Somatostatin (SSTR2) receptors mediate phospholipase C-independent Ca2+ mobilization in rat AR42J pancreas cells.
Rat AR42J pancreas cells, which express somatostatin-SSTR2 type receptors, responded to SSTR2-selective somatostatin (SRIF) agonist ligands with a dose-dependent increase in intracellular Ca2+. In addition to SRIF-14 and SRIF-28, the most potent SRIF peptides were the cyclic octapeptides, BIM-23014C, BIM-23023, SMS 201-995, and the cyclic hexapeptides, MK-678 and BIM-23027. The SSTR3 and SSTR5-selective ligands, BIM-23056 and BIM-23052, were inactive and weakly active, respectively. None of the SRIF peptides stimulated inositol phosphate turnover, indicating that Ca2+ mobilization was independent of phospholipase C activation. Incubation in calcium-free medium abolished the increase in intracellular Ca2+. These results indicate that activation of SSTR2 receptors in AR42J cells opens cell-surface calcium channels.[1]References
- Somatostatin (SSTR2) receptors mediate phospholipase C-independent Ca2+ mobilization in rat AR42J pancreas cells. Taylor, J.E. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
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