Phorbol Esters and Muscarinic Receptor Agonists Activate Phospholipase D in Heart and Brain

1991

Phospholipase D (PLD) hydrolyzes phosphatidylcholine and thereby seems to play a key role in a novel pathway of signal transduction. PLD activity in rat hippocampal slices and atria of rat, guinea pig and chicken hearts was determined by measuring the catalytic products choline (Ch), phosphatidic acid (PA) and, in the presence of a primary alcohol, phosphatidylpropanol or phosphatidylethanol. It was found that the PLD activity was high, even under resting conditions, in both tissues, especially in the hippocampus, and that the enzyme activity could be enhanced by activation of protein kinase C and by muscarinic receptor stimulation.