Stimulation of rat liver microsomal cGMP-inhibited cAMP phosphodiesterase (PDE III) by phospholipase C and D
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Updated: Aug 21, 2026

Monitoring Endoplasmic Reticulum Calcium Homeostasis Using a Gaussia Luciferase SERCaMP
Published on: September 6, 2015
1Department of Pharmacology, University of Padova, Italy.
Abstract:
The specific activity of cGMP-inhibited cAMP phosphodiesterase (PDE III) of rat liver microsomal membranes is increased in a concentration-dependent way by adding phospholipase C from Clostridium perfringens or phospholipase D from Streptomyces chromofuscus. The effect depends on an increase in Vmax of the enzyme. Treatment of microsomal membranes with phospholipase C causes a marked increase in the relative amounts of phosphatidylserine and phosphatidylinositol, and mild stimulation of PDE III activity. Treatment with phospholipase D increases phosphatidic acid and strongly increases PDE III activity. These data suggest that phosphatidic acid is the most important regulator of membrane-bound PDE III activity in liver.
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