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Ferroportin - Wikipedia, the free encyclopedia

Ferroportin

From Wikipedia, the free encyclopedia


Solute carrier family 40 (iron-regulated transporter), member 1
Identifiers
Symbol(s) SLC40A1; FPN1; HFE4; IREG1; MST079; MSTP079; MTP1; SLC11A3
External IDs OMIM: 604653 MGI1315204 HomoloGene40959
Orthologs
Human Mouse
Entrez 30061 53945
Ensembl ENSG00000138449 ENSMUSG00000025993
Uniprot Q9NP59 Q3TJ33
Refseq NM_014585 (mRNA)
NP_055400 (protein)
NM_016917 (mRNA)
NP_058613 (protein)
Location Chr 2: 190.13 - 190.15 Mb Chr 1: 45.85 - 45.87 Mb
Pubmed search [1] [2]

Ferroportin is a transmembrane protein that transports iron from the inside of a cell to the outside of it. It is found on the surface of cells that store or transport iron, including:

Recent research suggests that ferroportin is inhibited by hepcidin, which therefore is the "master regulator" of human iron metabolism. Hepcidin binds to ferroportin, and results in the internalisation of ferroportin within the cell. This results in retention of iron within the cell, and a reduction in iron levels within the plasma. This is part of the mechanism that causes anaemia of chronic disease; hepcidin is released from the liver in response to inflammatory cytokines, namely interleukin-6, which results in an increased hepcidin concentration and a consequent decrease in plasma iron levels.

Contents

[edit] Clinical significance

Ferroportin can be associated with African iron overload.

[edit] References

[edit] Further reading

  • Schimanski LM et al. (2005). "In vitro functional analysis of human ferroportin (FPN) and hemochromatosis-associated FPN mutations.". Blood 105 (10): 4096–4102. 
  • Pietrangelo A (2004). "The ferroportin disease.". Blood Cells Mol. Dis. 32 (1): 131–8. PMID 14757427. 
  • Robson KJ, Merryweather-Clarke AT, Cadet E, et al. (2005). "Recent advances in understanding haemochromatosis: a transition state.". J. Med. Genet. 41 (10): 721–30. doi:10.1136/jmg.2004.020644. PMID 15466004. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149. 
  • Donovan A, Brownlie A, Zhou Y, et al. (2000). "Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter.". Nature 403 (6771): 776–81. doi:10.1038/35001596. PMID 10693807. 
  • Abboud S, Haile DJ (2000). "A novel mammalian iron-regulated protein involved in intracellular iron metabolism.". J. Biol. Chem. 275 (26): 19906–12. doi:10.1074/jbc.M000713200. PMID 10747949. 
  • Haile DJ (2000). "Assignment of Slc11a3 to mouse chromosome 1 band 1B and SLC11A3 to human chromosome 2q32 by in situ hybridization.". Cytogenet. Cell Genet. 88 (3-4): 328–9. PMID 10828623. 
  • McKie AT, Marciani P, Rolfs A, et al. (2000). "A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation.". Mol. Cell 5 (2): 299–309. PMID 10882071. 
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. PMID 11076863. 
  • Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.154701. PMID 11230166. 
  • Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing.". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMID 11256614. 
  • Njajou OT, Vaessen N, Joosse M, et al. (2001). "A mutation in SLC11A3 is associated with autosomal dominant hemochromatosis.". Nat. Genet. 28 (3): 213–4. doi:10.1038/90038. PMID 11431687. 
  • Montosi G, Donovan A, Totaro A, et al. (2001). "Autosomal-dominant hemochromatosis is associated with a mutation in the ferroportin (SLC11A3) gene.". J. Clin. Invest. 108 (4): 619–23. PMID 11518736. 
  • Press RD (2002). "Hemochromatosis caused by mutations in the iron-regulatory proteins ferroportin and H ferritin.". Mol. Diagn. 6 (4): 347. PMID 11774199. 
  • Lee PL, Gelbart T, West C, et al. (2003). "A study of genes that may modulate the expression of hereditary hemochromatosis: transferrin receptor-1, ferroportin, ceruloplasmin, ferritin light and heavy chains, iron regulatory proteins (IRP)-1 and -2, and hepcidin.". Blood Cells Mol. Dis. 27 (5): 783–802. doi:10.1006/bcmd.2001.0445. PMID 11783942. 
  • Rolfs A, Bonkovsky HL, Kohlroser JG, et al. (2002). "Intestinal expression of genes involved in iron absorption in humans.". Am. J. Physiol. Gastrointest. Liver Physiol. 282 (4): G598–607. doi:10.1152/ajpgi.00371.2001. PMID 11897618. 
  • Thomas C, Oates PS (2002). "IEC-6 cells are an appropriate model of intestinal iron absorption in rats.". J. Nutr. 132 (4): 680–7. PMID 11925460. 
  • Wallace DF, Pedersen P, Dixon JL, et al. (2002). "Novel mutation in ferroportin1 is associated with autosomal dominant hemochromatosis.". Blood 100 (2): 692–4. PMID 12091366. 
  • Devalia V, Carter K, Walker AP, et al. (2002). "Autosomal dominant reticuloendothelial iron overload associated with a 3-base pair deletion in the ferroportin 1 gene (SLC11A3).". Blood 100 (2): 695–7. doi:10.1182/blood-2001-11-0132. PMID 12091367. 
  • Roetto A, Merryweather-Clarke AT, Daraio F, et al. (2002). "A valine deletion of ferroportin 1: a common mutation in hemochromastosis type 4.". Blood 100 (2): 733–4. PMID 12123233. 

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