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Na + ‐dependent high affinity uptake of l ‐glutamate in primary cultures of human fibroblasts isolated from three different types of tissue
Author(s) -
Balcar Vladimir J.,
Shen Jie,
Bao Shisan,
King Nicholas J.C.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80382-x
Subject(s) - glutamate receptor , chemistry , microbiology and biotechnology , biochemistry , biology , receptor
Cultured human fibroblasts isolated from embryonic muscle, skin and peripheral nerve tissues were found to accumulate [ 3 H]L‐glutamate by a Na + ‐dependent uptake process strongly inhibited by several glutamate/aspartate analogues including d ‐ and l ‐aspartate, d ‐ and l ‐ thero ‐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 K m 's were 5–20 μM, well within the ‘high affinity’ region. Variations in the capacity (V max ) of [ 3 H] 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.