Abstract
Agonists that increase intracellular cAMP in bovine parathyroid cells ((퓁)-isoproterenol (ISO), dopatnine, prostaglandin E2) as well as cAMP analogs (dibutyryl cAMP and 8-bromo-cAMP) stimulated the phosphorylation of 2 endogenous proteins with apparent molecular weights of 19K and 15K. The time course and concentration-dependence of ISO-stimulated phosphorylation in these cells correlated well with known effects of ISO on intracellular cAMP and PTH release. ISO-stimulated phosphorylation of these two proteins was rapidly reversed by (퓁)-propranolol. Although 2 mM extracellular calcium inhibited ISO-stimulated PTH secretion, it did not significantly affect the phosphorylation of the 19K and 15K bands. These results are consistent with a physiologic role for the phosphorylation of these proteins in agonist-stimulated PTH secretion in bovine parathyroid cells.
Original language | English (US) |
---|---|
Pages (from-to) | 1412-1414 |
Number of pages | 3 |
Journal | Endocrinology |
Volume | 111 |
Issue number | 4 |
DOIs | |
State | Published - Oct 1982 |
Externally published | Yes |
ASJC Scopus subject areas
- Endocrinology