Mechanism of Isoprenaline-Stimulated Diacylglycerol Formation in Rat Parotid Acinar Cells

Adenylate cyclase purified by affinity chromatography was activated about 2.5-fold in a Ca(2+)- and calmodulin-dependent fashion. G protein beta gamma-subunits, an inhibitor in the receptor-mediated inhibition of adenylate cyclase, inhibited the purified cyclase by more than 80%. The extent of beta gamma-induced inhibition was not affected by the activation with Ca2+ and calmodulin. Moreover, the prior addition of the beta gamma-subunits to the cyclase did not prevent the subsequent activation of the enzyme by Ca2+ and calmodulin. We conclude that the beta gamma-subunits inhibit adenylate cyclase activity in a calmodulin-independent mode.