Abstract— Uptake kinetics of l‐glutamate in cultured, normal glia cells obtained from the brain hemispheres of newborn mice were measured together with the activities of the glutamate metabolizing enzymes, glutamic‐oxaloacetate‐transaminase, glutamate dehydrogenase and glutamine synthetase. During 3 weeks of culturing, the activities of the enzymes rose from low neonatal values toward the levels in the adult brain (206, 12.3 and 25.9 nmol. min−1. mg−1 cell protein for the three enzymes, respectively). The uptake kinetics indicated an unsaturable component together with an uptake following Michaelis‐Menten kinetics with a Km of 220 μm and a Vmax of 7.9 nmol. min−1. mg−1 cell protein. The saturable glutamate uptake was inhibited by d‐glutamate, l‐aspartate and α‐aminoadipate whereas l‐glutamine, GABA and glutarate had no effect. The uptake which was Ca2+‐independent had a Km for sodium of 18mm and it was stimulated by an increase in the external potassium concentration from 5 to 10 and 25 mm. The results suggest that glia cells are important for the uptake of glutamate from synaptic clefts and for the subsequent metabolism of glutamate.
Journal of Neurochemistry – Wiley
Published: Dec 1, 1977
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