH) and is related to the cupin structural family. J Biol Chem 2002;277:26351-5.
36. Elkins JM, Hewitson KS, McNeill LA, Seibel JF, Schlemminger I, Pugh C, et al. Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1α. J Biol Chem 2003; 278:1802-6.
37. Richard DE, Berra E, Gothie E, Roux D, Pouyssegur J. p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1α (HIF-1α) and enhance the transcriptional activity of HIF-1α. J Biol Chem 1999;274:32631-7.
38. Jeong JW, Bae MK, Ahn MY, Kim SH, Sohn TK, Bae M, et al. Regulation and destabilization of HIF-1α by ARD1-mediated acetylation. Cell 2002;111:709-20.
39. Thrash-Bingham CA, Tartof KD. αHIF: a natural antisense transcript overexpressed in human renal cancer and during hypoxia. J Natl Cancer Inst 1999;91:143-51.
40. Makino Y, Cao R, Svensson K, Bertilsson G, Asman M, Tanaka H, et al. Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression. Nature 2001;414:550-4.
41. Bhattacharya S, Michels CL, Leung MK, Arany ZP, Kung AL, Livingston DM. Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1. Genes Dev 1999;13:64-75.
42. Metzen E, Berchner-Pfannschmidt U, Stengel P, Marxsen JH, Stolze I, Klinger M, et al. Intracellular localisation of human HIF-1α hydroylases: implications for oxygen sensing. J Cell Sci 2003;116:1319-26.
43. Appelhoff RJ, Tian YM, Raval RR, Turley H, Harris AL, Pugh CW, et al. Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. J Biol Chem 2004;279: 38458-65.
44. Seth P, Krop I, Porter D, Polyak K. Novel estrogen and tamoxifen induced genes identified by SAGE (serial analysis of gene expression). Oncogene 2002;21:836-43.
45. Nakayama K, Frew IJ, Hagensen M, Skals M, Habelhah H, Bhoumik A, et al. Siah2 regulates stability of prolyl-hydroxylases, controls HIF1a abundance, and modulates physiological responses to hypoxia. Cell 2004; 117:941-52.
46. Knowles HJ, Raval RR, Harris AL, Ratcliffe PJ. Effect of ascorbate on the activity of hypoxia inducible factor (HIF) in cancer cells. Cancer Res 2003;63:1764-8.
47. Astuti D, Latif F, Dallol A, Dahia PL, Douglas F, George E, et al. Gene mutations in the succinate dehydrogenase subunit SDHB cause susceptibility to familial pheochromocytoma and to familial paraganglioma. Am J Hum Genet 2001;69:49-54.
48. Alam NA, Rowan AJ, Wortham NC, Pollard PJ, Mitchell M, Tyrer JP, et al. Genetic and functional analyses of FH mutations in multiple cutaneous and uterine leiomyomatosis, heritary leiomyomatosis and renal cancer, and fumarate hydratase deficiency. Hum Mol Genet 2003;12:1241-52.
49. Wang GL, Jiang BH, Semenza GL. Effect of altered redox states on expression and DNA-binding activity of hypoxia-inducible factor 1. Biochem Biophys Res Commun 1995;212:550-6.
50. Srinivas V, Zhang LP, Zhu XH, Caro J. Characterization of an oxygen/redox-dependent degradation domain of hypoxia-inducible factor α (HIF-α) proteins. Biochem Biophys Res Commun 1999;260:557-61.
51. Shatrov VA, Sumbayev W, Zhou J, Brune B. Oxidized low-density lipoprotein (oxLDL) triggers hypoxia-inducible factor-1αa (HIF-1α) accumulation via redox-dependent mechanisms. Blood 2003;101:4847-9.
52. Palmer LA, Gaston B, Johns RA. Normoxic stabilization of hypoxia-inducible factor-1 expression and activity: redox-dependent effect of nitrogen oxides. Mol Pharmacol 2000;58:1197-203.
53. Huang LE, Arany Z, Livingston DM, Bunn HF. Activation of hypoxia-inducible transcription factor depends primarily on redox-sensitive stabilization of its a subunit. J Biol Chem 1996;271:32253-9.
54. Lando D, Pongratz I, Poellinger L, Whitelaw ML. A redox mechanism controls differential DNA binding activities of hypoxia-inducible factor (HIF) 1α and the HIF-like factor. J Biol Chem 2000;275:4618-27.
55. Huang LE, Willmore WG, Gu J, Goldberg MA, Bunn HF. Inhibition of hypoxia-inducible factor 1 activation by carbon monoxide and nitric oxide. J Biol Chem 1999;274:9038-44.
56. Metzen E, Zhou J, Jelkmann W, Fandrey J, Brune B. Nitric oxide impairs normoxic degradation of HIF-1a by inhibition of prolyl hydroxylases. Mol Biol Cell 2003;14:3470-81.
