Ferritin is a globular protein found mainly in the liver, which can store about 4500 iron ( Fe3+ )ions in a hollow shell made of 24 identical subunits. Inside the ferritin shell, iron ions form crystallites together with phosphate and hydroxide ions.
Ferritin without iron is called apoferritin. Apoferritin combines with iron making ferritin.
Some ferritin complexes in vertebrates are hetero-oligomers of two highly-related gene products with slightly different physiological properties. The ratio of the two homologous proteins in the complex depends on the relative expression levels of the two genes.
In the setting of anaemia, serum ferritin is the most sensitive lab test for iron deficiency anaemia.
Ferritin is also used as a marker for iron overload disorders, such as haemochromatosis and porphyria in which the ferritin level may be abnormally raised.
As ferritin is also an acute-phase reactant, it is often elevated in the course of disease. A normal C-reactive protein can be used to exclude elevated ferritin caused by acute phase reactions.
Free iron is toxic to cells, and the body has an elaborate set of protective mechanisms to bind iron in various tissue compartments. Within cells, iron is stored complexed to protein as ferritin or hemosiderin. Apoferritin binds to free ferrous iron and stores it in the ferric state. As ferritin accumulates within cells of the RE system, protein aggregates are formed as hemosiderin. Iron in ferritin or hemosiderin can be extracted for release by the RE cells although hemosiderin is less readily available. Under steady state conditions, the serum ferritin level correlates with total body iron stores; thus, the serum ferritin level is the most convenient laboratory test to estimate iron stores.
Ferritin is also used in materials science as a precursor in making iron nanoparticles for carbon nanotube growth by chemical vapor deposition.
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