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22-AUGUST-2008 06:13:22 - Ferritin Structure of the ferritin complex ferritin, light polypeptide Identifiers Symbol FTL Entrez 2512 HUGO 3999 OMIM 134790 RefSeq NM_000146 UniProt P02792 Other data Locus Chr. 19 q13.3-13.4 ferritin, heavy polypeptide 1 Identifiers Symbol FTH1 Alt. Symbols FTHL6 Entrez 2495 HUGO 3976 OMIM 134770 RefSeq NM_002032 UniProt P02794 Other data Locus Chr. 11 q13 ferritin mitochondrial Identifiers Symbol FTMT Entrez 94033 HUGO 17345 OMIM 608847 RefSeq NM_177478 UniProt Q8N4E7 Other data Locus Chr. 5 q23.1 This article requires authentication or verification by an expert. Please assist in recruiting an expert or improve this article yourself. This article has been tagged since May 2008. 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 1 Description 2 Function 3 Diagnostic uses 4 See also 5 References 6 External links Description Ferritin, a 450 kDa protein consisting of 24 subunits is present in every cell type. In vertebrates, these subunits are both the light L and the heavy H type with an apparent 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. The resulting particle is similar to the mineral ferrihydrite. 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. Function Free iron is toxic to cells as it acts as a catalyst in the formation of free radicals from reactive oxygen species via the Fenton Reaction.1 Hence organisms have evolved 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 reticuloendothelial 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. Diagnostic uses Serum ferritin levels are measured in patients as part of the iron studies workup for anemia and for restless legs syndrome. The ferritin levels measured have a direct correlation with the total amount of iron stored in the body except in certain circumstances, such as anemia of chronic disease. 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 could lead to anemia. Low ferritin levels 50 ng/mL have been associated with symptoms of restless legs syndrome even in the absence of anemia2. Normal blood levels are 30-300 ng/mL for males and 15-200 ng/mL for females. according to clinical medicine by Kumar Clark page 428 34 In the setting of anemia, serum ferritin is the most sensitive lab test for iron deficiency anemia.5 Ferritin is also used as a marker for iron overload disorders, such as hemochromatosis 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. Ferritin can be elevated during periods of acute malnourishment.6 In a certain study in Paris, France, the level of iron in the blood measured by ordering a ferritin serum test has been connected to ADHD in children. Specifically, the lower the iron level, the more severe the ADHD symptoms.7 See also Bacterioferritin Transferrin Ferritin light chain References ^ Orino K, Lehman L, Tsuji Y, Ayaki H, Torti SV, Torti FM 2001. Ferritin and the response to oxidative stress. Biochem J 357 1: 241-7. doi:10.1042/0264-6021:3570241. PMID 11415455. ^ Meir H. Kryger et al. 2002. Low body stores of iron and restless legs syndrome: a correctable cause of insomnia in adolescents and teenagers. Sleep Medicine 3: 127-132. ^ Beyond Cholesterol, Julius Torelli MD, 2005 ISBN 0-312-34863-0 p.84 ^ MedlinePlus Medical Encyclopedia: Ferritin ^ 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. doi:10.1016/0002-93439090143-2. PMID 2178409. ^ Kennedy A, Kohn M, Lammi A, Clarke S 2004. Iron status and haematological changes in adolescent female inpatients with anorexia nervosa. J Paediatr Child Health 40 8: 430-2. doi:10.1111/j.1440-1754.2004.00432.x. PMID 15265182. ^ Greene MD, Alan 2004-12-17. Iron and ADHD. Retrieved on 2008-08-19. External links http://sickle.bwh.harvard.edu/iron_transport.html v d e Carrier proteins, metalloproteins: iron-binding proteins heme Ferritin Bacterioferritin - Lactoferrin - Transferrin nonheme Hemerythrin - Inositol oxygenase - Iron-sulfur protein - Lipoxygenase - Tyrosine hydroxylase Retrieved from http://en..org/wiki/Ferritin Categories: Genes on chromosome 19 | Genes on chromosome 11 | Genes on chromosome 5 | Blood tests | Chemical pathology | Acute phase proteinsHidden categories: Protein pages needing a picture | Pages needing expert attention | articles needing factual verification since May 2008 Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page Languages Deutsch Español Français Italiano Nederlands ‪Norsk bokmÃ¥l‬ Polski Português SlovenÅ¡Ä?ina Suomi Svenska This page was last modified on 22 August 2008, at 22:02. of the GNU Free Documentation License. ® , Inc., a U.S.
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