Modulation of serotonin binding sites in Spisula solidissima oocytes by phorbol ester.
In Spisula solidissima oocytes, serotonin (5-hydroxytryptamine, 5-HT)-dependent meiosis reinitiation is mediated via specific 5-HT membrane binding sites. This oocyte response is inhibited by the phorbol ester TPA. To assess whether the inhibitory effect of TPA was due to alteration of oocyte membrane binding sites, we studied their characteristics after TPA treatment. [3H]-5HT binding assays revealed that TPA decreased the affinity and, after prolonged treatment, increased the number of oocyte binding sites. Moreover, inhibitory actions of TPA on 5-HT-induced meiosis reinitiation paralleled its inhibitory effects on 5-HT binding site affinity. The inhibitory actions in biological assays were restricted to TPA (an inactive analog of TPA, TPA-met was inefficient) and were completely reversed by staurosporine. Our data thus suggest an inhibitory role for protein kinase C on oocyte 5-HT binding sites under physiological conditions.
Ecole Normale Supérieure, Laboratoire de Biologie Moléculaire et Cellulaire, Lyon, France.
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D000818:Animals; D049872:Bivalvia; D002462:Cell Membrane / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D007700:Kinetics; D009865:Oocytes / Q000378:metabolism*; D011493:Protein Kinase C / Q000502:physiology; D011869:Radioligand Assay; D011985:Receptors, Serotonin / Q000187:drug effects* / Q000378:metabolism; D012701:Serotonin / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D011985:Receptors, Serotonin; D012701:Serotonin; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate