Functional properties of transfected human DMT1 iron transporter

Mark T. Worthington, Lauren Browne, Emily H. Battle, Roger Qi Luo

Research output: Contribution to journalArticlepeer-review

Abstract

Recently, mutation of the DMT1 gene has been discovered to cause ineffective intestinal iron uptake and abnormal body iron metabolism in the anemic Belgrade rat and mk mouse. DMT1 transports first-series transition metals, but only iron turns on an inward proton current. The process of iron transport was studied by transfection of human DMT1 into the COS-7 cell line. Native and epitope-tagged human DMT1 led to increased iron uptake. The human gene with the Belgrade rat mutation was found to have one-fifth of the activity of the wild-type protein. The pH optimum of human DMT1 iron uptake was 6.75, which is equivalent to the pH of the duodenal brush border. The transporter demonstrates uptake without saturation from 0 to 50 μM iron, recapitulating earlier studies of isolated intestinal enterocytes. Diethylpyrocarbonate inhibition of iron uptake in DMT1-transfected cells suggests a functional role for histidine residues. Finally, a model is presented that incorporates the selectivity of the DMT1 transporter for transition metals and a potential role for the inward proton current.

Original languageEnglish (US)
Pages (from-to)G1265-G1273
JournalAmerican Journal of Physiology - Gastrointestinal and Liver Physiology
Volume279
Issue number6 42-6
DOIs
StatePublished - 2000

Keywords

  • Intestinal iron transporter
  • Iron uptake

ASJC Scopus subject areas

  • Physiology
  • Hepatology
  • Gastroenterology
  • Physiology (medical)

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