Inhibition of parathyroid hormone secretion correlates with increased incorporation of 32P into phosphatidylinositol and lysophosphatidylinositol.

We have studied the incorporation of radioactive P (32P) into lipids of bovine parathyroid tissue under conditions of stimulated and inhibited hormone secretion. Utilizing low (0.5 mM) and high (3.0 mM) concentrations of calcium to regulate parathyroid hormone secretion, we initially found that the labeling of the cellular phospholipids with 32P was greater in those tissues incubated in high-calcium medium. Thin-layer chromatography of lipid extracts prepared from tissue incubated in either low- or high-calcium media revealed that the increased incorporation of 32P (high or low) was localized primarily to two phospholipids. To determine whether the increases were due directly to the different calcium concentrations, the experiments were performed in media containing normal calcium concentrations (1.25 mM) and low (0.5) or high (3.0) magnesium concentrations to modulate hormone secretion. The results were identical to those obtained using low and high calcium, indicating that the increased 32P incorporation was not an effect of high calcium but rather correlated with the inhibition of hormone secretion. The use of other secretagogues confirmed this correlation. The identity of the two phospholipids was established, by two-dimensional thin-layer chromatography, to be phosphatidylinositol (PI) and lysophosphatidylinositol (LPI). The correlation of increased 32P incorporation with inhibition of secretion led us next to examine isolated secretory granules from tissues exposed to either high-or low-calcium conditions. Thin-layer chromatography of granule lipid extracts yielded chromatograms containing PI and LPI, and the radioactivity of each was greater in the high-calcium sample than in the low-calcium sample.(ABSTRACT TRUNCATED AT 250 WORDS)