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Activation of Protein Kinase C by Phorbol Esters and Arachidonic Acid Required for the Optimal Potentiation of Glutamate Exocytosis
Author(s) -
Herrero Immaculada,
MirasPortugal María Teresa,
SánchezPrieto José
Publication year - 1992
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.1471-4159.1992.tb08478.x
Subject(s) - exocytosis , protein kinase c , long term potentiation , arachidonic acid , chemistry , glutamate receptor , protein kinase a , biochemistry , second messenger system , microbiology and biotechnology , biology , kinase , enzyme , secretion , receptor
The effects of arachidonic acid and phorbol esters in the Ca 2+ ‐dependent release of glutamate evoked by 4‐aminopyridine (4‐AP) in rat cerebrocortical synaptosomes were studied. In the absence of arachidonic acid, high concentrations (500 n M ) of 4β‐phorbol dibutyrate (4β‐PDBu) were required to enhance the release of glutamate. However, in the presence of arachidonic acid, low concentrations of 4β‐PDBu (1–50 n M ) were effective in potentiating glutamate exocytosis. This potentiation of glutamate release by phorbol esters was not observed with the methyl ester of arachidonic acid, which does not activate protein kinase C. Moreover, pretreatment of synaptosomes with the protein kinase inhibitor staurosporine also prevented the stimulatory effect by arachidonic acid and phorbol esters. These results suggest that the activation of protein kinase C by both arachidonic acid and phorbol esters may play a role in the potentiation of glutamate exocytosis.