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The protein encoded by HEPH is similar to an iron transport protein found in mouse. Additionally we are shipping Hephaestin Antibodies (48) and Hephaestin Kits (9) and many more products for this protein.
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In mice with mutation of Cp and Heph, iron accumulates in glia, while neurons have low iron levels. Both neurons and glia degenerate and mice become ataxic unless given an iron chelator.
The multicopper ferroxidase (show A2BP1 Proteins) hephaestin enhances intestinal iron absorption in mice.
Data (including data from studies in knockout mice) suggest that hephaestin and ceruloplasmin (show CP Proteins) play distinct roles in regulation of gene expression in various regions of the brain and are involved in iron homeostasis.
Cp and Heph are necessary for iron export from the retina but are not essential for iron import into the retina.
results show that Heph is expressed by oligodendrocytes and plays an important role in iron efflux from these cells.
Hephaestin and Ireg1 (show SLC40A1 Proteins) expression respond to systemic rather than local signals of iron status.
Hephaestin has both amine oxidase (show MAOA Proteins) and ferroxidase (show CP Proteins) activity primary intestinal enterocytes and may facilitate iron export from intestinal enterocytes; also activity and structural studies of truncated Heph in sla mice
Ceruloplasmin (show CP Proteins) ane hephaestin are critical for CNS iron homeostasis and that loss of Cp and Heph in the mouse leads to age-dependent retinal neurodegeneration.
CDX2 (show CDX2 Proteins) expression was modulated in response to changes in intracellular iron levels, implying a regulatory pathway in which increased iron levels lead to increased expression of CDX2 (show CDX2 Proteins) and HEPH and enhanced iron export.
Copper is required for the proper processing and/or stability of hephaestin.
This review describes function of hephaestin as ferroxidase (show CP Proteins) is essential for iron binding to apotransferrin in the lamina propria of the intestinal mucosa, a process that is important for further transport of iron to the liver by the portal vein.
Iron efflux from human brain microvasculature endothelial cells ferroportin (show SLC40A1 Proteins) requires the action of an exocytoplasmic ferroxidase (show CP Proteins) which can be either endogenous hephaestin or extracellular ceruloplasmin (show CP Proteins).
Heph is active in placenta but may not play a key role in placental iron transport.
These results support the hypothesis that hephaestin is involved in iron mobilization of iron from the intestine to circulation.
In contrast to ceruloplasmin (show CP Proteins), hephaestin was incapable of direct oxidation of adrenaline and dopamine implying a difference in biological substrate specificities between these two homologous ferroxidases.
Hephaestin is expressed in enterocytes, in the antral portion of the stomach, in the myenteric and submucous plexi, and in pancreatic beta-cells.
The gene structure, spanning approximately 100 kb, was assembled from the cDNA clones and the chromosome X genomic sequence data. Modelling supports its role as a membrane-tethered ferroxidase (show CP Proteins).
The hephaestin protein mRNA expression is not significantly altered by variations in iron homeostasis. The effect of phlebotomy-induced erythropoiesis did not alter either gene transcript mRNA expression.
Reombinant hephaestin was shown to have both multicopper oxidase and ferroxidase (show CP Proteins) activity.
Results suggest the possibility that FPN-1 (show SLC40A1 Proteins) might associate and interact with Heph in the process of iron exit across the basolateral membrane of intestinal absorptive cell.
The protein encoded by this gene is similar to an iron transport protein found in mouse. The mouse protein is similar to ceruloplasmin, a serum multi-copper ferroxidase, and is thought to be a membrane-bound protein responsible for transport of dietary iron from epithelial cells of the intestinal lumen into the circulatory system. In mouse, defects in this gene can lead to severe microcytic anemia. Three transcript variants encoding different isoforms have been described for this gene.
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