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Activation of High‐Affinity Uptake of Glutamate by Phorbol Esters in Primary Glial Cell Cultures
Author(s) -
Casado Mariano,
Zafra Francisco,
Aragón Carmen,
Giménez Cecilio
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb08278.x
Subject(s) - protein kinase c , glutamate receptor , activator (genetics) , neuroglia , diacylglycerol kinase , astrocyte , microbiology and biotechnology , biochemistry , biology , protein kinase a , chemistry , kinase , receptor , endocrinology , central nervous system
The effects of 12‐ O ‐tetradecanoylphorbol 13‐acetate (TPA), a potent activator of protein kinase C, on high‐affinity Na + ‐dependent glutamate transport were investigated in primary cultures of neurons and glial cells from rat brain cortex. Incubation of glial cells with TPA led to concentration‐ and time‐dependent increases in the glutamate transport that could be completely suppressed by the addition of the protein kinase C (PKC) inhibitor 1‐(5‐isoquinolinylsulfonyl)‐2‐methylpiperazine. The TPA effects could be mimicked by oleoylacetylglycerol and by the diacylglycerol kinase inhibitor R59022. The effects of TPA were potentiated by the Ca 2+ ionophore A23187. Under the chosen experimental conditions TPA had no effect on glutamate transport in neurons. We conclude that PKC activates the sodium‐dependent high‐affinity glutamate transport in glial cells and that it has dissimilar effects on neurons and glial cells.