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Vol. 54, Issue 3, 453-458, September 1998
Laboratory of Molecular Pharmacology, Department of Pharmacology,
MCP-Hahnemann School of Medicine, Allegheny University of the Health
Sciences, Philadelphia, Pennsylvania 19129
We investigated the effects of D1 dopamine receptor
stimulation on the activation of mitogen-activated protein kinases
(MAPKs) in SK-N-MC human neuroblastoma cells. We found that the
D1 dopamine receptor agonist SKF38393 induced similar time-
and dose-related activation of p38 MAPK and c-Jun amino-terminal kinase
(JNK), whereas extracellular signal-regulated kinase activity was not affected by D1 dopamine receptor stimulation. Maximal
stimulation of p38 MAPK and JNK was observed after a 15-min incubation
with 100 µM SKF38393. In contrast, 10 µM
quinpirole, a D2 dopamine receptor agonist, did not
activate p38 MAPK or JNK. Treatment of cells with 10 µM
SCH23390, a D1 dopamine receptor antagonist, significantly
inhibited the activation of both kinases by SKF38393. These results
indicate that activation of the p38 MAPK and JNK signaling pathways is
mediated by dopamine D1 receptors in SK-N-MC neuroblastoma
cells. Furthermore, dibutyryl-cAMP mimicked SKF38393-mediated stimulation of p38 MAPK and JNK. Inhibition of protein kinase A by 1 µM H-89 or 10 µM adenosine 3',5'-cyclic
monophosphothioate (Rp-isomer, triethylammonium salt) markedly
attenuated the activation of p38 MAPK and JNK. Conversely, the
selective protein kinase C inhibitor calphostin C did not block
D1 dopamine receptor-stimulated activation of p38 MAPK and
JNK. These results demonstrate, for the first time, that the
Gs-coupled D1 dopamine receptor activates the
p38 MAPK and JNK signaling pathways by a protein kinase A-dependent mechanism.
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