HMOX1: Difference between revisions

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*{{cite journal  | author=Ishikawa K |title=Heme oxygenase-1 against vascular insufficiency: roles of atherosclerotic disorders |journal=Curr. Pharm. Des. |volume=9 |issue= 30 |pages= 2489–97 |year= 2003 |pmid= 14529548 |doi=10.2174/1381612033453767  }}
*{{cite journal  | author=Ishikawa K |title=Heme oxygenase-1 against vascular insufficiency: roles of atherosclerotic disorders |journal=Curr. Pharm. Des. |volume=9 |issue= 30 |pages= 2489–97 |year= 2003 |pmid= 14529548 |doi=10.2174/1381612033453767  }}
*{{cite journal  |vauthors=Exner M, Minar E, Wagner O, Schillinger M |title=The role of heme oxygenase-1 promoter polymorphisms in human disease |journal=Free Radic. Biol. Med. |volume=37 |issue= 8 |pages= 1097–104 |year= 2005 |pmid= 15451051 |doi= 10.1016/j.freeradbiomed.2004.07.008 }}
*{{cite journal  |vauthors=Exner M, Minar E, Wagner O, Schillinger M |title=The role of heme oxygenase-1 promoter polymorphisms in human disease |journal=Free Radic. Biol. Med. |volume=37 |issue= 8 |pages= 1097–104 |year= 2005 |pmid= 15451051 |doi= 10.1016/j.freeradbiomed.2004.07.008 }}
*{{cite journal  | author=Ozono R |title=New biotechnological methods to reduce oxidative stress in the cardiovascular system: focusing on the Bach1/heme oxygenase-1 pathway |journal=Current pharmaceutical biotechnology |volume=7 |issue= 2 |pages= 87–93 |year= 2006 |pmid= 16724942 |doi=10.2174/138920106776597630  }}
*{{cite journal  | author=Ozono R |title=New biotechnological methods to reduce oxidative stress in the cardiovascular system: focusing on the Bach1/heme oxygenase-1 pathway |journal=Current Pharmaceutical Biotechnology |volume=7 |issue= 2 |pages= 87–93 |year= 2006 |pmid= 16724942 |doi=10.2174/138920106776597630  }}
*{{cite journal  |vauthors=Tracz MJ, Alam J, Nath KA |title=Physiology and pathophysiology of heme: implications for kidney disease |journal=J. Am. Soc. Nephrol. |volume=18 |issue= 2 |pages= 414–20 |year= 2007 |pmid= 17229906 |doi= 10.1681/ASN.2006080894 }}
*{{cite journal  |vauthors=Tracz MJ, Alam J, Nath KA |title=Physiology and pathophysiology of heme: implications for kidney disease |journal=J. Am. Soc. Nephrol. |volume=18 |issue= 2 |pages= 414–20 |year= 2007 |pmid= 17229906 |doi= 10.1681/ASN.2006080894 }}
*{{cite journal  |vauthors=Chang CF, Cho S, Wang J |title=(-)-Epicatechin protects hemorrhagic brain via synergistic Nrf2 pathways |journal=Ann Clin Transl Neurol. |volume=1 |issue= 4 |pages= 258–271 |year= 2014 |pmid= 24741667 |doi= 10.1002/acn3.54 |pmc=3984761}}
*{{cite journal  |vauthors=Chang CF, Cho S, Wang J |title=(-)-Epicatechin protects hemorrhagic brain via synergistic Nrf2 pathways |journal=Ann Clin Transl Neurol. |volume=1 |issue= 4 |pages= 258–271 |year= 2014 |pmid= 24741667 |doi= 10.1002/acn3.54 |pmc=3984761}}
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{{Portal bar|Molecular and Cellular Biology|border=no}}
{{Portal bar|Molecular and Cellular Biology|border=no}}


[[Category:Human genes]]
[[Category:EC 1.14.99]]
[[Category:EC 1.14.99]]




{{genetics-stub}}
{{gene-22-stub}}

Latest revision as of 12:22, 9 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

HMOX1 (heme oxygenase (decycling) 1) is a human gene that encodes for the enzyme heme oxygenase 1 (EC 1.14.99.3). Heme oxygenase mediates the first step of heme catabolism, it cleaves heme to form biliverdin.

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, carbon monoxide, and ferrous iron.[1] The biliverdin is subsequently converted to bilirubin by biliverdin reductase. 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.[2]

The HMOX gene is located on the long (q) arm of chromosome 22 at position 12.3, from base pair 34,101,636 to base pair 34,114,748.

Related conditions

Anti-inflammatory effect

The ability of oxygenase 1 to catabolize free heme and produce carbon monoxide (CO) gives its anti-inflammatory properties by up-regulation of interleukin 10 (IL-10) and interleukin 1 receptor antagonist (IL-1RA) expression.[3]

See also

References

  1. Lehninger's Principles of Biochemistry, 5th Edition. New York: W.H. Freeman and Company. 2008. p. 876. ISBN 978-0-7167-7108-1.
  2. "Entrez Gene: HMOX1 heme oxygenase (decycling) 1".
  3. Piantadosi CA, Withers CM, Bartz RR, MacGarvey NC, Fu P, Sweeney TE, Welty-Wolf KE, Suliman HB (May 2011). "Heme oxygenase-1 couples activation of mitochondrial biogenesis to anti-inflammatory cytokine expression". J. Biol. Chem. 286 (18): 16374–85. doi:10.1074/jbc.M110.207738. PMC 3091243. PMID 21454555.

Further reading