57. Sogawa K, Numayama-Tsuruta K, Ema M, Abe M, Abe H, Fujii-Kuriyama Y. Inhibition of hypoxia-inducible factor 1 activity by nitric oxide donors in hypoxia. Proc Natl Acad Sci USA 1998;95:7368-73.
58. Wang F, Sekine H, Kikuchi Y, Takasaki C, Miura C, Heiwa O, et al. HIF-1a-prolyl hydroxylase: molecular target of nitric oxide in the hypoxic signal transduction pathway. Biochem Biophys Res Commun 2002;295: 657-62.
59. Taylor CT, Furuta GT, Synnestvedt K, Colgan SP. Phosphorylation-dependent targeting of cAMP response element binding protein to the ubiquitin/proteasome pathway in hypoxia. Proc Natl Acad Sci USA 2000; 97:12091-6.
60. Koumenis C, Naczki C, Koritzinsky M, Rastani S, Diehl A, Sonenberg N, et al. Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2a. Mol Cell Biol 2002;22:7405-16.
61. Lopez-Barneo J, Pardal R, Ortega-Saenz P. Cellular mechanism of oxygen sensing. Annu Rev Physiol 2001; 63:259-87.
62. Hanson ES, Rawlins ML, Leibold EA. Oxygen and iron regulation of iron regulatory protein 2. J Biol Chem 2003;278:40337-42.
63. Rechsteiner M, Rogers SW. PEST sequences and regulation by oroteolysis. Trends Biol Sci 1996;21:267-71.
64. Warnecke C, Griethe W, Weidemann A, Jurgensen JS, Willam C, Bachmann S, et al. Activation of the hypoxia-inducible factor-pathway and stimulation of angiogenesis by application of prolyl hydroxylase inhibitors. FASEB J 2003;17:1186-8.
65. Milkiewicz M, Pugh CW, Egginton S. Inhibition of endogenous HIF inactivation induces angiogenesis in ischaemic skeletal muscles of mice. J Physiol 2004;560: 21-6.
66. Imai K. Hemoglobin Chesapeake (92a, arginine-leucine). Precise measurements and analyses of oxygen equilibrium. J Biol Chem 1974;249:7607-12.
67. de la Chapelle A, Traskelin AL, Juvonen E. Truncated erythropoietin receptor causes dominantly inherited benign human erythrocytosis. Proc Natl Acad Sci USA 1993;90:4495-9.
68. Kaelin WG, Maher ER. The VHL tumour-suppressor gene paradigm. Trend Gen 1998;14:423-6.
69. Beroud C, Joly D, Gallou C, Staroz F, Orfanelli MT, Junien C. Software and database for the analysis of mutations in the VHL gene. Nucleic Acids Res 1998; 26:256-8.
70. Neumann HPH, Bender BU. Genotype-phenotype correlations in von Hippel-Lindau disease. J Int Med 1998; 243:541-5.
71. Bishop T, Lau KW, Epstein AC, Kim SK, Jiang M, O'Rourke D, et al. Genetic analysis of pathways regulated by the von Hippel-Lindau tumor suppressor in Caenorhabditis elegans. PLoS Biol 2004;2:1549-60.
72. Clifford SC, Cockman ME, Smallwood AC, Mole DR, Woodward ER, Maxwell PH, et al. Contrasting effects on HIF-1α regulation by disease-causing pVHL mutations correlate with patterns of tumourigenesis in von Hippel-Lindau disease. Hum Mol Genet 2001;10:1029-38.
73. Hoffman MA, Ohh M, Yang H, Klco JM, Ivan M, Kaelin WG Jr. von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF. Hum Mol Genet 2001;10:1019-27.
74. Ang SO, Chen H, Hirota K, Gordeuk VR, Jelinek J, Guan Y, et al. Disruption of oxygen homeostasis underlies congenital Chuvash polycythemia. Nat Gen 2002; 32:614-21.
75. Percy MJ, McMullin MF, Jowitt SN, Potter M, Treacy M, Watson WH, et al. Chuvash-type congenital polycythemia in 4 families of Asian and Western European ancestry. Blood 2003;102:1097-9.
76. Cario H, Schwarz K, Jorch N, Kyank U, Petrides PE, Schneider DT, et al. Mutations in the von-Hippel-Lindau (VHL) tumor suppressor gene and VHL-haplotype analysis in patients with presumable congenital erythrocytosis. Haematologica 2005;90:19-24.
77. Bento MC, Chang KT, Guan YL, Liu E, Caldas G, Gatti RA, et al. Congenital polycythemia with homozygous and heterozygous mutations of von Hippel-Lindau VHL gene: five new Caucasian patients. Haematologica 2005;90:128-9.
78. Gordeuk VR, Stockton DW, Prchal JT. Congenital polycythemias/ erythrocytoses. Haematologica 2005;90: 109-16.
79. Mejia OM, Prchal JT, León-Velarde F, Hurtado A, Stockton DW. Genetic association analysis of chronic mountain sickness in an Andean high-altitude population. Haematologica 2005;90:13-8.