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The present study was undertaken to investigate the mechanism by which arginine vasopressin (AVP) increases insulin secretion in rat insulinoma (RINmSF) cells by using a specific phospholipase C (PLC) inhibitor, U-73122, and a phospholipase A2 (PLAj) inhibitor, N-(p-amylcinnamoyl)anthranilic acid (ACA). AVP (0.1-100 niv!) increased insulin secretion and cytosolic free Ca^^ concentration 'Reprinted with permission from J. Pharmacol. Exp. Ther. 1994, 207, 400-404. Copyright @ 1994 J. Pharmacol. Exp. Ther. ^ Author for correspondence. 27 ([Ca^^^Ji) dose-dependently. Moreover, U-73122 (2-8 |iM) inhibited the A VPinduced increases in the intracellular concentration of inositol 1,3,4-trisphosphate (IP3) and [Ca^^Jj dose-dependently. At 8 j^M U-73122 abolished the AVP's effect on IP3 and [Ca"^]j, but it only reduced the AVP-induced increase in insulin secretion by 35%. In contrast, 8 |LIM U-73122 did not reduce the ionomycin (a Ca"^ ionophore, 100 nM)-induced increase in [Ca^^'ji. The discrepancy between the results of [Ca*"^]; and insulin secretion may be due to the multiple signal transduction pathways associated with the activation of AVP receptors, specifically the Ca^^-independent pathway. The phospholipase Aj inhibitor ACA (100 jiM) did not antagonize the AVP (10 nM)-induced increase in insulin release. These results suggested: 1) U-73122 blocks PLC activhies but fails to block other signal transduction pathways that trigger insulin secretion in these cells, and 2) AVP increases insulin release from RINmSF cells through both the PLC mediated Ca""^dependent and Ca^^'-independent pathways.

Mechanisms of arginine vasopressin-induced insulin secretion in RINm5F cells