Serum iron-binding capacity
Serum ferritin Liver biopsy
The intra-luminal pH of the duodenum;
Chelation with ascorbate or citrate, which facilitates absorption;
The presence of plant phytates and tannins, which reduce the availability of iron.
Iron distribution is achieved by transferrin, the major iron transporting protein in the serum and the extracellular fluid. Transferrin is a single chain glycoprotein with two similar iron-binding sites. It is predominantly synthesised in the liver and has a half-life of 8 days. The high iron affinity of transferrin protects the body from free iron. The iron-transferrin complex is attached to high affinity cell surface transferrin receptors in the liver and in developing red blood cells in the bone marrow. The ensuing complex is internalised into clathrin-coated endosomes. An ATP-dependent proton pump lowers the endosomal pH to less than 6, when transferrin divests itself of its attached iron and exits the endosomal membrane in a process mediated by divalent metal transporter 1 and an endosomal oxido-reductase. The transferrin molecule is recycled to the cell surface and released back into the circulation. Iron is stored as ferritin and haemosiderin.
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