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Research ArticleArticle

Expression of the GLT-1 Subtype of Na+-Dependent Glutamate Transporter: Pharmacological Characterization and Lack of Regulation by Protein Kinase C

Jue Tan, Olga Zelenaia, Dana Correale, Jeffrey D. Rothstein and Michael B. Robinson
Journal of Pharmacology and Experimental Therapeutics June 1999, 289 (3) 1600-1610;
Jue Tan
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Olga Zelenaia
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Dana Correale
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Jeffrey D. Rothstein
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Michael B. Robinson
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Abstract

Several subtypes of Na+-dependent glutamate transporters have been pharmacologically differentiated in brain tissues. Five distinct cDNA clones that express Na+-dependent glutamate transport activity have been isolated. One goal of the current study was to compare the pharmacological properties of the rat GLT-1 subtype of transporter to those identified previously using rat brain tissues. To accomplish this goal, GLT-1 was stably transfected into two different cell lines that express low levels of endogenous transport activity (MCB and L-M (TK-)). Several clones stably transfected with GLT-1 were isolated. In each cell line, Na+-dependent glutamate transport activity was saturable with similarKm values (19 and 37 μM). The pharmacological properties of GLT-1-mediated transport in these cell lines paralleled those observed for the predominant pharmacology observed in cortical crude synaptosomes. These data are consistent with other lines of evidence that suggest that GLT-1 may be sufficient to explain most of the Na+-dependent glutamate transport activity in cortical synaptosomes. Although recent studies using HeLa cells have suggested that GLT-1 can be rapidly up-regulated by activation of protein kinase C (PKC), modulation of PKC or phosphatase activity had no effect on GLT-1-mediated activity in these transfected cell lines. To determine if GLT-1 regulation by PKC is cell-specific, HeLa cells, which endogenously express the EAAC1 subtype of transporter, were stably transfected with GLT-1. Although EAAC1-mediated activity was increased by activation of PKC, we found no evidence for regulation of GLT-1. Despite the present findings, GLT-1 activity may be regulated by PKC under certain conditions.

Footnotes

  • Send reprint requests to: Michael B. Robinson, Abramson Pediatric Research Building, Room 502, 34th and Civic Center Blvd., Philadelphia, PA 19104-4318. E-mail:robinson{at}pharm.med.upenn.edu

  • ↵1 This work was supported by National Institutes of Health Grants NS29868 and HD26979 (M.B.R.) and NS36465 (M.B.R., J.D.R.).

  • Abbreviations:
    Bis
    bisindolylmaleimide II
    DHK
    dihydrokainate
    EAA
    excitatory amino acid
    l-AAD
    l-α-aminoadipate
    l-AP3
    l-2-amino-3-phosphonopropionate
    PMA
    phorbol 12-myristate 13-acetate
    PKC
    protein kinase C
    l-trans-PDC
    l-trans-pyrrolidine-2,4-dicarboxylate
    mGluR
    metabotropic glutamate receptor
    DMSO
    dimethyl sulfoxide
    • Received August 26, 1998.
    • Accepted February 16, 1999.
  • The American Society for Pharmacology and Experimental Therapeutics
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Journal of Pharmacology and Experimental Therapeutics: 289 (3)
Journal of Pharmacology and Experimental Therapeutics
Vol. 289, Issue 3
1 Jun 1999
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Research ArticleArticle

Expression of the GLT-1 Subtype of Na+-Dependent Glutamate Transporter: Pharmacological Characterization and Lack of Regulation by Protein Kinase C

Jue Tan, Olga Zelenaia, Dana Correale, Jeffrey D. Rothstein and Michael B. Robinson
Journal of Pharmacology and Experimental Therapeutics June 1, 1999, 289 (3) 1600-1610;

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Research ArticleArticle

Expression of the GLT-1 Subtype of Na+-Dependent Glutamate Transporter: Pharmacological Characterization and Lack of Regulation by Protein Kinase C

Jue Tan, Olga Zelenaia, Dana Correale, Jeffrey D. Rothstein and Michael B. Robinson
Journal of Pharmacology and Experimental Therapeutics June 1, 1999, 289 (3) 1600-1610;
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