Transepithelial Taurine Transport in Caco-2 Cell Monolayers

Transepithelial Taurine Transport in Caco-2 Cell Monolayers Here we characterized transepithelial taurine transport in monolayers of cultured human intestinal Caco-2 cells by analyzing kinetic apical and basolateral uptake and efflux parameters. Basolateral uptake was Na+- and Cl−- dependent and was inhibited by β-amino acids. Uptake by this membrane showed properties similar to those of the apical TauT system. In both membranes, taurine uptake fitted a model consisting of a non-saturable plus a saturable component, with a higher half-saturation constant and transport capacity at the apical membrane (K m, 17.1 μmol/L; V max, 28.4 pmol·cm−2·5 min−1) than in the basolateral domain (K m, 9.46 μmol/L; V max, 5.59 pmol·cm−2·5 min−1). The non-saturable influx component, estimated in the absence of Na+ and Cl−, showed no significant differences between apical and basolateral membranes (K D, 89.2 and 114.7 nL·cm−2 · 5 min−1, respectively). Taurine efflux from the cells is a diffusive process, as shown in experiments using preloaded cells and in trans-stimulation studies (apical K D,72.7 and basolateral K D, 50.1 nL·cm−2·5 min−1). Basolateral efflux rates were significantly lower than passive influx rates. We conclude that basolateral taurine uptake in Caco-2 cells is mediated by a transport mechanism that shares some properties with the apical system TauT. Moreover, calculation of unidirectional and transepithelial taurine fluxes reveals that apical influx of this amino acid is higher than basolateral efflux rates, thereby enabling epithelial cells to accumulate taurine against a concentration gradient. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Transepithelial Taurine Transport in Caco-2 Cell Monolayers

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Publisher
Springer-Verlag
Copyright
Copyright © 2005 by Springer Science+Business Media, Inc.
Subject
Life Sciences; Human Physiology; Biochemistry, general
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-005-0750-y
Publisher site
See Article on Publisher Site

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