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Concept
Ferritin
Summary
Ferritin is a universal intracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including archaea, bacteria, algae, higher plants, and animals. It is the primary intracellular iron-storage protein in both prokaryotes and eukaryotes, keeping iron in a soluble and non-toxic form. In humans, it acts as a buffer against iron deficiency and iron overload.
Ferritin is found in most tissues as a cytosolic protein, but small amounts are secreted into the serum where it functions as an iron carrier. Plasma ferritin is also an indirect marker of the total amount of iron stored in the body; hence, serum ferritin is used as a diagnostic test for iron-deficiency anemia. Aggregated ferritin transforms into a toxic form of iron called hemosiderin.
Ferritin is a globular protein complex consisting of 24 protein subunits forming a hollow nanocage with multiple metal–protein interactions. Ferritin that is not combined with iron is called apoferritin.
Ferritin genes are highly conserved between species. All vertebrate ferritin genes have three introns and four exons. 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. The tyrosine residue at amino acid position 27 is thought to be associated with biomineralization.
Ferritin is a hollow globular protein of mass 474 kDa and comprising 24 subunits. Typically it has internal and external diameters of about 8 and 12 nm, respectively. The nature of these subunits varies by class of organism:
In vertebrates, the subunits are of two types, light (L) and heavy (H), which have apparent molecular mass of 19 kDa and 21 kDa, respectively; their sequences are homologous (about 50% identical).
Amphibians have an additional ("M") type of ferritin.
Plants and bacteria have a single ferritin; it most closely resembles the vertebrate H-type.
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