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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]
Hemosiderin or haemosiderin is an iron-storage complex that is composed of partially digested ferritin and lysosomes. The breakdown of heme gives rise to biliverdin and iron. [1] [2] The body then traps the released iron and stores it as hemosiderin in tissues. [3] Hemosiderin is also generated from the abnormal metabolic pathway of ferritin. [3]
Low, as the body holds iron intracellularly with ferritin. Low. The body produces less transferrin (but more ferritin), presumably to keep iron away from pathogens that require it for their metabolism. This is mainly regulated by increased hepcidin production. Normal Pregnancy or use of hormonal contraception, but without iron deficiency Normal ...
Iron can be stored in ferritin as ferric iron due to the ferroxidase activity of the ferritin heavy chain. [43] Dysfunctional ferritin may accumulate as hemosiderin, which can be problematic in cases of iron overload. [44] The ferritin storage iron pool is much larger than the labile iron pool, ranging in concentration from 0.7 mM to 3.6 mM. [40]
Iron-deficiency anemia is confirmed by tests that include serum ferritin, serum iron level, serum transferrin, and total iron binding capacity. [59] A low serum ferritin is most commonly found. However, serum ferritin can be elevated by any type of chronic inflammation and thus is not consistently decreased in iron-deficiency anemia. [23]
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.
Ferritin is present in the cytoplasm of cells and limits the intracellular iron level to approximately 1 μM. Ferritin is a much larger protein than transferrin and is capable of binding several thousand iron atoms in a nontoxic form. Siderophores are unable to directly mobilise iron from ferritin.
In sideroblastic anemia, the body has iron available but cannot incorporate it into hemoglobin, which red blood cells need in order to transport oxygen efficiently. The disorder may be caused either by a genetic disorder or indirectly as part of myelodysplastic syndrome , [ 2 ] which can develop into hematological malignancies (especially acute ...