Anionic amino acid transport systems in isolated basal plasma membrane of human placenta.

The placenta absorbs anionic amino acids from the maternal and fetal circulations but does not significantly transfer these amino acids from mother to fetus. Uptake of L-aspartate and L-glutamate by basal (fetal-facing) plasma membrane vesicles from placental syncytiotrophoblast was stimulated by an inward sodium and an outward potassium gradient. Measurable saturable uptake was entirely sodium dependent and electrogenic. Studies of concentration dependence resolved a high-affinity (microM) system that has characteristics of the X-AG system found in other tissues including the placental microvillous plasma membrane. Uptake of 0.2 microM L-glutamate was inhibited by 2 mM L-glutamate, L-aspartate, D-aspartate, L-cysteate, and L-cysteinesulfinic acid and was uninhibited by 2 mM D-glutamate, L-glutamine, L-alanine, L-serine, L-asparagine, and taurine or by 1 mM methylaminoisobutyric acid. The X-AG system in the two membranes of the placental syncytiotrophoblast may mediate the concentrative uptake of anionic amino acids from the maternal and fetal circulations into the placenta.