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The glutamate receptor of the Qp-type activates protein kinase C and is regulated by protein kinase C.

Abstract：

:In striatal neurons in primary culture quisqualate potently stimulated the formation of inositol phosphates via a metabotropic receptor we recently termed Qp in order to distinguish it from the classical ionotropic quisqualate receptor termed Qi. Here we show that 10 microM of quisqualate activated in a rapid and transient manner protein kinase C as assessed by its translocation from the cytosolic to the membrane fraction. As 10 microM alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA), the Qi specific agonist, was without effect, this translocation was most probably mediated by the Qp receptor. Phorbol 12,13-dibutyrate blocked in a dose-dependent manner the Qp receptor-induced inositol phosphate formation (IC50 = 2 +/- 0.4 nM). The inactive ester 4 alpha-phorbol-12,13-didecanoate was without effect. Very low concentrations of staurosporine completely reversed the phorbol 12,13-dibutyrate-induced blockade (IC50 = 2.2 +/- 1.3 nM). It can therefore be concluded that the Qp receptor is able to activate protein kinase C and that the activity of this metabotropic receptor is regulated by protein kinase C.

journal_name

Neurosci Lett

journal_title

Neuroscience letters

authors

Manzoni OJ,Finiels-Marlier F,Sassetti I,Blockaert J,le Peuch C,Sladeczek FA

doi

10.1016/0304-3940(90)90553-l

subject

Has Abstract

pub_date

1990-02-05 00:00:00

pages

146-51

issue

1-2

eissn

0304-3940

issn

1872-7972

pii

0304-3940(90)90553-L

journal_volume

109

pub_type

杂志文章

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