The biosynthesis of phosphatidylserines by acylation of 1-acyl-sn-glycero-3-phosphoserine in rat liver.
The conversion of 1-[14C]acyl-sn-glycero-3-phosphoserine into molecular species of [14C]phosphatidylserine was studied using rat liver homogenate and microsomal preparations in the absence of added fatty acyl moieties. In liver homogenates, 81% of the newly-formed phosphatidylserines were tetraenoic (arachidonoyl) species while saturated, monoenoic, dienoic, trienoic, pentaenoic, and hexaenoic (docosahexaenoyl) species each represented 2-5% of the total. A similar pattern of molecular species was produced in liver microsomes. The selectivity of the microsomal acyl-CoA:1-acyl-sn-glycero-3-phosphoserine acyltransferase towards different acyl-CoA derivatives was also investigated. The relative suitability of the various acyl-CoA esters as substrates was found to be of the following order:20:4 = 18:2 greater than 18:1 greater than 16:0 = 18:0. These results with endogenous acyl donors suggest that the acylation of 1-acyl-sn-glycero-3-phosphoserine may partly account for the enrichment of liver phosphatidylserine in arachidonic acid but does not appear to be primarily responsible for the preponderance of docosahexaenoic acid in this phospholipid. The fatty acid specificity of the acyl-CoA: 1-acyl-sn-glycero-3-phosphoserine acyltransferase may contribute to the preferential formation of arachidonoyl phosphatidylserine.
D000215:Acylation; D000217:Acyltransferases / Q000378:metabolism; D000818:Animals; D004075:Diglycerides; D005227:Fatty Acids / Q000032:analysis; D005989:Glycerides; D008099:Liver / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism; D010718:Phosphatidylserines / Q000096:biosynthesis*; D010768:Phosphoserine / Q000031:analogs & derivatives*; D051381:Rats; D012694:Serine / Q000031:analogs & derivatives*
D004075:Diglycerides; D005227:Fatty Acids; D005989:Glycerides; D010718:Phosphatidylserines; D010768:Phosphoserine; D012694:Serine; D000217:Acyltransferases; C025461:1-acylglycerophosphoserine acyltransferase