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Gene Review

Hpx  -  hemopexin

Mus musculus

Synonyms: Hemopexin, Hpxn, hx
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Disease relevance of Hpxn


High impact information on Hpxn

  • Analysis of single-null mice demonstrated the antioxidant action of haptoglobin and hemopexin in vivo and suggests that the 2 proteins cooperate in the resolution of hemolytic stress [2].
  • Hemopexin (Hx) is a plasma glycoprotein mainly expressed in liver and, less abundantly, in the central and peripheral nervous systems [1].
  • These data indicate that, although Hx is not crucial either for iron metabolism or as a protection against oxidative stress under physiologic conditions, it does play an important protective role after hemolytic processes [1].
  • These data demonstrate for the first time that the hemopexin domain of MMP-9 has a high affinity binding site for gelatin, and the particular recombinant domain is able to block MMP-9 activity and tumor cell invasion [5].
  • The structure of the exons encoding the catalytic domain and pro-domain of MMP-14 is distinct from previously described MMP genes, whereas the exons encoding the hemopexin-like domains are similar to those of most other MMP genes [6].

Biological context of Hpxn


Anatomical context of Hpxn

  • Among plasma-protective proteins against oxidative damage caused by red blood cell rupture, haptoglobin and hemopexin are thought to play a crucial role [2].
  • Hepatocytes on matrigel secreted substantially higher amounts of albumin, transferrin, haptoglobin, and hemopexin, Northern blot analyses of extracted cellular RNA, expressed increased amounts of mRNA for the liver-specific protein albumin (as compared with cells on vitrogen) [9].
  • Respective roles of inflammation and axonal breakdown in the regulation of peripheral nerve hemopexin: an analysis in rats and in C57BL/Wlds mice [10].
  • We also show that HPX synthesis is dramatically increased in macrophages during their activation or after IL-6 stimulation [10].
  • We conclude that, after nerve injury, HPX overexpression occurs first in Schwann cells as a result of axotomy and is subsequently regulated by inflammation [10].

Associations of Hpxn with chemical compounds

  • A new bioactive factor capable of stimulating the production of acute-phase transport proteins, haptoglobin, hemopexin and ceruloplasmin, was found in mouse serum soon after the administration of lentinan, an immunomodulatory polysaccharide [11].
  • The greatest changes (four-fold 48 h after LPS administration) were observed for haptoglobin and hemopexin [12].
  • Consequently, the increases in haptoglobin and hemopexin were marked and 90% or more of the increased sialic acid was derived from these two glycoproteins after exposure to UV radiation [13].
  • Biol. Chem. 259, 12049-12053) contains only 4 histidine residues which are conserved in rabbit, human, rat, and mouse hemopexin [14].
  • This conformational change which plays a pivotal role in hemopexin function requires the bis-histidyl coordination with heme iron and leads to a tighter association between domain I and domain II shown by the co-migration of heme-domain I and domain II in sucrose gradients [3].

Other interactions of Hpxn

  • Membrane phospholipid reorganization differentially regulates metallothionein and heme oxygenase by heme-hemopexin [15].
  • Concentrations of hemopexin, a porphyrin-binding serum protein synthesized exclusively in the liver, increased significantly and concomitantly with levels of erythrocyte and liver protoporphyrin and coproporphyrin in mice made porphyric with 1% griseofulvin in the feed [16].

