Title: Ferritin
CAS Registry Number: 9007-73-2
Trademarks: Ferrofolin (Schering AG); Ferrol (UCB); Ferrosprint (Pfizer); Ferrostar (Mediolanum); Sanifer (Esseti); Sideros (Sanofi-Synthelabo); Unifer (Tosi)
Literature References: Major iron storage protein; widely distributed in the plant and animal kingdoms. Consists of a 24-subunit protein shell surrounding a crystalline hydrous ferric oxide core. The core may contain up to 4500 Fe3+ ions. The protein shell, apoferritin, has a mol wt of ~445,000. Isoln and crystallization of horse spleen ferritin: V. Laufberger, Bull. Soc. Chim. Biol. 19, 1575 (1937); S. Granick, J. Biol. Chem. 146, 451 (1942). X-ray structural study of apoferritin: P. M. Harrison, J. Mol. Biol. 6, 404 (1963). Review of properties and role in iron metabolism: S. Granick, Chem. Rev. 38, 379-403 (1946); of structure, biosynthesis and function: R. R. Crichton, N. Engl. J. Med. 284, 1413-1422 (1971); P. M. Harrison, T. G. Hoy, "Ferritin" in Inorganic Biochemistry vol. 1, G. L. Eichhorn, Ed. (Elsevier, New York, 1973) pp 253-279; H. N. Munro, M. C. Linder, Physiol. Rev. 58, 317-396 (1978); of applications in clinical medicine: J. W. Halliday, L. W. Powell, Prog. Hematol. 11, 229-266 (1979); of biology: M. Worwood, Blood Rev. 4, 259-269 (1990); of structure and role in iron mineralization: N. D. Chasteen, P. M. Harrison, J. Struct. Biol. 126, 182-194 (1999); of mitochondrial ferritin: J. Drysdale et al., Blood Cells Mol. Dis. 29, 376-383 (2002); of role in dietary iron supplementation: E. C. Theil, Annu. Rev. Nutr. 24, 327-343 (2004).
Properties: Red-brown, water-soluble protein. Forms cubic and orthorhombic crystals.
Use: Tool for the study of protein synthesis and regulatory mechanisms.
Therap-Cat: Hematinic.
Keywords: Hematinic.
Ferrocene Ferrocholinate Ferroglycine Sulfate Ferrosoferric Oxide Ferrous Bisglycinate

Structure of the murine ferritin complex 1lb3[1]
Pfam PF00210
Pfam clan CL0044
InterPro IPR008331
SCOP 1fha
ferritin, light polypeptide
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
Symbol FTH1
Alt. symbols FTHL6
Entrez 2495
HUGO 3976
OMIM 134770
RefSeq NM_002032
UniProt P02794
Other data
Locus Chr. 11 q13
ferritin mitochondrial
Mitochondrial Ferritin.png
Crystallographic structure of mitochondrial ferritin.[2]
Symbol FTMT
Entrez 94033
HUGO 17345
OMIM 608847
RefSeq NM_177478
UniProt Q8N4E7
Other data
Locus Chr. 5 q23.1

Ferritin is a ubiquitous intracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including algae, bacteria, higher plants, and animals. In humans, it acts as a buffer against iron deficiency and iron overload.[3] 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.[4]

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