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Ferroportin-1, also known as solute carrier family 40 member 1 (SLC40A1) or iron-regulated transporter 1 (IREG1), is a protein that in humans is encoded by the SLC40A1 gene. [5] Ferroportin is a transmembrane protein that transports iron from the inside of a cell to the outside of the cell.
[17] [18] The higher order multifunctional glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) also acts as a transferrin receptor. [19] [20] Transferrin-bound ferric iron is recognized by these transferrin receptors, triggering a conformational change that causes endocytosis. Iron then enters the cytoplasm from the endosome via ...
After absorption, the iron from preparation becomes part of the iron pool in the body. Upon stimulation, the reduction of iron storage Fe3+ in the enterocyte to Fe2+ ferroportin allows the passage of iron through the cell membrane for export. In the blood, ferroportin is then converted to transferrin to reach other tissues. [14]
Transferrin glycoproteins bind iron tightly, but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of total body iron, it forms the most vital iron pool with the highest rate of turnover (25 mg/24 h). Transferrin has a molecular weight of around 80 kDa and contains two specific high-affinity Fe(III) binding sites.
Ferritin genes are highly conserved between species. All vertebrate ferritin genes have three introns and four exons. [8] In human ferritin, introns are present between amino acid residues 14 and 15, 34 and 35, and 82 and 83; in addition, there are one to two hundred untranslated bases at either end of the combined exons. [9]
Transferrin receptor protein 1 (TfR1), also known as Cluster of Differentiation 71 (CD71), is a protein that in humans is encoded by the TFRC gene. [ 5 ] [ 6 ] TfR1 is required for iron import from transferrin into cells by endocytosis .
Included for each food is its weight in grams, its calories, and (also in grams,) the amount of protein, carbohydrates, dietary fiber, fat, and saturated fat. [1] As foods vary by brands and stores, the figures should only be considered estimates, with more exact figures often included on product labels.
The differences between those cytochromes lies in the different side-chains. For instance cytochrome a has a heme a prosthetic group and cytochrome b has a heme b prosthetic group. These differences result in different Fe 2+ /Fe 3+ redox potentials such that various cytochromes are involved in the mitochondrial electron transport chain. [17]