Na+ dependence of in vitro pancreatic amylase release.

The effects of Na+ on the in vitro release of amylase from mouse pancreas were studied. Replacement of Na+ in the medium by Tris, choline, or sucrose blocked the stimulation of amylase release by bethanechol and caerulein, whereas replacement by Li+ was without effect. The inhibiton was rapid and reversible, with stimulated amylase release linearly related to the log of the medium Na+ concentration over the range of 20-100 mM Na+. In contrast to the inhibition of amylase release stimulated by physiological secretagogues, enzyme release stimulated by the Ca2+ ionophore A23187 was unaffected by removal of Na+ from the medium. Tissue and intracellular Na+ and K+ contents were unchanged after stimulation of secretion by physiological stimulants. It is concluded that Na+ may be important in the early steps of stimulus-secretion coupling leading to the putative rise in intracellular Ca2+ that triggers pancreatic enzyme release.