Inhibition of parathyroid hormone release from dispersed bovine cells by ouabain

Ouabain, at concentrations of 3 X 10(-4)-10(-3) M, inhibited secretion of PTH approximately 50% in a freshly dispersed bovine parathyroid cell preparation. This inhibition was found with both unstimulated and secretagogue-stimulated PTH release. Reductions in PTH secretion were found at all concentrations of Ca++ tested between 0.3 mM and 2.0 mM and in the presence of the divalent cation chelators EDTA and EGTA, indicating that extracellular Ca++ is not an absolute requirement for the inhibition. The ouabain inhibition did not appear to be mediated through changes in either adenylate cyclase activity or total cellular cAMP, implying a locus distal to the generation of this cyclic nucleotide. The data suggest that transmembrane potential and/or distribution of monovalent cations across the plasma membrane is important in the maintenance of PTH secretion. The mechanisms involved in this control do not appear to involve extracellular Ca++ directly.