Haemopexin

This MedLibrary.org supplementary page on Haemopexin is provided directly from the open source Wikipedia as a service to our readers. Please see the note below on authorship of this content, as well as the Wikipedia usage guidelines. To search for other content from our encyclopedia supplement, please use the form below:

Related Sponsors

BM Pharmacy Generic pharmaceuticals at unbeatable prices. Insomnia, men's health, hair health, pain control. bmpharmacy.com
Online Pharmacy Carisoprodol, tadalafil, sildenafil, vardenafil and more... xlpharmacy.com
MedBasket.com Discreet. Inexpensive. Fast shipping. Great selection. What more can we say? medbasket.com
Frugalmed 2000 reasons to shop with us first. frugalmed.com
Ads by Tiva

Hemopexin
Identifiers
Symbols HPX;
External IDs OMIM: 142290 MGI: 105112 HomoloGene: 511
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 3263 15458
Ensembl ENSG00000110169 ENSMUSG00000030895
Uniprot P02790 Q3UKP2
Refseq NM_000613 (mRNA)
NP_000604 (protein)		 NM_017371 (mRNA)
NP_059067 (protein)
Location Chr 11: 6.41 - 6.42 Mb Chr 7: 105.47 - 105.47 Mb
Pubmed search [1] [2]

Hemopexin, also known as HPX, is a human gene.[1]

The protein encoded by this gene, hemopexin (or haemopexin) binds heme with the highest affinity of any known protein. Its function of scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin 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.

Contents

Clinical significance

Its levels in serum reflect how much heme is present in the blood. Low levels indicate that there is a lot of it. Therefore, low hemopexin levels indicates that there has been significant degradation of heme containing compounds - the latter being primarily hemoglobin, it indicates hemolysis and low hemopexin levels are therefore one of the diagnostic features of a hemolytic anemia.

References

  1. ^ "Entrez Gene: HPX hemopexin".

Further reading

  • Piccard H, Van den Steen PE, Opdenakker G (2007). "Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins.". J. Leukoc. Biol. 81 (4): 870–92. doi:10.1189/jlb.1006629. PMID 17185359. 
  • Morgan WT, Muller-Eberhard U, Lamola AA (1978). "Interaction of rabbit hemopexin with bilirubin.". Biochim. Biophys. Acta 532 (1): 57–64. PMID 620056. 
  • Liu HM, Atack JR, Rapoport SI (1989). "Immunohistochemical localization of intracellular plasma proteins in the human central nervous system.". Acta Neuropathol. 78 (1): 16–21. PMID 2735186. 
  • Smith A, Tatum FM, Muster P, et al. (1988). "Importance of ligand-induced conformational changes in hemopexin for receptor-mediated heme transport.". J. Biol. Chem. 263 (11): 5224–9. PMID 2833500. 
  • 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. PMID 2842511. 
  • Altruda F, Poli V, Restagno G, et al. (1985). "The primary structure of human hemopexin deduced from cDNA sequence: evidence for internal, repeating homology.". Nucleic Acids Res. 13 (11): 3841–59. PMID 2989777. 
  • Taketani S, Kohno H, Naitoh Y, Tokunaga R (1987). "Isolation of the hemopexin receptor from human placenta.". J. Biol. Chem. 262 (18): 8668–71. PMID 3036819. 
  • Law ML, Cai GY, Hartz JA, et al. (1989). "The hemopexin gene maps to the same location as the beta-globin gene cluster on human chromosome 11.". Genomics 3 (1): 48–52. PMID 3220477. 
  • Morgan WT, Alam J, Deaciuc V, et al. (1988). "Interaction of hemopexin with Sn-protoporphyrin IX, an inhibitor of heme oxygenase. Role for hemopexin in hepatic uptake of Sn-protoporphyrin IX and induction of mRNA for heme oxygenase.". J. Biol. Chem. 263 (17): 8226–31. PMID 3372522. 
  • Takahashi N, Takahashi Y, Putnam FW (1985). "Complete amino acid sequence of human hemopexin, the heme-binding protein of serum.". Proc. Natl. Acad. Sci. U.S.A. 82 (1): 73–7. PMID 3855550. 
  • Takahashi N, Takahashi Y, Putnam FW (1984). "Structure of human hemopexin: O-glycosyl and N-glycosyl sites and unusual clustering of tryptophan residues.". Proc. Natl. Acad. Sci. U.S.A. 81 (7): 2021–5. PMID 6371807. 
  • Frantíková V, Borvák J, Kluh I, Morávek L (1985). "Amino acid sequence of the N-terminal region of human hemopexin.". FEBS Lett. 178 (2): 213–6. PMID 6510521. 
  • Smith A, Alam J, Escriba PV, Morgan WT (1993). "Regulation of heme oxygenase and metallothionein gene expression by the heme analogs, cobalt-, and tin-protoporphyrin.". J. Biol. Chem. 268 (10): 7365–71. PMID 8463269. 
  • Morris CM, Candy JM, Edwardson JA, et al. (1993). "Evidence for the localization of haemopexin immunoreactivity in neurones in the human brain.". Neurosci. Lett. 149 (2): 141–4. PMID 8474687. 
  • Hrkal Z, Kuzelová K, Muller-Eberhard U, Stern R (1996). "Hyaluronan-binding properties of human serum hemopexin.". FEBS Lett. 383 (1-2): 72–4. PMID 8612795. 
  • Hunt RC, Hunt DM, Gaur N, Smith A (1996). "Hemopexin in the human retina: protection of the retina against heme-mediated toxicity.". J. Cell. Physiol. 168 (1): 71–80. doi:10.1002/(SICI)1097-4652(199607)168:1<71::AID-JCP9>3.0.CO;2-5. PMID 8647924. 
  • Miller YI, Smith A, Morgan WT, Shaklai N (1996). "Role of hemopexin in protection of low-density lipoprotein against hemoglobin-induced oxidation.". Biochemistry 35 (40): 13112–7. doi:10.1021/bi960737u. PMID 8855948. 
  • Grinberg LN, O'Brien PJ, Hrkal Z (1999). "The effects of heme-binding proteins on the peroxidative and catalatic activities of hemin.". Free Radic. Biol. Med. 27 (1-2): 214–9. PMID 10443938. 
  • Nakajima S, Moriyama T, Hayashi H, et al. (2000). "Hemopexin as a carrier protein of tumor-localizing Ga-metalloporphyrin-ATN-2.". Cancer Lett. 149 (1-2): 221–6. PMID 10737728. 
  • Shipulina N, Smith A, Morgan WT (2001). "Heme binding by hemopexin: evidence for multiple modes of binding and functional implications.". J. Protein Chem. 19 (3): 239–48. PMID 10981817. 
 This article on a gene on chromosome 11 is a stub. You can help Wikipedia by expanding it.

External links

See also

 This article on a gene on chromosome 11 is a stub. You can help Wikipedia by expanding it.
v • d • e
Protein: glycoproteins
v • d • e
Globulins: beta globulins
v • d • e
Acute phase proteins
Amyloid
Other positive
Negative

Wikipedia content modification information:

  • This page was last modified on 7 August 2008, at 10:51.

Wikipedia Authorship and Review

Wikipedia content provided here is not reviewed directly by MedLibrary.org. Wikipedia content is authored by an open community of volunteers and is not produced by or in any way affiliated with MedLibrary.org.

Wikipedia Usage Guidelines

This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article on "Haemopexin".

The URL for this specific entry is:

All Wikipedia text is available under the terms of the GNU Free Documentation License. (See Copyrights for details). Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc.