Ferritin

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Structure of the ferritin complex
ferritin, light polypeptide
Identifiers
Symbol(s) FTL
Entrez 2512
OMIM 134790
RefSeq NM_000146
UniProt P02792
Other data
Locus Chr. 19 q13.3-13.4
ferritin, heavy polypeptide 1
Identifiers
Symbol(s) FTH1 FTHL6
Entrez 2495
OMIM 134770
RefSeq NM_002032
UniProt P02794
Other data
Locus Chr. 11 q13
ferritin mitochondrial
Identifiers
Symbol(s) FTMT
Entrez 94033
OMIM 608847
RefSeq NM_177478
UniProt Q8N4E7
Other data
Locus Chr. 5 q23.1

Ferritin is a globular protein complex consisting of 24 protein subunits and is the main intracellular iron storage protein in both prokaryotes and eukaryotes, keeping it in a soluble and non-toxic form. Ferritin which is not combined with iron is called apoferritin.

Contents

[edit] Description

The Ferritin protein complex consists of 24 protein subunits. In vertebrates, these are both the light (L) and the heavy (H) type with a molecular weight of 19 kDA or 21 kDA respectively. In plants and bacteria the complex only consists of the H-chain type. Inside the ferritin shell, iron ions form crystallites together with phosphate and hydroxide ions. Each Ferritin complex can store about 4500 iron (Fe3+)ions.

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.

[edit] Uses

Serum ferritin levels are measured in patients as part of the iron studies workup for anemia. The ferritin levels measured have a direct correlation with the total amount of iron stored in the body. If ferritin is high there is iron in excess, which would be excreted in the stool. If ferritin is low there is a risk for lack in iron which sooner or later could lead to anaemia.

In the setting of anaemia, serum ferritin is the most sensitive lab test for iron deficiency anaemia.[1]

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.

[edit] Cardiology diagnostic test

Normal blood levels:

Male: 12-300ng/mL
Female: 12-150ng/mL
Cost: $US 85
How to lower/raise: avoid or eat foods rich in iron: eggs, liver, red meat, soy products

source: Beyond Cholesterol, Julius Torelli MD, 2005 ISBN 0-312-34863-0 p.84

[edit] References

  1. ^ Guyatt G, Patterson C, Ali M, Singer J, Levine M, Turpie I, Meyer R (1990). "Diagnosis of iron-deficiency anemia in the elderly.". Am J Med 88 (3): 205-9. PMID 2178409.

[edit] See also