Transport of glutamine inXenopus laevis oocytes: Relationship with transport of other amino acids

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Abstract
Summary We have investigated transport of the amino acid glutamine across the surface membranes of prophase-arrestedXenopus laevis oocytes. Glutamine accumulation was linear with time for 30 min; it was stereospecific with aK m of 0.12±0.02mm andV max of 0.92±0.17 pmol/oocyte · min forl-glutamine. Transport ofl-glutamine was Na+-dependent, the cation not being replaceable with Li+, K+, choline, tris(hydroxymethyl)-aminomethane (Tris), tetramethylammonium (TMA) or N-methyld-glucamine NMDG); external Cl− appeared to be necessary for full activation of Na+-dependent glutamine transport. Two external Na+ may be required for the transport of one glutamine molecule.l-glutamine transport (at 50 μm glutamine) was inhibited by the presence of other amino acids:l-alanine,d-alanine,l-leucine,l-asparagine andl-arginine (about 60% inhibition at 1mm);l-histidine,l-valine and glycine (25 to 40% inhibition at 1mm);l-serine,l-lysine,l-phenylalanine andl-glutamate (45 to 55% inhibition at 10mm). N-methylaminoisobutyric acid (meAIB) had no effect at 10mm, but 2-aminobicyclo[2,2,1]heptane-2-carboxylic acid (BCH) inhibited Na+/glutamine transport by about 50% at 10mm.l-glutamine was a competitive inhibitor of the Na+-dependent transport ofl-alanine,d-alanine andl-arginine; this evidence is consistent with the existence of a single system transporting all four amino acids. Glutamine uptake in oocytes appears to be catalyzed by a transport system distinct from the cotransport Systems A, ASC, N and Gly, although it resembles System B0,+.