Recombinant Expression and Functional Characterization of Human Hephaestin: A Multicopper Oxidase with Ferroxidase Activity

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The Multicopper Ferroxidase Hephaestin Enhances Intestinal Iron Absorption in Mice

Hephaestin is a vertebrate multicopper ferroxidase important for the transfer of dietary iron from intestinal cells to the blood. Hephaestin is mutated in the sex-linked anemia mouse, resulting in iron deficiency. However, sex-linked anemia mice still retain some hephaestin ferroxidase activity. They survive, breed, and their anemia improves with age. To gain a better understanding of the role ...

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Hephaestin is a mammalian gene that encodes a predicted multicopper oxidase required for intestinal iron export. To examine if hephaestin can act as a ferroxidase, we studied yeast strains transformed with plasmids containing both a full-length hephaestin and a hephaestin lacking a transmembrane domain. Yeast with a deletion in FET3, which encodes a cell-surface multicopper oxidase, cannot grow...

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INTESTINE Mislocalisation of hephaestin, a multicopper ferroxidase involved in basolateral intestinal iron transport, in the sex linked anaemia mouse

Background: Hephaestin is a multicopper ferroxidase required for basolateral transport of iron from enterocytes. Sex linked anaemia (sla) mice have a defect in the release of iron from intestinal enterocytes into the circulation due to an interstitial deletion in the hephaestin gene (heph). Results: We have demonstrated that hephaestin is primarily localised to a supranuclear compartment in bot...

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Mislocalisation of hephaestin, a multicopper ferroxidase involved in basolateral intestinal iron transport, in the sex linked anaemia mouse.

BACKGROUND Hephaestin is a multicopper ferroxidase required for basolateral transport of iron from enterocytes. Sex linked anaemia (sla) mice have a defect in the release of iron from intestinal enterocytes into the circulation due to an interstitial deletion in the hephaestin gene (heph). RESULTS We have demonstrated that hephaestin is primarily localised to a supranuclear compartment in bot...

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ژورنال

عنوان ژورنال: Biochemistry

سال: 2005

ISSN: 0006-2960,1520-4995

DOI: 10.1021/bi051559k