hemopexin


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hemopexin

 [he″mo-pek´sin]
a heme-binding serum protein.

he·mo·pex·in

(hē'mō-peks'in), [MIM*142290]
A serum glycoprotein related to β-globulins, with molecular weight around 57,000, containing 22% carbohydrate; important in binding heme and porphyrins, preventing excretion, and perhaps regulating heme in drug metabolism.
[hemo- + G. pēxis, fixation, + -in]

he·mo·pex·in

(hē'mō-peks'in)
A serum protein related to β-globulins, important in binding heme and porphyrins, preventing excretion, and perhaps regulating heme in drug metabolism.
Synonym(s): haemopexin.
[hemo- + G. pēxis, fixation, + -in]
References in periodicals archive ?
Postexposure administration of hemopexin, a heme-scavenging protein, decreased lung injury and improved survival.[52] Studies also demonstrated that humanized transgenic mice overexpressing HO-1 were significantly protected from exposure to Br[sub]2.[52] These are the first studies delineating the pathogenesis of Br[sub]2 toxicity in respiratory diseases and demonstrated the critical role of heme in ARDS caused by Br[sub]2[Figure 3].
Based on a multipe sequence alignment with representative orthologues from other fish species and human hemopexin, the CcWap65 polypeptide shares varying degrees of homology with their corresponding orthologues (Fig.
(1984) The structure of a trisialyl di-antennary N-type glycopeptide obtained from rat plasma hemopexin. Glycoconj.
Li et al., "The hemopexin domain of matrix metalloproteinase-9 activates cell signaling and promotes migration of Schwann cells by binding to low-density lipoprotein receptor-related protein," The Journal of Neuroscience, vol.
Welsh et al., "Hemopexin induces nephrin-dependent reorganization of the actin cytoskeleton in podocytes," Journal of the American Society of Nephrology, vol.
Deletion of the hemopexin or heme oxygenase-2 gene aggravates brain injury following stroma-free hemoglobin-induced intracerebral hemorrhage.
Proteolytic action of kallikrein-related peptidase 7 produces unique active matrix metalloproteinase-9 lacking the C-terminal hemopexin domains.
Association of Hemopexin in Tear Film and Conjunctival macrophages With Vernal Keratoconjuctivitis.
These "pawns" include transferrin, lactoferrin, ferritin, haptoglobin (hemoglobin chaperone), and hemopexin (heme chaperone), all of which are modified in the presence of infection.
Zucker, "Distinct roles for the catalytic and hemopexin domains of membrane type 1-matrix metalloproteinase in substrate degradation and cell migration," Journal of Biological Chemistry, vol.
plasma concentrations of acute phase proteins or reactants such as haptoglobin (Hp), alpha-acid glycoprotein, alpha-1-antitrypsin, fibrinogen, complement components C3 and C4 and hemopexin, immunoglobulins, cytokines) and substances which are known to induce an acute phase response (e.g.