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Am J Physiol Gastrointest Liver Physiol 279: G366-G373, 2000;
0193-1857/00 $5.00
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Vol. 279, Issue 2, G366-G373, August 2000

EAAT1 is involved in transport of L-glutamate during differentiation of the Caco-2 cell line

Agnès Mordrelle1, Eric Jullian2, Cyrille Costa1, Estelle Cormet-Boyaka1, Robert Benamouzig1, Daniel Tomé1, and Jean-François Huneau1

1 Institut National de la Recherche Agronomique, Laboratoire de Nutrition Humaine et Physiologie Intestinale, Institut National Agronomique Paris-Grignon, 75231 Paris Cedex 05; and 2 Laboratoire d'Histologie-Embryologie, Faculté de Médecine Cochin, 75014 Paris, France

Little is known concerning the expression of amino acid transporters during intestinal epithelial cell differentiation. The transport mechanism of L-glutamate and its regulation during the differentiation process were investigated using the human intestinal Caco-2 cell line. Kinetic studies demonstrated the presence of a single, high-affinity, D-aspartate-sensitive L-glutamate transport system in both confluent and fully differentiated Caco-2 cells. This transport was clearly Na+ dependent, with a Hill coefficient of 2.9 ± 0.3, suggesting a 3 Na+-to-1 glutamate stoichiometry and corresponding to the well-characterized XA,G- system. The excitatory amino acid transporter (EAAT)1 transcript was consistently expressed in the Caco-2 cell line, whereas the epithelial and neuronal EAAT3 transporter was barely detected. In contrast with systems B0 and y+, which have previously been reported to be downregulated when Caco-2 cells stop proliferating, L-glutamate transport capacity was found to increase steadily between day 8 and day 17. This increase was correlated with the level of EAAT1 mRNA, which might reflect an increase in EAAT1 gene transcription and/or stabilization of the EAAT1 transcript.

glutamate transport; intestinal epithelium


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