Transport of tyrosine, phenylalanine, tryptophan and glycine in neuroblastoma clones.

— Amino acid transport was studied in three neuroblastoma clones, N-TD6, which synthesizes norepinephrine, N-T16, which synthesizes small amounts of serotonin, and N-S20Y, which synthesizes acetylcholine. All three clones exhibited high-affinity saturable transport systems for tyrosine, phenylalanine, tryptophan and glycine as well as systems unsaturated at amino acid concentrations of 1 mM in the external medium. Tyrosine, phenylalanine and tryptophan enter all three clones by rapidly exchanging transport systems which appear to be relatively insensitive to lowered external [Na+] or to the presence of 2,4-dinitrophenol (DNP). Glycine uptake was slower and was much more sensitive to lowered external [Na+] and to the presence of DNP in the medium. Glycine transport in N-T16 cells was decreased more markedly at low temperature than was transport of the three aromatic amino acids. Km and Vmax values found for saturable transport of tyrosine, phenylalanine and tryptophan were sufficiently low to suggest that, if similar amino acid transport systems exist in neuronal membranes, and if amino acid levels in brain extracellular fluid are similar to levels in plasma, such systems may serve, in conjunction with transport systems in cerebral capillaries, to limit the entry of amino acids into brain cells when blood amino levels are near the normal physiological range.