AJP - Cell Physiology, Vol 255, Issue 6 C737-C744, Copyright © 1988 by American Physiological Society

ARTICLES

Low-affinity intestinal L-aspartate transport with 2:1 coupling stoichiometry for Na+/Asp

T. G. Wingrove and G. A. Kimmich
Department of Biophysics, University of Rochester Medical Center, New York 14642.

Epithelial cells isolated from chick small intestine were used to define the ionic and electrical characteristics of a low-affinity (Km = 4.1 mM) L-aspartate transport system. L-Glutamate and D-aspartate, but not D-glutamate, were found to inhibit L-aspartate influx, suggesting that this uptake system has a substrate specificity similar to that previously described for a high-affinity (Km = 16 microM) acidic amino acid transporter in the same cells. Low-affinity uptake is Na+ dependent with a Hill coefficient (n) of 1.4. Intracellular K+ moderately enhances but is not required for aspartate influx, and this response is modulated by changes in intracellular pH. The Na+-dependent uptake of aspartate is electroneutral, as evidenced by insensitivity to pronounced changes in delta psi induced by anion gradients or valinomycin in the presence of K+ gradients. Because the above characteristics can be consistent with several transport models, direct measurement of delta Na+-delta Asp coupling stoichiometry were performed. The coupling ratio was determined to be approximately 2.0. A model for intestinal Na+-dependent L-Asp transport is suggested in which each transport cycle involves inward transfer of 2Na+:1Asp+ and outward transfer of K+ or H+ in a net electroneutral set of events.

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