Hemopexin

From Wikipedia, the free encyclopedia
Jump to: navigation, search
This article is about the hemopexin protein. For the family of proteins containing hemopexin-like repeats, see hemopexin family.
Hemopexin
Identifiers
Symbols HPX ; HX
External IDs OMIM142290 MGI105112 HomoloGene511 GeneCards: HPX Gene
EC number 3.2.1.35
RNA expression pattern
PBB GE HPX 39763 at tn.png
PBB GE HPX 210013 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3263 15458
Ensembl ENSG00000110169 ENSMUSG00000030895
UniProt P02790 Q91X72
RefSeq (mRNA) NM_000613 NM_017371
RefSeq (protein) NP_000604 NP_059067
Location (UCSC) Chr 11:
6.45 – 6.46 Mb
Chr 7:
105.59 – 105.6 Mb
PubMed search [1] [2]

Hemopexin (or haemopexin; HPX), also known as beta-1B-glycoprotein is a protein that in humans is encoded by the HPX gene[1][2][3] and belongs to hemopexin family of proteins.[4]

Function[edit]

Hemopexin binds heme with the highest affinity of any known protein. Its function is scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin and thus protects the body from the oxidative damage that free heme can cause. In addition, hemopexin releases its bound ligand for internalisation upon interacting with a specific receptor situated on the surface of liver cells. This function of hemopexin is to preserve the body's iron.[5]

Clinical significance[edit]

Its levels in serum reflect how much heme is present in the blood. Therefore, low hemopexin levels indicates that there has been significant degradation of heme containing compounds and hemopexin is made to scavenge any heme it can. Low hemopexin levels are one of the diagnostic features of a hemolytic anemia.

References[edit]

  1. ^ "Entrez Gene: HPX hemopexin". 
  2. ^ Altruda F, Poli V, Restagno G, Silengo L (1988). "Structure of the human hemopexin gene and evidence for intron-mediated evolution". J. Mol. Evol. 27 (2): 102–8. doi:10.1007/BF02138368. PMID 2842511. 
  3. ^ Altruda F, Poli V, Restagno G, Argos P, Cortese R, Silengo L (June 1985). "The primary structure of human hemopexin deduced from cDNA sequence: evidence for internal, repeating homology". Nucleic Acids Res. 13 (11): 3841–59. doi:10.1093/nar/13.11.3841. PMC 341281. PMID 2989777. 
  4. ^ Bode W (June 1995). "A helping hand for collagenases: the haemopexin-like domain". Structure 3 (6): 527–30. doi:10.1016/s0969-2126(01)00185-x. PMID 8590012. 
  5. ^ Tolosano E, Altruda F (April 2002). "Hemopexin: structure, function, and regulation". DNA Cell Biol. 21 (4): 297–306. doi:10.1089/104454902753759717. PMID 12042069. 

Further reading[edit]

External links[edit]

See also[edit]