AJP - Renal Journal of Neurophysiology
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Am J Physiol Renal Physiol 255: F1249-F1255, 1988;
0363-6127/88 $5.00
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AJP - Renal Physiology, Vol 255, Issue 6 1249-F1255, Copyright © 1988 by American Physiological Society

ARTICLES

LLC-PK1 cells express Na+-lactate cotransport in apical membranes after confluency

C. Poustis-Delpont, R. Mengual and P. Sudaka
Laboratoire de Biochimie, Faculte de Medecine, Nice, France.

L-[3H]lactate uptake was characterized in LLC-PK1 cell apical membrane vesicles obtained by intensive culture on microcarrier beads. The apical membrane preparation technique involved MgCl2 precipitation. Na+-dependent L-[3H]lactate uptake was present only after confluency; its appearance paralleled the subcellular localization of aminopeptidase in apical membranes. L-[3H]lactate uptake was Na+-dependent and electrogenic. Only the Na+-dependent component of L-[3H]lactate uptake was saturable with one family of independent carriers. The apparent affinity constant was 1.1 +/- 0.25 mM and the apparent maximal velocity was 29 +/- 3 nmol.mg-1.min-1. The Na+-lactate cotransport stoichiometry was 2 Na+ for 1 lactate. The specificity of the L-lactate transport system was compatible with that of the monocarboxylic acid pathway described previously in brush-border membranes of kidney cortex and discrete from the tricarboxylic acid carrier, the D-glucose transporter, and the general pathway for anions. The LLC-PK1 cell line appears to be a useful tool for study of the regulation of L-lactate uptake and biosynthesis of the renal monocarboxylic acid transporter.


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