Differential Effect of Puromycin on Triacylglycerol and Phosphatidylcholine Synthesis in Rat Mecosal Microsomes

Publisher Website
Google Scholar
Abstract
The transferases involved in triacylglycerol and phosphatidylcholine synthesis were studied in mucosal microsomes of normal and puromycin-treated rats. The mono- and diacylglycerol acyltransferases showed similar activity in both normal and puromycin-treated microsomes. Cholinephosphotransferase was inhibited 55–60% and lysophos-phatidylcholine acyltransferase was inhibited 35–40% in mucosal microsomes from puromycin-treated rats. These results demonstrate that puromycin inhibits cholinephos-photransferase and lysophosphatidylcholine acyltransferase without interfering with the acyltransferases involved in triacylglycerol synthesis. Since the transferases involved in phosphatidylcholine synthesis are largely located in the rough endoplasmic reticulum, it is suggested that the inhibition of these enzymes is due to the selective disassembly of the rough endoplasmic reticulum by puromycin as demonstrated elsewhere.