Different incorporation rates of arachidonic acid into alkenylacyl-, alkylacyl- and diacylphosphatidylethanolamine of rat erythrocytes.

Rat erythrocyte phosphatidylethanolamine (PE) consists of 60% alkenylacyl, 5% alkylacyl and 35% diacyl types. The fatty acid at the 2-position of these types is mainly composed of arachidonic acid. When intact rat erythrocytes were incubated with exogenous arachidonic acid, about 90% of the arachidonic acid incorporated into the PE fraction was found in the 2-position of the diacyl type. The rates of incorporation of arachidonic acid into alkenylacyl-, alkylacyl- and diacylPE were 78, 134 and 1360 pmol/h per mumol of the corresponding PE, respectively. The substrate specificities of endogenous phospholipase A2 and acyl-CoA:lysophospholipid acyltransferase were observed. DiacylPE was hydrolysed rapidly by endogenous phospholipase A2, while alkenylacyl- and alkylacylPE were poor substrates for the enzyme. The selective transfer of arachidonic acid into the 2-position of 1-acyl-lysoPE was observed. 1-Alkenyl- and 1-alkyl-lysoPE were also poor substrates for acyl-CoA:lysophospholipid acyltransferase. The acyltransferase activities with the lysoPE analogues were higher than the phospholipase A2 activities with PE analogues. These results suggest that the different incorporation rates of arachidonic acid into alkenylacyl-, alkylacyl- and diacylPE are based on the substrate specificity of endogenous phospholipase A2.