The selective esterification of the 5'-hydroxyl of thymidine.
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The incorporation of [1-14C] palmitic acid into tissue lipids of the medial and intimal layers of swine aortic homogenates was investigated. The homogenates obtained were metabolically active as indicated by their ready incorporation of labeled palmitic acid into phospholipids, diglycerides and triglycerides in the presence of alpha-glycerophosphate in the incubation medium. Predominantly, labeling of phospholipids and especially of phosphatidylcholine was found when alpha-glycerophosphate or lysolecithin served as the fatty acid acceptor. Glycerol and monoolein did not serve as fatty acid acceptors. More than 98% of the radioactivity was recovered as the rephosphatidylcholine fraction at the level of 0.64 micromoles/ml of lysolecithin in the incubation medium.
The purpose of the present study was to investigate the physiological control of the main regulatory enzymes of cholesterol metabolism in isolated enterocytes obtained from chick duodenum, jejunum and ileum. Cholesterol feeding resulted in an inhibition of 3-hydroxy-3-methyl-glutaryl-CoA reductase and mevalonate 5-pyrophosphate decarboxylase, while cholestyramine feeding increased reductase activity in all the regions studied and decarboxylase activity only in duodenum. Cholesterol feeding markedly increased acyl-CoA:cholesterol acyltransferase, but the effects of cholestyramine were less clear. The effects on transferase activity cannot be due to differences in the availability of acyl-CoA as exogenous substrate as no significant differences were found in acyl-CoA hydrolase activity after any of the dietary treatments. The effects of cholesterol feeding were related to changes in the cholesterol content of epithelial cells, whereas in the case of cholestyramine this relationship was less apparent.
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