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Absorption of dietary iron in iron salt form (as in most supplements) varies somewhat according to the body's need for iron, and is usually between 10% and 20% of iron intake. Absorption of iron from animal products, and some plant products, is in the form of heme iron, and is more efficient, allowing absorption of from 15% to 35% of intake.
Duodenal cytochrome B (Dcytb) also known as cytochrome b reductase 1 is an enzyme that in humans is encoded by the CYBRD1 gene.. Dcytb CYBRD1 was first identified as a ferric reductase enzyme which catalyzes the reduction of Fe 3+ to Fe 2+ required for dietary iron absorption in the duodenum of mammals. [5]
Absorption of dietary iron in iron salt form (as in most supplements) varies somewhat according to the body's need for iron, and is usually between 10% and 20% of iron intake. Absorption of iron from animal products, and some plant products, is in the form of heme iron, and is more efficient, allowing absorption of from 15% to 35% of intake.
The process of iron transportation consists of iron being reduced by ferrireductases that are present on the cell surface or by dietary reductants such as ascorbate . [10] Once the Fe 3+ has been reduced to Fe 2+ , the DMT1 transporter protein transports the Fe 2+ ions into the cells that line the small intestine ( enterocytes ). [ 10 ]
Hephaestin is a member of the family of copper oxidases that includes mammalian ceruloplasmin, yeast fet3 and fet5, and bacterial ascorbate oxidase, among others.While hephaestin shares 50% amino acid sequence identity with its serum homologue ceruloplasmin, the hephaestin protein includes an additional 86 amino acids at the C-terminus, which code for a single transmembrane domain and a short ...
Erythroferrone is a hormone that regulates iron metabolism through its actions on hepcidin. [5] As shown in mice and humans, it is produced in erythroblasts, which proliferate when new red cells are synthesized, such as after hemorrhage when more iron is needed (so-called stress erythropoiesis). [12]
Ferroportin-mediated iron efflux is calcium-activated; studies of human Fpn expressed in Xenopus laevis oocytes demonstrated that calcium is a required cofactor for Fpn, but that Fpn does not transport calcium. [12] Thus, Fpn does not function as an iron/calcium antiporter. The thermodynamic driving force for Fpn remains unknown.
Hepcidin is a protein that in humans is encoded by the HAMP gene. Hepcidin is a key regulator of the entry of iron into the circulation in mammals. [6]During conditions in which the hepcidin level is abnormally high, such as inflammation, serum iron falls due to iron trapping within macrophages and liver cells and decreased gut iron absorption.