Functional expression of 5-HT1c receptor cDNA in COS 7 cells and its influence on protein kinase C

Two subtypes of receptors for serotonin (5-hydroxytryptamine; 5-HT) are known to stimulate inositol (1,4,5)-trisphosphate production, the 5-HT1c and 5-HT2 receptors. In this study we investigated the ability of 5-HT1c receptors, transiently expressed in COS 7 cells, to functionally interact with protein kinase C-alpha, the indigenous (phorbol ester-responsive) isoform of the enzyme in those cells. Serotonin caused translocation of the [3H]phorbol 12,13-dibutyrate (PDBu) binding site of PKC-alpha from the cytosolic to the membrane fraction in a Ca(2+)-dependent manner which was prevented by the 5-HT1c receptor antagonist mianserin. The lipid activators of PKC, PDBu and 1,2-dioctanoyl-sn-glycerol (DOG) also caused translocation, but through a mechanism apparently quite independent of Ca2+.