Analytical, diagnostic and therapeutic context of Hpxn


  1. Defective recovery and severe renal damage after acute hemolysis in hemopexin-deficient mice. Tolosano, E., Hirsch, E., Patrucco, E., Camaschella, C., Navone, R., Silengo, L., Altruda, F. Blood (1999) [Pubmed]
  2. Enhanced splenomegaly and severe liver inflammation in haptoglobin/hemopexin double-null mice after acute hemolysis. Tolosano, E., Fagoonee, S., Hirsch, E., Berger, F.G., Baumann, H., Silengo, L., Altruda, F. Blood (2002) [Pubmed]
  3. Use of hemopexin domains and monoclonal antibodies to hemopexin to probe the molecular determinants of hemopexin-mediated heme transport. Morgan, W.T., Muster, P., Tatum, F.M., McConnell, J., Conway, T.P., Hensley, P., Smith, A. J. Biol. Chem. (1988) [Pubmed]
  4. In vitro and in vivo comparative study of chimeric liver-specific promoters. Kramer, M.G., Barajas, M., Razquin, N., Berraondo, P., Rodrigo, M., Wu, C., Qian, C., Fortes, P., Prieto, J. Mol. Ther. (2003) [Pubmed]
  5. The matrix metalloproteinase 9 (mmp-9) hemopexin domain is a novel gelatin binding domain and acts as an antagonist. Roeb, E., Schleinkofer, K., Kernebeck, T., Pötsch, S., Jansen, B., Behrmann, I., Matern, S., Grötzinger, J. J. Biol. Chem. (2002) [Pubmed]
  6. The matrix metalloproteinase-14 (MMP-14) gene is structurally distinct from other MMP genes and is co-expressed with the TIMP-2 gene during mouse embryogenesis. Apte, S.S., Fukai, N., Beier, D.R., Olsen, B.R. J. Biol. Chem. (1997) [Pubmed]
  7. Specific expression in brain and liver driven by the hemopexin promoter in transgenic mice. Tolosano, E., Cutufia, M.A., Hirsch, E., Silengo, L., Altruda, F. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  8. Mechanism of metallothionein gene regulation by heme-hemopexin. Roles of protein kinase C, reactive oxygen species, and cis-acting elements. Ren, Y., Smith, A. J. Biol. Chem. (1995) [Pubmed]
  9. Regulation of gene expression in adult rat hepatocytes cultured on a basement membrane matrix. Schuetz, E.G., Li, D., Omiecinski, C.J., Muller-Eberhard, U., Kleinman, H.K., Elswick, B., Guzelian, P.S. J. Cell. Physiol. (1988) [Pubmed]
  10. Respective roles of inflammation and axonal breakdown in the regulation of peripheral nerve hemopexin: an analysis in rats and in C57BL/Wlds mice. Camborieux, L., Julia, V., Pipy, B., Swerts, J.P. J. Neuroimmunol. (2000) [Pubmed]
  11. Macrophage-mediated acute-phase transport protein production induced by lentinan. Suga, T., Maeda, Y.Y., Uchida, H., Rokutanda, M., Chihara, G. Int. J. Immunopharmacol. (1986) [Pubmed]
  12. Reference maps of mouse serum acute-phase proteins: changes with LPS-induced inflammation and apolipoprotein A-I and A-II transgenes. Wait, R., Chiesa, G., Parolini, C., Miller, I., Begum, S., Brambilla, D., Galluccio, L., Ballerio, R., Eberini, I., Gianazza, E. Proteomics (2005) [Pubmed]
  13. Changes in serum levels of sialoglycoproteins in mice exposed to UV-B radiation. Yamamoto, K., Furuya, T., Kameoka, Y., Kawanaka, M. Biol. Pharm. Bull. (1998) [Pubmed]
  14. Identification of the histidine residues of hemopexin that coordinate with heme-iron and of a receptor-binding region. Morgan, W.T., Muster, P., Tatum, F., Kao, S.M., Alam, J., Smith, A. J. Biol. Chem. (1993) [Pubmed]
  15. Membrane phospholipid reorganization differentially regulates metallothionein and heme oxygenase by heme-hemopexin. Escriba, P.V., Morales, P., Smith, A. DNA Cell Biol. (2002) [Pubmed]
  16. Griseofulvin causing hyperhemopexinemia and hepatic proliferation in mice: an in vivo and in vitro study. Cripps, D.J., Liem, H.H., Muller-Eberhard, U. J. Invest. Dermatol. (1977) [Pubmed]
  17. Expression of the mRNA of heme-binding protein 23 is coordinated with that of heme oxygenase-1 by heme and heavy metals in primary rat hepatocytes and hepatoma cells. Immenschuh, S., Iwahara, S., Satoh, H., Nell, C., Katz, N., Muller-Eberhard, U. Biochemistry (1995) [Pubmed]
  18. Hemopexin levels in mice. Ishiguro, T., Imanishi, K., Suzuki, I. Int. J. Immunopharmacol. (1984) [Pubmed]
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