| Literature DB >> 21437029 |
Abstract
Human iron transporters manage iron carefully because tissues need iron for critical functions, but too much iron increases the risk of reactive oxygen species. Iron acquisition occurs in the duodenum via divalent metal transporter (DMT1) and ferroportin. Iron trafficking depends largely on the transferrin cycle. Nevertheless, non-digestive tissues have a variety of other iron transporters that may render DMT1 modestly redundant, and DMT1 levels exceed those needed for the just-mentioned tasks. This review begins to consider why and also describes advances after 2008 that begin to address this challenge.Entities:
Keywords: Divalent metal transporter (DMT1); Ferric reductase; Ferroportin; Iron regulatory protein (IRP); Iron-responsive element (IRE); Isoforms; Transferrin
Year: 2010 PMID: 21437029 PMCID: PMC3040799 DOI: 10.1007/s12263-010-0184-8
Source DB: PubMed Journal: Genes Nutr ISSN: 1555-8932 Impact factor: 5.523