HMOX2

From Wikipedia, the free encyclopedia

Heme oxygenase (decycling) 2

PDB rendering based on 2q32.

Available structures: 2q32

Identifiers

Symbol(s)

HMOX2; HO-2

External IDs

OMIM: 141251 MGI: 109373 HomoloGene: 1611

Gene ontology
Molecular Function:	• heme oxygenase (decyclizing) activity • iron ion binding • electron carrier activity • metal ion binding
Cellular Component:	• endoplasmic reticulum • microsome
Biological Process:	• heme oxidation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002134 (mRNA)
NP_002125 (protein)

NM_010443 (mRNA)
NP_034573 (protein)

Location

Chr 16: 4.47 - 4.5 Mb

Chr 16: 4.64 - 4.68 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: HMOX2 heme oxygenase (decycling) 2.

[edit] 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.