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  • Title: Na(+)-dependent high affinity uptake of L-glutamate in primary cultures of human fibroblasts isolated from three different types of tissue.
    Author: Balcar VJ, Shen J, Bao S, King NJ.
    Journal: FEBS Lett; 1994 Feb 14; 339(1-2):50-4. PubMed ID: 7906230.
    Abstract:
    Cultured human fibroblasts isolated from embryonic muscle, skin and peripheral nerve tissues were found to accumulate [3H]L-glutamate by a Na(+)-dependent uptake process strongly inhibited by several glutamate/aspartate analogues including D- and L-aspartate, D- and L-threo-3-hydroxyaspartate and L-trans-pyrrolidine-2,4-dicarboxylate but not D-glutamate. It was also reduced by elevated concentrations of K+, Rb+ and Cs+. The values of Km's were 5-20 microM, well within the 'high affinity' region. Variations in the capacity (Vmax) of [3H]L-glutamate uptake did not correlate with the origin (muscle, skin or nerve tissue) of the fibroblasts. The uptake characteristics suggest that it is mediated by a transport system similar to that commonly observed only in brain tissue.
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