Activation of High-Affinity Uptake of Glutamate by Phorbol Esters in Primary Glial Cell Cultures
Version of Record online: 5 OCT 2006
Journal of Neurochemistry
Volume 57, Issue 4, pages 1185–1190, October 1991
How to Cite
Casado, M., Zafra, F., Aragón, C. and Giménez, C. (1991), Activation of High-Affinity Uptake of Glutamate by Phorbol Esters in Primary Glial Cell Cultures. Journal of Neurochemistry, 57: 1185–1190. doi: 10.1111/j.1471-4159.1991.tb08278.x
- Issue online: 5 OCT 2006
- Version of Record online: 5 OCT 2006
- Received October 17, 1990; revised manuscript received February 11, 1991: accepted February 28, 1991.
- Glutamate uptake;
- Phorbol esters;
- Glial cells;
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 Ca2+ 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.