A study of the molecular species of diacylglycerol, phosphatidylcholine and phosphatidylethanolamine and of cholinephosphotransferase and ethanolaminephosphotransferase activities in the type II pneumocyte.
The percent distributions of the molecular species of diacylglycerol, phosphatidylcholine and phosphatidylethanolamine in rat whole lung and type II pneumocytes were found to differ significantly. Diacylglycerol from the type II pneumocyte is enriched in the disaturated species and diminished in the polyenoic species compared to whole lung. Type II pneumocyte phosphatidylcholine is enriched in the disaturated species and diminished in all other species compared to whole lung. Relative to whole lung, type II pneumocyte phosphatidylethanolamine is greatly enriched in monoenoic and depleted in polyenoic fatty acid species. Analysis of the fatty acid composition of the molecular species in general indicated differences in relative amounts of fatty acids which were most pronounced in palmitic, palmitoleic, stearic and oleic acids, both within and between type II pneumocyte and whole lung glycerolipids. Significant differences between molecular species also existed within type II pneumocyte glycerolipids. In this cell type, phosphatidylcholine is enriched in disaturated and diminished in monoenoic species compared to diacylglycerol. Phosphatidylethanolamine is enriched in monoenoic and polyenoic species relative to diacylglycerol. In order to determine whether differences observed in type II pneumocyte glycerolipid molecular species were attributable to differences in the specificities of cholinephosphotransferase and ethanolaminephosphotransferase, the selectivity of these enzymes was examined. While cholinephosphotransferase showed diminished activity towards 1-stearoyl-2-linoleoyl-sn-glycerol, neither enzyme showed selectivity towards other tested diacylglycerols under a variety of conditions. Therefore, while in the type II pneumocyte significant amounts of phosphatidylcholine (particularly the disaturated species) and phosphatidylethanolamine may be synthesized de novo, enzymes responsible for remodeling (phospholipase A2 and acyltransferases) may play an important role in establishing the final molecular species composition of both phosphatidylcholine and phosphatidylethanolamine.
D000818:Animals; D002798:Diacylglycerol Cholinephosphotransferase / Q000378:metabolism*; D004075:Diglycerides / Q000032:analysis*; D004982:Ethanolaminephosphotransferase / Q000378:metabolism*; D005989:Glycerides / Q000032:analysis*; D008168:Lung / Q000032:analysis / Q000166:cytology / Q000201:enzymology*; D008297:Male; D010713:Phosphatidylcholines / Q000032:analysis*; D010714:Phosphatidylethanolamines / Q000032:analysis*; D010770:Phosphotransferases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D004075:Diglycerides; D005989:Glycerides; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D010770:Phosphotransferases; D004982:Ethanolaminephosphotransferase; D002798:Diacylglycerol Cholinephosphotransferase