The glutamate receptor of the Qp-type activates protein kinase C and is regulated by protein kinase C.
Neurosci Lett
; 109(1-2): 146-51, 1990 Feb 05.
Article
in En
| MEDLINE
| ID: mdl-2156190
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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein Kinase C
/
Receptors, Neurotransmitter
/
Corpus Striatum
Limits:
Animals
Language:
En
Journal:
Neurosci Lett
Year:
1990
Document type:
Article
Affiliation country:
France