Protein kinase C modulates cAMP content in proximal tubular cells: role of phosphodiesterase inhibition

LANDER. Protein kinase C modulates CAMP content in proximal tubular cells: role of phosphodiesterase inhibition. Am. J. Phys-iol. 261 (Renal Fluid Electrolyte Physiol. 30): F587-F592, 1991.-The present study was designed to evaluate whether protein kinase C (PKC) activation affects hormone-modulated adenosine 3’,5’-cyclic monophosphate (CAMP) accumulation in rabbit renal proximal tubular cells in primary culture. When intracellular CAMP content was measured in the presence of Ro 20-1724, a selective inhibitor of type III phosphodiesterase (PDE), activation of PKC by the phorbol ester phorbol l2-myristate 13-acetate (PMA) or by diacylglycerol kinase inhib-itor R 59022 reinforced parathyroid hormone (PTH)- and for-skolin-stimulated CAMP accumulation. During PKC activa-tion, the inhibitory effect of norepinephrine on CAMP content persisted, whereas that of angiotensin II (ANG II) was blunted