| Autor: |
Ulianich, Luca, Elia, Maria Giovanna, Treglia, Antonella Sonia, Muscella, Antonella, Di Jeso, Bruno, Storelli, Carlo, Marsigliante, Santo |
| Zdroj: |
Journal of Endocrinology; July 2006, Vol. 190 Issue: 3 p641-649, 9p |
| Abstrakt: |
In PC Cl3 cells, a continuous, fully differentiated rat thyroid cell line, P2Y2purinoceptor activation provoked a transient increase of [Ca2+]i, followed by a decreasing sustained phase. The α and β1 protein kinase C (PKC) inhibitor Gö6976 decreased the rate of decrement to the basal [Ca2+]ilevel 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+]ilevel 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+]ilevel after P2Y2stimulation 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 P2Y2stimulation. |
| Databáze: |
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