Endogenous substrates for camp-dependent phosphorylation in dispersed bovine parathyroid cells

Roz D. Lasker, Allen M. Spiegel

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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 languageEnglish (US)
Pages (from-to)1412-1414
Number of pages3
JournalEndocrinology
Volume111
Issue number4
DOIs
Publication statusPublished - Oct 1982
Externally publishedYes

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ASJC Scopus subject areas

  • Endocrinology

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