Rapid regulation of divalent metal transporter (DMT1) protein but not mRNA expression by non-haem iron in human intestinal Caco-2 cells

FEBS Lett. 2002 Jan 2;510(1-2):71-6. doi: 10.1016/s0014-5793(01)03225-2.

Abstract

A divalent metal transporter, DMT1, located on the apical membrane of intestinal enterocytes is the major pathway for the absorption of dietary non-haem iron. Using human intestinal Caco-2 TC7 cells, we have shown that iron uptake and DMT1 protein in the plasma membrane were significantly decreased by exposure to high iron for 24 h, in a concentration-dependent manner, whereas whole cell DMT1 protein abundance was unaltered. This suggests that part of the response to high iron involved redistribution of DMT1 between the cytosol and cell membrane. These events preceded changes in DMT1 mRNA, which was only decreased following 72 h exposure to high iron.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Caco-2 Cells
  • Carrier Proteins / metabolism
  • Cation Transport Proteins / genetics
  • Cation Transport Proteins / metabolism*
  • Cations, Divalent
  • Cell Differentiation
  • Dose-Response Relationship, Drug
  • Down-Regulation*
  • Gene Expression / drug effects*
  • Heme
  • Humans
  • Intestines / cytology
  • Iron / pharmacokinetics*
  • Iron-Binding Proteins*
  • Metals / metabolism
  • Microfilament Proteins / metabolism
  • RNA, Messenger / biosynthesis*
  • Receptors, Transferrin / metabolism
  • Time Factors

Substances

  • Carrier Proteins
  • Cation Transport Proteins
  • Cations, Divalent
  • Iron-Binding Proteins
  • Metals
  • Microfilament Proteins
  • RNA, Messenger
  • Receptors, Transferrin
  • solute carrier family 11- (proton-coupled divalent metal ion transporters), member 2
  • villin
  • Heme
  • Iron