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Vol. 56, Issue 5, 1025-1030, November 1999
Department of Psychopharmacology, Institut de Recherches Servier,
Croissy (Paris), France
The mitogen-activated protein kinase (MAPK) cascade is stimulated by
both receptor tyrosine kinases and G protein-coupled receptors. We show
that recombinant human dopamine D3 receptors expressed in
Chinese hamster ovary cells transiently activate MAPK via pertussis
toxin-sensitive Gi and/or Go proteins. The involvement of
D3 receptors was confirmed by use of the D3
agonists PD 128,907 and (+)-7-hydroxy-2-dipropylaminotetralin, which
mimicked the response to dopamine (DA). Furthermore, haloperidol
and the selective D3 receptor antagonists S 14297 and GR
218,231 attenuated DA-induced MAPK activation; however, when tested
alone, S 14297 weakly stimulated MAPK activity, suggesting partial
agonist activity. The transduction mechanisms by which hD3
receptors activate MAPK were explored with specific kinase inhibitors.
Genistein and lavendustin A, inhibitors of tyrosine kinase activity,
did not reduce DA-induced MAPK activation. In contrast, PD 98059, an
inhibitor of MAPK kinase, and Ro 31-8220 and Gö 6983, inhibitors
of protein kinase C (PKC), blocked DA-induced MAPK activation.
However, MAPK activation was insensitive to PKC down-regulation by
phorbol esters, indicating the involvement of an "atypical" PKC.
Furthermore, MAPK activation involved phosphatidylinositol 3-kinase
inasmuch as its inhibition by LY 294002 and wortmannin reduced
DA-induced MAPK activation. In conclusion, this study demonstrates that
stimulation of hD3 receptors activates MAPK. This action is
mediated via an atypical isoform of PKC, possibly involving cross-talk
with products of phosphatidylinositol 3-kinase activation.
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