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    Identification of an iron-hepcidin complex

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    Authors
    Farnaud, Sébastien
    Rapisarda, Chiara
    Bui, Tam
    Drake, Alex F.
    Cammack, Richard
    Evans, Robert W
    Affiliation
    University of Westminster
    Issue Date
    2008-08-01
    Subjects
    hepcidins
    iron chemistry
    
    Metadata
    Show full item record
    Abstract
    Following its identification as a liver-expressed antimicrobial peptide, the hepcidin peptide was later shown to be a key player in iron homoeostasis. It is now proposed to be the 'iron hormone' which, by interacting with the iron transporter ferroportin, prevents further iron import into the circulatory system. This conclusion was reached using the corresponding synthetic peptide, emphasizing the functional importance of the mature 25-mer peptide, but omitting the possible functionality of its maturation. From urine-purified native hepcidin, we recently demonstrated that a proportion of the purified hepcidin had formed iron-hepcidin complexes. This interaction was investigated further by computer modelling and, based on the sequence similarity of hepcidin with metallothionein, a three-dimensional model of hepcidin, containing one atom of iron, was constructed. To characterize these complexes further, the interaction with iron was analysed using different spectroscopic methods. Monoferric hepcidin was identified by MS, as were possibly other complexes containing two and three atoms of iron respectively, although these were present only in minor amounts. UV/visible absorbance and CD studies identified the iron-binding events which were facilitated at a physiological pH. EPR spectroscopy identified the ferric state of the bound metal, and indicated that the iron-hepcidin complex shares some similarities with the rubredoxin iron-sulfur complex, suggesting the presence of Fe(3+) in a tetrahedral sulfur co-ordination. The potential roles of iron binding for hepcidin are discussed, and we propose either a regulatory function in the maturation of pro-hepcidin into active hepcidin or as the necessary link in the interaction between hepcidin and ferroportin.
    Citation
    Farnaud, S., et al (2008) 'Identification of an iron-hepcidin complex' Biochem. J. 413 (3):553-7
    Publisher
    Portland Press
    Journal
    The Biochemical journal
    URI
    http://hdl.handle.net/10547/593392
    DOI
    10.1042/BJ20080406
    PubMed ID
    18447830
    Additional Links
    http://www.biochemj.org/content/413/3/553.long
    Type
    Article
    Language
    en
    ISSN
    1470-8728
    ae974a485f413a2113503eed53cd6c53
    10.1042/BJ20080406
    Scopus Count
    Collections
    Cell and Cryobiology Research Group

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