Abstract
This chapter focuses on the muscarinic activation of phosphatidylcholine hydrolysis. The release of choline from tissues or cells is a sensitive indicator of an enhanced hydrolysis of phosphatidylcholine (PtdCho) and is easily determined by chemiluminescence. In certain cells, choline release may reflect the activity of a specific receptor-activated enzyme catalyzing PtdCho hydrolysis. A physiological role of the receptor-mediated release of choline in the brain is given by its role as biosynthetic precursor for acetylcholine (ACh) and phospholipids. When PtdCho hydrolysis is investigated to identify the phospholipase involved, the sole determination of enzymatic products may provide ambiguous results because of rapid metabolic interconversion. The chapter discusses the muscarinic activation of PtdCho hydrolysis in myocardial tissues of rats, chickens, and guinea-pigs. Phorbol ester through activation of protein kinase C enhances the formations of choline, phosphatidic acid, and, in the presence of ethanol, PEth indicating an activation of phospholipase D (PLD). Aluminium fluoride (AlF), an activator of trimeric G-proteins, also enhances both PLD and PI-phospholipase C (PLC) activity.
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