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Symbols HPX ;
External IDs Template:OMIM5 Template:MGI HomoloGene511
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

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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]


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.

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.

Differential Diagnosis




  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.

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See also


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