Abstract:
:Uptake of L-[3H]glutamate by monolayers of fibroblasts cultured from human embryonic skin has been studied in the presence of several nonradioactive structural analogs of glutamate and aspartate. Results have suggested that the structural specificites of glutamate transporters in cultured human fibroblasts are similar to those of glutamate transporters in the mammalian brain. Only subtle differences have been detected: in the mammalian cerebral cortex, enantiomers of threo-3-hydroxyaspartate are almost equipotent as inhibitors of L-[3H]glutamate uptake while, in human fibroblasts, the D-isomer has been found to be an order of magnitude less potent than the corresponding L-isomer. Kinetic analysis of a model in which substrates are recognized by the glutamate transporter binding site(s) as both alpha- and beta-amino acids indicated that such a mechanism cannot explain the apparent negative cooperativity characterizing the effects of D- and L-aspartate. Molecular modeling has been used to estimate the optimum conformation of L-glutamate as it interacts with the transporter(s). Flow cytometry has indicated that all fibroblasts in culture express at least moderate levels of four glutamate transporters cloned from human brain. Small subpopulations (< 3%) of cells, however, were strongly labeled with antibodies against EAAT1 (GLAST) and EAAT2 (GLT-1) transporters. We conclude that these two transporters--known to be strongly expressed in brain tissue--can be principally responsible for the "high affinity" transport of glutamate also in nonneural cells.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Cooper B,Chebib M,Shen J,King NJ,Darvey IG,Kuchel PW,Rothstein JD,Balcar VJdoi
10.1006/abbi.1998.0626subject
Has Abstractpub_date
1998-05-15 00:00:00pages
356-64issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(98)90626-9journal_volume
353pub_type
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