DMT1 and iron transport

被引:197
|
作者
Yanatori, Izumi [1 ]
Kishi, Fumio [2 ]
机构
[1] Stanford Univ, Dept Biochem, Sch Med, 279 Campus Dr, Stanford, CA 94305 USA
[2] Yamaguchi Prefectural Govt, Hagi Publ Hlth & Welf Ctr, 531-1 Emukai, Hagi, Yamaguchi 7580041, Japan
关键词
Divalent metal transporter 1 (DMT1); Iron; Iron chaperone; Isoform; RNA-BINDING PROTEINS; MOLECULAR-MECHANISMS; UNTRANSLATED REGION; NATURAL-RESISTANCE; ZINC-TRANSPORTER; LATE ENDOSOMES; HEME; EXPRESSION; IDENTIFICATION; CHAPERONE;
D O I
10.1016/j.freeradbiomed.2018.07.020
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Many past and recent advances in the field of iron metabolism have relied upon the discovery of divalent metal transporter 1, DMT1 in 1997. DMT1 is the major iron transporter and contributes non-heme iron uptake in most types of cell. Each DMT1 isoform exhibits different expression patterns in cell-type specificity and distinct subcellular distribution, which enables cells to uptake both transferrin-bound and non-transferrin-bound irons efficiently. DMT1 expression is regulated by iron through the translational and degradation pathways to ensure iron homeostasis. It is considered that mammalian iron transporters including DMT1 cannot transport ferric iron but ferrous iron. Being reduced to ferrous state is likely to damage cells and tissues through the production of reactive oxygen species. Recently, iron chaperones have been identified, which can provide an answer to how ferrous iron is transported safely in cytosol. We summarize DMT1 expression depending on the types of cell or tissue and the function and mechanism of one of the iron chaperones, PCBP2.
引用
收藏
页码:55 / 63
页数:9
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