Hypoxia-Inducible Factor Prolyl-Hydroxylase: Purification and Assays of PHD2

Methods in Enzymology

Volumn 435, Issue , 2007, Pages 25-42

  Hewitson, Kirsty S ^a   Schofield, Christopher J ^a   Ratcliffe, Peter J ^b  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; HYPOXIA INDUCIBLE FACTOR 1ALPHA; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; SUCCINIC ACID; VON HIPPEL LINDAU PROTEIN; CARBON DIOXIDE; HYPOXIA INDUCIBLE FACTOR 1; OXYGEN; RECOMBINANT PROTEIN; SUCCINIC ACID DERIVATIVE;

BINDING ASSAY; DERIVATIZATION; ENZYME ACTIVITY; FLUORESCENCE; HYDROXYLATION; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; OXYGEN CONSUMPTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN PURIFICATION; REVIEW; STEADY STATE; ANIMAL; ARTICLE; BIOSYNTHESIS; CHEMISTRY; ESCHERICHIA COLI; GENETICS; HUMAN; ISOLATION AND PURIFICATION;

ANIMALIA;

ANIMALS; CARBON DIOXIDE; CHROMATOGRAPHY, LIQUID; ESCHERICHIA COLI; HUMANS; HYPOXIA-INDUCIBLE FACTOR 1; HYPOXIA-INDUCIBLE FACTOR 1, ALPHA SUBUNIT; MASS SPECTROMETRY; OXYGEN; OXYGEN CONSUMPTION; PROCOLLAGEN-PROLINE DIOXYGENASE; RECOMBINANT PROTEINS; SUCCINATES;

EID: 39749104199     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)35002-7     Document Type: Review

References (42)

