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¹ Dipartimento di Scienze e Tecnologie Biologiche e Ambientali, Università degli Studi di Lecce, Ecotekne, Via Provinciale per Monteroni, 73100 Lecce, Italy
² Istituto di Endocrinologia e Oncologia Sperimentale G Salvatore, CNR, Naples, Italy
³ Dipartimento di Biologia e Patologia Cellulare e Molecolare L Califano, Naples, Italy

(Requests for offprints should be addressed to B D Jeso; Email: bdijeso{at}ilenic.unile.it or S Marsigliante; Email: santo.marsigliante{at}unile.it)

In PC Cl3 cells, a continuous, fully differentiated rat thyroid cell line, P2Y₂ purinoceptor activation provoked a transient increase of [Ca²⁺]_i, followed by a decreasing sustained phase. The and ß1 protein kinase C (PKC) inhibitor Gö6976 decreased the rate of decrement to the basal [Ca²⁺]_i level and increased the peak of Ca²⁺ entry of the P2Y₂-provoked Ca²⁺transients. These effects of Gö 6976 were not caused by an increased permeability of the plasma membrane, since the Mn²⁺ and Ba²⁺ uptake were not changed by Gö 6976. Similarly, the Na⁺/Ca²⁺ exchanger was not implicated, since the rate of decrement to the basal [Ca²⁺]_i level was equally decreased in physiological and Na⁺-free buffers, in the presence of Gö 6976. On the contrary, the activity of the sarcoplasmic–endoplasmic reticulum Ca²⁺ATPase (SERCA) 2b was profoundly affected by Gö 6976 since the drug was able to completely inhibit the stimulation of the SERCA 2b activity elicited by P2-purinergic agonists. Finally, the PKC activator phorbol myristate acetate had effects opposite to Gö 6976, in that it markedly increased the rate of decrement to the basal [Ca²⁺]_i level after P2Y₂ stimulation and also increased the activity of SERCA 2b. These results suggest that SERCA 2b plays a role in regulating the sustained phase of Ca²⁺ transients caused by P2Y₂ stimulation.