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Volume 271, Number 32, Issue of August 9, 1996 pp. 19503-19508
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Dopamine D1A Receptor Regulation of Phospholipase C Isoform

(Received for publication, March 25, 1996, and in revised form, May 16, 1996)

Pei-Ying Yu Dagger , Gilbert M. Eisner § , Ikuyo Yamaguchi , M. Maral Mouradian par , Robin A. Felder and Pedro A. Jose Dagger §

From the Dagger  Department of Pediatrics, Georgetown University Medical Center and the § Department of Physiology and Biophysics, Georgetown University School of Medicine, Washington, D. C. 20007, the  Department of Pathology, University of Virginia School of Medicine, Charlottesville, Virginia 22908, and the par  Genetic Pharmacology Unit, NINDS, National Institutes of Health, Bethesda, Maryland 20892

In LTK- cells stably transfected with rat D1A receptor cDNA, fenoldopam, a D1 agonist, increased phosphatidylinositol 4,5-bisphosphate hydrolysis in a time-dependent manner. In the cytosol, phospholipase C (PLC) activity increased (50 ± 7%) in 30 s, returned to basal level at 4 h, and decreased below basal values by 24 h; in the membrane, PLC activity also increased (36 ± 13%) in 30 s, returned to basal level at 10 min, and decreased below basal value at 4 and 24 h. Fenoldopam also increased PLC-gamma protein in a time-dependent manner. The latter was blocked by the D1 antagonist SKF83742 and by a D1A antisense oligodeoxynucleotide, indicating involvement of the D1A receptor. The fenoldopam-induced increase in PLC-gamma and activity was mediated by protein kinase A (PKA) since it was blocked by the PKA antagonist Rp-8-CTP-adenosine cyclic 3':5'-monophosphorothioate (Rp-8-CTP-cAMP-S) and mimicked by direct stimulation of adenylyl cyclase with forskolin or by a PKA agonist, Sp-cAMP-S. Protein kinase C (PKC) was also involved, since the fenoldopam-induced increase in PLC-gamma protein was blocked by two different PKC inhibitors, calphostin C and chelerythrine; calphostin C also blocked the fenoldopam-induced increase in PLC activity. In addition, forskolin and a PKA agonist, Sp-8-CTP-cAMP-S, increased PKC activity, and direct stimulation of PKC with phorbol 12-myristate 13-acetate increased PLC-gamma protein and activity, effects that were blocked by calphostin C. We suggest that the D1A-mediated stimulation of PLC occurs as a result of PKA activation. PKA then stimulates PLC-gamma in cytosol and membrane via activation of PKC.


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