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Iron transport ability of the Slc39a (ZIP) family of metal‐ion transporters
Author(s) -
Zhang Wei,
Knutson Mitchell
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.641.24
Subject(s) - transporter , chemistry , zinc , dmt1 , biochemistry , ferric , hek 293 cells , ascorbic acid , metal , biophysics , microbiology and biotechnology , biology , inorganic chemistry , gene , food science , organic chemistry
Mammalian ZIP proteins represent a family of 14 transmembrane metal‐ion transporters that have been characterized mainly by their ability to transport zinc. Recently, we have found that two ZIP family members, Zip14 and Zip8, are able to mediate the cellular uptake of iron in addition to zinc. The aim of the present study was to assess the iron transport ability of the 12 other mammalian ZIP proteins. HEK 293T cells were transfected with ZIP protein‐encoding cDNAs, and iron ( 59 Fe) uptake from ferric citrate was assessed. Expression of the ZIPs was confirmed by quantitative RT‐PCR. Among these ZIP proteins, we found that only Zip2 overexpression was able to enhance the cellular uptake of iron. However unlike iron uptake by Zip14, iron transport by Zip2 was not enhanced by the addition of L‐ascorbic acid and was not inhibited by potassium ferricyanide, indicating that iron reduction is not required prior to transport via Zip2. These studies suggest that Zip2 can transport iron, which may contribute to the altered iron homeostasis previously reported in Zip2 knockout mice (Peters et al., Genesis. 2007). Funded by NIH. Grant Funding Source : NIH