HMOX2

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Heme oxygenase (decycling) 2
PDB rendering based on 2q32.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols HMOX2 ; HO-2
External IDs Template:OMIM5 Template:MGI HomoloGene: 1611
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Heme oxygenase (decycling) 2, also known as HMOX2, is a human gene.[1]

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: HMOX2 heme oxygenase (decycling) 2".

Further reading

  • Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr. (2007). "Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2". J Biol Chem. 282 (52): 37624–31. PMID 17965015.
  • Barañano DE, Snyder SH (2001). "Neural roles for heme oxygenase: contrasts to nitric oxide synthase". Proc. Natl. Acad. Sci. U.S.A. 98 (20): 10996–1002. doi:10.1073/pnas.191351298. PMID 11572959.
  • Doré S (2002). "Decreased activity of the antioxidant heme oxygenase enzyme: implications in ischemia and in Alzheimer's disease". Free Radic. Biol. Med. 32 (12): 1276–82. PMID 12057765.
  • Kemp PJ (2005). "Hemeoxygenase-2 as an O2 sensor in K+ channel-dependent chemotransduction". Biochem. Biophys. Res. Commun. 338 (1): 648–52. doi:10.1016/j.bbrc.2005.08.110. PMID 16137652.
  • McCoubrey WK, Ewing JF, Maines MD (1992). "Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal". Arch. Biochem. Biophys. 295 (1): 13–20. PMID 1575508.
  • Ishikawa K, Takeuchi N, Takahashi S; et al. (1995). "Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2". J. Biol. Chem. 270 (11): 6345–50. PMID 7890772.
  • Kutty RK, Kutty G, Rodriguez IR; et al. (1994). "Chromosomal localization of the human heme oxygenase genes: heme oxygenase-1 (HMOX1) maps to chromosome 22q12 and heme oxygenase-2 (HMOX2) maps to chromosome 16p13.3". Genomics. 20 (3): 513–6. doi:10.1006/geno.1994.1213. PMID 8034330.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Takahashi K, Hara E, Suzuki H; et al. (1996). "Expression of heme oxygenase isozyme mRNAs in the human brain and induction of heme oxygenase-1 by nitric oxide donors". J. Neurochem. 67 (2): 482–9. PMID 8764571.
  • Saito-Ohara F, Ikeuchi T, Matsumoto M, Kurata S (1997). "Assignment of the mouse heme oxygenase genes: heme oxygenase-1 (Hmox1) to chromosome 10 band C1 and heme oxygenase-2 (Hmox2) to chromosome 16 band B1". Cytogenet. Cell Genet. 77 (3–4): 180–1. PMID 9284910.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
  • Yoshiki N, Kubota T, Aso T (2000). "Expression and localization of heme oxygenase in human placental villi". Biochem. Biophys. Res. Commun. 276 (3): 1136–42. doi:10.1006/bbrc.2000.3551. PMID 11027601.
  • Hanselmann C, Mauch C, Werner S (2001). "Haem oxygenase-1: a novel player in cutaneous wound repair and psoriasis?". Biochem. J. 353 (Pt 3): 459–66. PMID 11171041.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Appleton SD, Marks GS, Nakatsu K; et al. (2003). "Effects of hypoxia on heme oxygenase expression in human chorionic villi explants and immortalized trophoblast cells". Am. J. Physiol. Heart Circ. Physiol. 284 (3): H853–8. doi:10.1152/ajpheart.00655.2002. PMID 12578814.
  • Galey D, Becker K, Haughey N; et al. (2003). "Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes". J. Neurovirol. 9 (3): 358–71. PMID 12775419.
  • Zenclussen AC, Lim E, Knoeller S; et al. (2004). "Heme oxygenases in pregnancy II: HO-2 is downregulated in human pathologic pregnancies". Am. J. Reprod. Immunol. 50 (1): 66–76. PMID 14506930.
  • Boehning D, Moon C, Sharma S; et al. (2003). "Carbon monoxide neurotransmission activated by CK2 phosphorylation of heme oxygenase-2". Neuron. 40 (1): 129–37. PMID 14527438.
  • Appleton SD, Lash GE, Marks GS; et al. (2004). "Effect of glucose and oxygen deprivation on heme oxygenase expression in human chorionic villi explants and immortalized trophoblast cells". Am. J. Physiol. Regul. Integr. Comp. Physiol. 285 (6): R1453–60. doi:10.1152/ajpregu.00234.2003. PMID 14615405.

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