1. Appelhoff R.J., Tian Y.M., Raval R.R., Turley H., Harris A.L., Pugh C.W., Ratcliffe P.J., and Gleadle J.M. Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. J. Biol. Chem. 279 (2004) 38458-38465
2. Bacon N.C.M., Wappner P., O'Rourke J.F., Bartlett S.M., Shilo B., Pugh C.W., and Ratcliffe P.J. Regulation of the Drosophila bHLH-PAS protein Sima by hypoxia: Functional evidence for homology with mammalian HIF-1 α. Biochem. Biophys. Res. Commun. 249 (1998) 811-816
3. Berra E., Benizri E., Ginouves A., Volmat V., Roux D., and Pouyssegur J. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1 α in normoxia. EMBO J. 22 (2003) 4082-4090
4. Bruick R.K., and McKnight S.L. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294 (2001) 1337-1340
5. Clifton I., McDonough M.A., Ehrismann D., Kershaw N.J., Granatino N., and Schofield C.J. Structural studies on 2-oxoglutarate oxygenases and related double-stranded β-helix fold proteins. J. Inorg. Biochem. 100 (2006) 644-669
6. Costas M., Mehn M.P., Jensen M.P., and Que Jr. L. Dioxygen activation at mononuclear nonheme iron active sites: Enzymes, models, and intermediates. Chem. Rev. 104 (2004) 939-986
7. Cunliffe C.J., Franklin T.J., and Gaskell R.M. Assay of prolyl 4-hydroxylase by the chromatographic determination of C-14 succinic acid on ion-exchange minicolumns. Biochem. J. 240 (1986) 617-619
8. Ehrismann D., Flashman E., Genn D.N., Mathioudakis N., Hewitson K.S., Ratcliffe P.J., and Schofield C.J. Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay. Biochem. J. 401 (2007) 227-234
9. Epstein A.C.R., Gleadle J.M., McNeill L.A., Hewitson K.S., O'Rourke J., Mole D.R., Mukherji M., Metzen E., Wilson M.I., Dhanda A., Tian Y.M., Masson N., et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107 (2001) 43-54
10. Hausinger R.P. Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes. Crit. Rev. Biochem. Mol. Biol. 39 (2004) 21-68
11. Hewitson K.S., Granatino N., Welford R.W.D., McDonough M.A., and Schofield C.J. Oxidation by 2-oxoglutarate oxygenases: Non-haem iron systems in catalysis and signalling. Philos. Transact. A Math. Phys. Eng. Sci. 363 (2005) 807-828
12. Hewitson K.S., Lienard B.M.R., McDonough M.A., Clifton I.J., Butler D., Soares A.S., Oldham N.J., McNeill L.A., and Schofield C.J. Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates. J. Biol. Chem. 282 (2007) 3293-3301
13. Hewitson K.S., McNeill L.A., Riordan M.V., Tian Y.M., Bullock A.N., Welford R.W., Elkins J.M., Oldham N.J., Bhattacharya S., Gleadle J.M., Ratcliffe P.J., Pugh C.W., 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. 277 (2002) 26351-26355
14. Hirsila M., Koivunen P., Gunzler V., Kivirikko K.I., and Myllyharju J. Characterisation of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor HIF. J. Biol. Chem. 278 (2003) 30772-30780
15. Hon W.C., Wilson M.I., Harlos K., Claridge T.D.W., Schofield C.J., Pugh C.W., Maxwell P.H., Ratcliffe P.J., Stuart D.I., and Jones E.Y. Structural basis for the recognition of hydroxyproline in HIF-1 α by pVHL. Nature 417 (2002) 975-978
16. 2 sensing. Science 292 (2001) 464-468
17. 2-regulated prolyl hydroxylation. Science 292 (2001) 468-472
18. Jiang H.Q., Guo R., and Powell-Coffman J.A. The Caenorhabditis elegans hif-1 gene encodes a bHLH-PAS protein that is required for adaptation to hypoxia. Proc. Natl. Acad. Sci. USA 98 (2001) 7916-7921
19. Lando D., Peet D.J., Whelan D.A., Gorman J.J., and Whitelaw M.L. Asparagine hydroxylation of the HIF transactivation domain: A hypoxic switch. Science 295 (2002) 858-861
20. Lavista-Llanos S., Centanin L., Irisarri M., Russo D.M., Gleadle J.M., Bocca S.N., Muzzopappa M., Ratcliffe P.J., and Wappner P. Control of the hypoxic response in Drosophila melanogaster by the basic helix-loop-helix PAS protein similar. Mol. Cell. Biol. 22 (2002) 6842-6853
21. Lieb M.E., Menzies K., Moschella M.C., Ni R., and Taubman M.B. Mammalian EGLN genes have distinct patterns of mRNA expression and regulation. Biochem. Cell. Biol. 80 (2002) 421-426
