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Am J Physiol Lung Cell Mol Physiol 279: L911-L915, 2000;
1040-0605/00 $5.00
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Vol. 279, Issue 5, L911-L915, November 2000

Selectivity properties of a Na-dependent amino acid cotransport system in adult alveolar epithelial cells

Xinpo Jiang1, David H. Ingbar2, and Scott M. O'Grady1

Departments of 1 Physiology and 2 Medicine, University of Minnesota, Minneapolis, Minnesota 55455

We investigated the amino acid specificity of a Na-dependent amino acid cotransport system that contributes to transepithelial Na absorption in the apical membrane of cultured adult rat alveolar epithelial cell monolayers. Short-circuit current was increased by basic, uncharged polar, and nonpolar amino acids but not by L-aspartic acid or L-proline. EC50 values for L-lysine and L-histidine were 0.16 and 0.058 mM, respectively. The L-lysine-stimulated short-circuit current was Na dependent, with a concentration causing a half-maximal stimulation by Na of 44.24 mM. L-Serine, L-glutamine, and L-cysteine had EC50 values of 0.095, 0.25, and 0.12 mM, respectively. L-Alanine had the highest affinity, with an EC50 of 0.027 mM. We conclude that monolayer cultures of adult rat alveolar epithelial cells possess a broad-specificity Na-dependent amino acid cotransport system with properties consistent with system B0,+. We suggest that this cotransport system plays a critical role in recycling of constituent amino acids that make up glutathione, thus ensuring efficient replenishment of this important antioxidant within the alveolar fluid.

sodium absorption; ion transport; hyperoxia; antioxidant; system B0,+


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