Cholecystokinin induces a decrease in Ca2+ current in snail neurons that appears to be mediated by protein kinase C.
Three distinct classes of protein kinases have been shown to regulate Ca2+ current in excitable tissues. Cyclic AMP-dependent protein kinase mediates the action of noradrenaline on the Ca2+ current of cardiac muscle cells. Cyclic GMP-dependent protein kinase mediates the serotonin-induced modulation of the Ca2+ current in identified snail neurons. The Ca2+/diacylglycerol-dependent protein kinase (protein kinase C) has also been found to regulate Ca2+ currents of neurons. However, no neurotransmitter has yet been shown to regulate Ca2+ current through the activation of protein kinase C. We now report that cholecystokinin, a widely occurring neuropeptide which is present in molluscan neuron, modulates the Ca2+ current in identified neurons of the snail Helix aspersa, and that this effect appears to be mediated by protein kinase C. Specifically, sulphated cholecystokinin octapeptide 26-33 (CCK8), activators of protein kinase C, and intracellular injection of protein kinase C, all shorten the Ca2+-dependent action potential and decrease the amplitude of the Ca2+ current in these cells. All these effects are not reversible within the duration of the experiments. Moreover, intracellular injections of low concentrations of protein kinase C, which are ineffective by themselves, enhance the effectiveness of low concentrations of CCK8 on the Ca2+ current.
D000818:Animals; D002118:Calcium / Q000378:metabolism*; D004533:Egtazic Acid / Q000494:pharmacology; D004553:Electric Conductivity; D004789:Enzyme Activation / Q000187:drug effects; D006372:Helix, Snails / Q000502:physiology*; D007473:Ion Channels / Q000187:drug effects / Q000502:physiology*; D009474:Neurons / Q000502:physiology*; D011493:Protein Kinase C / Q000502:physiology*; D012844:Sincalide / Q000494:pharmacology*
D007473:Ion Channels; D004533:Egtazic Acid; D011493:Protein Kinase C; D012844:Sincalide; D002118:Calcium