Cannabaceae

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Hypoxia-inducible factor-proline dioxygenase
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EC no.1.14.11.29
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Hypoxia-inducible factor-proline dioxygenase (EC 1.14.11.29, HIF hydroxylase) is an enzyme with systematic name hypoxia-inducible factor-L-proline, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2

Hypoxia-inducible factor-proline dioxygenase contains iron, and requires ascorbate.

Hypoxia-inducible factor (HIF) is an evolutionarily conserved transcription factor[7] that allows the cell to respond physiologically to low concentrations of oxygen.[8] A class of prolyl hydroxylases which act specifically on HIF has been identified;[9] hydroxylation of HIF allows the protein to be targeted for degradation.[9] HIF prolyl-hydroxylase has been targeted by a variety of inhibitors that aim to treat stroke,[10] kidney disease,[11] ischemia,[12] anemia,[13] and other important diseases. Clinically observed prolyl hydroxylase domain mutations, as in the case of erythrocytosis- and breast cancer-associated PHD2 mutations, affect its selectivity for its HIF substrate, which has important implication for drug design.[14]

In humans, there are three isoforms of hypoxia-inducible factor-proline dioxygenase. These are PHD1, PHD2 and PHD3. PHD2, in particular, was identified as the most important human oxygen sensors due to its slow reaction with oxygen.[15]

