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Iron absorption by CaCo 2 cells cultivated in serum‐free medium as in vitro model of the human intestinal epithelial barrier
Author(s) -
Halleux Christine,
Schneider YvesJacques
Publication year - 1994
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041580104
Subject(s) - enterocyte , paracellular transport , caco 2 , apical membrane , transferrin , ferritin , transcytosis , chemistry , biophysics , in vitro , biochemistry , absorption (acoustics) , transcellular , microbiology and biotechnology , biology , cell , endocytosis , small intestine , membrane , physics , acoustics , permeability (electromagnetism)
A cell culture system consisting of confluent monolayer of human enterocyte‐like CaCo 2 cells, cultivated in a serum‐free nutritive medium, on microporous synthetic membranes has been used as an in vitro model of the intestinal epithelial barrier. The uptake of 55 ferric citrate, as well as the transepithelial passage from the apical to the basolateral pole, have been studied. CaCo 2 cells accumulate iron in a time‐ and concentration‐dependent process, largely specific from the apical pole. When 55 ferric citrate is added at the apical pole, radioiron appears at the basal pole and the clearance rate is ∼four times higher than in the opposite direction; the amounts of 55 Fe increase with the concentration in iron citrate and the duration of incubation. At least two concurrent mechanisms could be involved in iron absorption across monolayers of CaCo 2 cells. A first route would correspond to a paracellular passage of the metal from the apical to the basal pole. The second route would involve a selective intake of iron at the apical pole and could require a reduction of ferric iron, prior to the entry. Iron accumulated by the cells would, for a minor part, be stored within ferritin, whereas the major part would be excreted at the basolateral pole, either as low molecular weight material of undetermined chemical composition but from which iron is easily mobilized by apotransferrin or associated with neosynthesized apotransferrin. Vesicular transport and protein synthesis seem to be required. © 1994 Wiley‐Liss, Inc.