A Multicopper Ferroxidase Involved in Iron Binding to Transferrins in Dunaliella salina Plasma Membranes

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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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Effects of iron deficiency on iron binding and internalization into acidic vacuoles in Dunaliella salina.

Uptake of iron in the halotolerant alga Dunaliella salina is mediated by a transferrin-like protein (TTf), which binds and internalizes Fe(3+) ions. Recently, we found that iron deficiency induces a large enhancement of iron binding, which is associated with accumulation of three other plasma membrane proteins that associate with TTf. In this study, we characterized the kinetic properties of ir...

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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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Identification of Low Molecular Mass GTP-Binding Proteins in Membranes of the Halotolerant Alga Dunaliella salina.

A family of specific guanine nucleotide-binding proteins in Dunaliella salina was studied. Polypeptides of different subcellular fractions were separated by electrophoresis and transferred to nitrocellulose or Immobilon membranes. Incubation of the transfer blots with [(35)S]GTPgammaS or [alpha-(32)P]GTP showed no evidence for GTP-binding proteins in the chloroplast and cytosol fractions. Howev...

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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: Journal of Biological Chemistry

سال: 2007

ISSN: 0021-9258

DOI: 10.1074/jbc.m609756200