IUPHAR/BPS Guide to Pharmacology CITE
https://doi.org/10.2218/gtopdb/F278/2023.1

Haem oxygenase in GtoPdb v.2023.1



Timothy R. Billiar1, Giuseppe Cirino2, David Fulton3, Roberto Motterlini4, Andreas Papapetropoulos5 and Csaba Szabo6
  1. University of Pittsburgh, USA
  2. University of Naples-Federico II, Italy
  3. Georgia Regents University, USA
  4. University of Paris Est Creteil, France
  5. University of Athens, Greece
  6. University of Texas, USA


Abstract

Haem oxygenase (heme,hydrogen-donor:oxygen oxidoreductase (α-methene-oxidizing, hydroxylating)), E.C. 1.14.99.3, converts heme into biliverdin and carbon monoxide, utilizing NADPH as cofactor.

Contents

This is a citation summary for Haem oxygenase in the Guide to Pharmacology database (GtoPdb). It exists purely as an adjunct to the database to facilitate the recognition of citations to and from the database by citation analyzers. Readers will almost certainly want to visit the relevant sections of the database which are given here under database links.

GtoPdb is an expert-driven guide to pharmacological targets and the substances that act on them. GtoPdb is a reference work which is most usefully represented as an on-line database. As in any publication this work should be appropriately cited, and the papers it cites should also be recognized. This document provides a citation for the relevant parts of the database, and also provides a reference list for the research cited by those parts. For further details see [3].

Please note that the database version for the citations given in GtoPdb are to the most recent preceding version in which the family or its subfamilies and targets were substantially changed. The links below are to the current version. If you need to consult the cited version, rather than the most recent version, please contact the GtoPdb curators.

Database links

Haem oxygenase
https://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=278
    Enzymes
            HO1(Haem oxygenase 1)
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=1441
            HO2(Haem oxygenase 2)
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=1442

References

  1. Araujo JA, Meng L, Tward AD, Hancock WW, Zhai Y, Lee A, Ishikawa K, Iyer S, Buelow R and Busuttil RW et al.. (2003) Systemic rather than local heme oxygenase-1 overexpression improves cardiac allograft outcomes in a new transgenic mouse. J Immunol 171: 1572-80 [PMID:12874251]
  2. Araujo JA, Zhang M and Yin F. (2012) Heme oxygenase-1, oxidation, inflammation, and atherosclerosis. Front Pharmacol 3: 119 [PMID:22833723]
  3. Buneman P, Christie G, Davies JA, Dimitrellou R, Harding SD, Pawson AJ, Sharman JL and Wu Y. (2020) Why data citation isn't working, and what to do about it Database 2020 [PMID:32367113]
  4. Drummond GS and Kappas A. (1981) Prevention of neonatal hyperbilirubinemia by tin protoporphyrin IX, a potent competitive inhibitor of heme oxidation. Proc Natl Acad Sci USA 78: 6466-70 [PMID:6947237]
  5. Hayashi S, Omata Y, Sakamoto H, Higashimoto Y, Hara T, Sagara Y and Noguchi M. (2004) Characterization of rat heme oxygenase-3 gene. Implication of processed pseudogenes derived from heme oxygenase-2 gene. Gene 336: 241-50 [PMID:15246535]
  6. Romanoski CE, Che N, Yin F, Mai N, Pouldar D, Civelek M, Pan C, Lee S, Vakili L and Yang WP et al.. (2011) Network for activation of human endothelial cells by oxidized phospholipids: a critical role of heme oxygenase 1. Circ Res 109: e27-41 [PMID:21737788]
  7. Vlahakis JZ, Kinobe RT, Bowers RJ, Brien JF, Nakatsu K and Szarek WA. (2006) Imidazole-dioxolane compounds as isozyme-selective heme oxygenase inhibitors. J Med Chem 49: 4437-41 [PMID:16821802]