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Results show that both HEPH and CP are expressed in subcutaneous adipose tissue. Ablation of either MCF leads to a compensatory increase in the other, which contributes to the balance of iron status. However, ablation of both induces severe iron deposition in adipocytes and displays disordered carbohydrate metabolism characterized as type 2 diabetes.
We thus used hephaestin (Heph) and ceruloplasmin (Cp) single-knockout mice and Heph/Cp double-knockout mice to investigate the roles of multicopper ferroxidases(MCF) in pancreatic iron homeostasis. We found that both HEPH and CP were expressed in the mouse pancreas, and that ablation of either MCF had limited effect on the pancreatic iron levels.
Hephaestin and ceruloplasmin have roles in facilitating iron metabolism in the mouse kidney
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 hephaestin enhances intestinal iron absorption in mice.
Data (including data from studies in knockout mice) suggest that hephaestin and ceruloplasmin 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 expression respond to systemic rather than local signals of iron status.
Hephaestin has both amine oxidase and ferroxidase activity primary intestinal enterocytes and may facilitate iron export from intestinal enterocytes; also activity and structural studies of truncated Heph in sla mice
Ceruloplasmin 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 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 and HEPH and enhanced iron export.
Copper is required for the proper processing and/or stability of hephaestin.
Expression of hephaestin (Heph) increased significantly in cerebral cortex and caudate putamen of old (80-week-old), ceruloplasmin-deficient (CP-/-) mice; expression of Heph was unaltered in substantia nigra and cerebellum.
This review describes function of hephaestin as ferroxidase 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 requires the action of an exocytoplasmic ferroxidase which can be either endogenous hephaestin or extracellular ceruloplasmin.
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, 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.
location was observed on or near the cell surface suggesting it might participate in surface membrane transport of iron
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.
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 activity.
Results suggest the possibility that FPN-1 might associate and interact with Heph in the process of iron exit across the basolateral membrane of intestinal absorptive cell.
stable complex between these Cp and Hp and Tf does not occur under the experimental conditions used
Repletion of copper in Caco2 cells leads to reconstitution of hephaestin protein expression, activity, and transepithelial iron transport.
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.
, sex linked anemia