Endogenous substrates for cAMP-dependent phosphorylation in dispersed bovine parathyroid cells.

R. D. Lasker, Allen M. Spiegel

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Agonists that increase intracellular cAMP in bovine parathyroid cells ((l)-isoproterenol (ISO), dopamine, 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 (l)-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 languageEnglish (US)
Pages (from-to)1412-1414
Number of pages3
JournalEndocrinology
Volume111
Issue number4
StatePublished - Oct 1982
Externally publishedYes

Fingerprint

Isoproterenol
Phosphorylation
8-Bromo Cyclic Adenosine Monophosphate
Proteins
Dinoprostone
Propranolol
Dopamine
Molecular Weight
Calcium

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

Endogenous substrates for cAMP-dependent phosphorylation in dispersed bovine parathyroid cells. / Lasker, R. D.; Spiegel, Allen M.

In: Endocrinology, Vol. 111, No. 4, 10.1982, p. 1412-1414.

Research output: Contribution to journalArticle

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