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L-Alanine absorption in human intestinal Caco-2 cells driven by the proton electrochemical gradient by D. T. Thwaites; G. T. A. McEwan; C. D. A. Brown; B. H. Hirst; N. L. Simmons is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is L-Alanine absorption in human intestinal Caco-2 cells driven by the proton electrochemical gradient about?

In human Caco-2 intestinal epithelial layers, L-alanine absorption can be energized by a proton gradient across the brush-border membrane. Acidification of the apical medium, even in Na(+)-free media, is associated with a saturable net transepithelial absorption of L-alanine. L-Alanine transport causes cytosolic acidification consistent with proton/amino acid symport. L-Alanine transport in Na(+)-free media is rheogenic, stimulating an inward short-circuit current in voltage-clamped epithelial monolayers. By measurement of rapid L-alanine influx across the apical membrane, L-alanine-stimulated inward short-circuit current and intracellular acidification in the same cell batch, we estimate L-alanine/proton stoichiometry to be 1:0.62 +/- 0.25 (SD) (short-circuit current) or 1:0.73 +/- 0.19 (intracellular acidification). From competition studies, it is likely that L-proline, alpha-aminoisobutyric acid, and beta-alanine, but not L-valine and L-serine, are substrates for proton-linked, substrate transport in the brush border of Caco-2 cells.

Who reads L-Alanine absorption in human intestinal Caco-2 cells driven by the proton electrochemical gradient?

Author

D. T. Thwaites; G. T. A. McEwan; C. D. A. Brown; B. H. Hirst; N. L. Simmons

Publisher

Springer; Springer-Verlag; Springer Verlag; Springer Science and Business Media LLC (ISSN 0022-2631)

Published

1994

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)