22. Lloyd M.D., Lee H.J., Harlos K., Zhang Z.H., Baldwin J.E., Schofield C.J., Charnock J.M., Garner C.D., Hara T., van Scheltinga A.C.T., Valegard K., Viklund J.A.C., et al. Studies on the active site of deacetoxycephalosporin C synthase. J. Mol. Biol. 287 (1999) 943-960
23. Masson N., Willam C., Maxwell P.H., Pugh C.W., and Ratcliffe P.J. Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation. EMBO J. 20 (2001) 5197-5206
24. McDonough M.A., Li V., Flashman E., Chowdhury R., Mohr C., Lienard B.M.R., Zondlo J., Oldham N.J., Clifton I.J., Lewis J., McNeill L.A., Kurzeja R.J.M., et al. Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2). Proc. Natl. Acad. Sci. USA 103 (2006) 9814-9819
25. McNeill L.A., Bethge L., Hewitson K.S., and Schofield C.J. A fluorescence-based assay for 2-oxoglutarate-dependent oxygenases. Anal. Biochem. 336 (2005) 125-131
26. McNeill L.A., Flashman E., Buck M.R.G., Hewitson K.S., Clifton I.J., Jeschke G., Claridge T.D.W., Ehrismann D., Oldham N.J., and Schofield C.J. Hypoxia-inducible factor prolyl-hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate. Mol. Biosyst. 1 (2005) 321-324
27. Muhling J., Fuchs M., Campos M.E., Gonter J., Engel J.M., Sablotzki A., Menges T., Weiss S., Dehne M.G., Krull M., and Hempelmann G. Quantitative determination of free intracellular α-keto acids in neutrophils. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 789 (2003) 383-392
28. Mukherji M., Chien W., Kershaw N.J., Clifton I.J., Schofield C.J., Wierzbicki A.S., and Lloyd M.D. Structure-function analysis of phytanoyl-CoA 2-hydroxylase mutations causing Refsum's disease. Hum. Mol. Genet. 10 (2001) 1971-1982
29. Myllyharju J., and Kivirikko K.I. Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl-4-hydroxylase. EMBO J. 16 (1997) 1173-1180
30. Myllyla R., Majamaa K., Gunzler V., Hanauskeabel H.M., and Kivirikko K.I. Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J. Biol. Chem. 259 (1984) 5403-5405
31. Pugh C.W., and Ratcliffe P.J. Regulation of angiogenesis by hypoxia: Role of the HIF system. Nat. Med. 9 (2003) 677-684
32. Searls T., Butler D., Chien W., Mukherji M., Lloyd M.D., and Schofield C.J. Studies on the specificity of unprocessed and mature forms of phytanoyl-CoA 2-hydroxylase and mutation of the iron binding ligands. J. Lipid Res. 46 (2005) 1660-1667
33. Semenza G.L. HIF-1 and human disease: One highly involved factor. Genes Dev. 14 (2000) 1983-1991
34. Singh B.K., Szamosi I., and Shaner D. A high-performance liquid-chromatography assay for threonine serine dehydratase. Anal. Biochem. 208 (1993) 260-263
35. Tuckerman J.R., Zhao Y.G., Hewitson K.S., Tian Y.M., Pugh C.W., Ratcliffe P.J., and Mole D.R. Determination and comparison of specific activity of the HIF-prolyl hydroxylases. FEBS Lett. 576 (2004) 145-150
36. Valegård K., van Scheltinga A.C., Lloyd M.D., Hara T., Ramaswamy S., Perrakis A., Thompson A., Lee H.J., Baldwin J.E., Schofield C.J., Hajdu J., and Andersson I. Structure of a cephalosporin synthase. Nature 394 (1998) 805-809
37. Wappner P., Irisarri M., Lavista-Llanos S., Mondotte J.A., and Centanin L. The hypoxic response in Drosophila depends on the bHLH-PAS protein similar and the prolyl-4-hydroxylase, fatiga, that operates as an oxygen sensor. Dev. Biol. 259 (2003) 520-524
38. Welford R.W.D., Schlemminger I., McNeill L.A., Hewitson K.S., and Schofield C.J. The selectivity and inhibition of AlkB. J. Biol. Chem. 278 (2003) 10157-10161
39. 2-regulated gene expression. FASEB J. 16 (2002) 1151-1162
40. Willam C., Maxwell P.H., Nichol L., Lygate C., Tian Y.-M., Bernhardt W., Wiesener M., Ratcliffe P.J., Eckardt K.U., and Pugh C.W. HIF prolyl hydroxylases in the rat; organ distribution and changes in expression following hypoxia and coronary artery ligation. J. Mol. Cell. Cardiol. 41 (2006) 68-77
41. Xu J.H., and Jordan R.B. Kinetics and mechanism of the reaction of aqueous iron(Iii) with ascorbic-acid. Inorg. Chem. 29 (1990) 4180-4184
42. Yu F., White S.B., Zhao Q., and Lee F.S. HIF-1 α binding to VHL is regulated by stimulus-sensitive proline hydroxylation. Proc. Natl. Acad. Sci. USA 98 (2001) 9630-9635