References

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  1. ^ Jaakkola, P.; Mole, D.R.; Tian, Y.M.; Wilson, M.I.; Gielbert, J.; Gaskell, S.J.; Kriegsheim Av; Hebestreit, H.F.; Mukherji, M.; Schofield, C.J.; Maxwell, P.H.; Pugh, C.W.; Ratcliffe, P.J. (2001). "Targeting of HIF-α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation". Science. 292 (5516): 468–472. Bibcode:2001Sci...292..468J. doi:10.1126/science.1059796. PMID 11292861.
  2. ^ Ivan, M.; Kondo, K.; Yang, H.; Kim, W.; Valiando, J.; Ohh, M.; Salic, A.; Asara, J.M.; Lane, W.S.; Kaelin, W.G. (2001). "HIFα targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing". Science. 292 (5516): 464–468. Bibcode:2001Sci...292..464I. doi:10.1126/science.1059817. PMID 11292862.
  3. ^ Bruick, R.K.; McKnight, S.L. (2001). "A conserved family of prolyl-4-hydroxylases that modify HIF". Science. 294 (5545): 1337–1340. Bibcode:2001Sci...294.1337B. doi:10.1126/science.1066373. PMID 11598268.
  4. ^ Epstein, A.C.; 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.; Hamilton, D.L.; Jaakkola, P.; Barstead, R.; Hodgkin, J.; Maxwell, P.H.; Pugh, C.W.; Schofield, C.J.; Ratcliffe, P.J. (2001). "C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation". Cell. 107 (1): 43–54. doi:10.1016/S0092-8674(01)00507-4. PMID 11595184.
  5. ^ Oehme, F.; Ellinghaus, P.; Kolkhof, P.; Smith, T.J.; Ramakrishnan, S.; Hutter, J.; Schramm, M.; Flamme, I. (2002). "Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors". Biochem. Biophys. Res. Commun. 296 (2): 343–349. doi:10.1016/S0006-291X(02)00862-8. PMID 12163023.
  6. ^ McNeill, L.A.; Hewitson, K.S.; Gleadle, J.M.; Horsfall, L.E.; Oldham, N.J.; Maxwell, P.H.; Pugh, C.W.; Ratcliffe, P.J.; Schofield, C.J. (2002). "The use of dioxygen by HIF prolyl hydroxylase (PHD1)". Bioorg. Med. Chem. Lett. 12 (12): 1547–1550. doi:10.1016/S0960-894X(02)00219-6. PMID 12039559.
  7. ^ Bacon, N. C.; Wappner, P; O'Rourke, J. F.; Bartlett, S. M.; Shilo, B; Pugh, C. W.; Ratcliffe, P. J. (1998). "Regulation of the Drosophila bHLH-PAS protein Sima by hypoxia: Functional evidence for homology with mammalian HIF-1 alpha". Biochemical and Biophysical Research Communications. 249 (3): 811–6. doi:10.1006/bbrc.1998.9234. PMID 9731218.
  8. ^ Smith, T. G.; Robbins, P. A.; Ratcliffe, P. J. (2008). "The human side of hypoxia-inducible factor". British Journal of Haematology. 141 (3): 325–34. doi:10.1111/j.1365-2141.2008.07029.x. PMC 2408651. PMID 18410568.
  9. ^ a b Bruick, R. K. (2001). "A Conserved Family of Prolyl-4-Hydroxylases That Modify HIF". Science. 294 (5545): 1337–40. Bibcode:2001Sci...294.1337B. doi:10.1126/science.1066373. PMID 11598268.
  10. ^ Karuppagounder, S. S.; Ratan, R. R. (2012). "Hypoxia-inducible factor prolyl hydroxylase inhibition: Robust new target or another big bust for stroke therapeutics?". Journal of Cerebral Blood Flow & Metabolism. 32 (7): 1347–1361. doi:10.1038/jcbfm.2012.28. PMC 3390817. PMID 22415525.
  11. ^ Warnecke, C.; Griethe, W.; Weidemann, A.; Jurgensen, J. S.; Willam, C.; Bachmann, S.; Ivashchenko, Y.; Wagner, I.; Frei, U.; Wiesener, M.; Eckardt, K. -U. (2003). "Activation of the hypoxia-inducible factor pathway and stimulation of angiogenesis by application of prolyl hydroxylase inhibitors". The FASEB Journal. 17 (9): 1186–8. doi:10.1096/fj.02-1062fje. PMID 12709400.
  12. ^ Selvaraju, V; Parinandi, N. L.; Adluri, R. S.; Goldman, J. W.; Hussain, N; Sanchez, J. A.; Maulik, N (2013). "Molecular Mechanisms of Action and Therapeutic Uses of Pharmacological Inhibitors of HIF-Prolyl 4-Hydroxylases for Treatment of Ischemic Diseases". Antioxidants & Redox Signaling. 20 (16): 2631–2665. doi:10.1089/ars.2013.5186. PMC 4026215. PMID 23992027.
  13. ^ Muchnik, E; Kaplan, J (2011). "HIF prolyl hydroxylase inhibitors for anemia". Expert Opinion on Investigational Drugs. 20 (5): 645–56. doi:10.1517/13543784.2011.566861. PMID 21406036.
  14. ^ Chowdhury, Rasheduzzaman; Leung, Ivanhoe K. H.; Tian, Ya-Min; Abboud, Martine I.; Ge, Wei; Domene, Carmen; Cantrelle, François-Xavier; Landrieu, Isabelle; Hardy, Adam P. (2016-08-26). "Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases". Nature Communications. 7: 12673. Bibcode:2016NatCo...712673C. doi:10.1038/ncomms12673. PMC 5007464. PMID 27561929.
  15. ^ Berra E, Benizri E, Ginouvès A, Volmat V, Roux D, Pouysségur J (Aug 2003). "HIF prolylhydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia". EMBO J. 22 (16): 4082–4090. doi:10.1093/emboj/cdg392. PMC 175782. PMID 12912907.
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source: https://en.wikipedia.org/wiki/HIF_prolyl-hydroxylase

One thought on “Cannabaceae”

  1. Well, that’s interesting to know that Psilotum nudum are known as whisk ferns. Psilotum nudum is the commoner species of the two. While the P. flaccidum is a rare species and is found in the tropical islands. Both the species are usually epiphytic in habit and grow upon tree ferns. These species may also be terrestrial and grow in humus or in the crevices of the rocks.
    View the detailed Guide of Psilotum nudum: Detailed Study Of Psilotum Nudum (Whisk Fern), Classification, Anatomy, Reproduction

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