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Papers In Press, published online ahead of print April 16, 2005
J. Lipid Res., doi:10.1194/jlr.M500054-JLR200
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Institut of Biochemistry and Molecular Biology, University of Graz, Graz 8010
Corresponding Author: sasa.frank{at}meduni-graz.at
We assessed the ability of EL to hydrolyze the sn-1 and sn-2 fatty acids (FAs) from HDL-phosphatidylcholine (HDL-PC). For this purpose, we incubated reconstituted discoidal HDL (rHDL) that contained free cholesterol (FC), apolipoprotein A-I (apo A-I) and either 1-palmitoyl-2-oleoylphosphatidylcholine (POPC), 1-palmitoyl-2-linoleoylphosphatidylcholine (PLPC) or 1-palmitoyl-2-arachidonylphosphatidylcholine (PAPC) with EL- and control- (LacZ)- conditioned medium. Gas chromatography (GC) analysis of the reaction mixtures revealed that both, the sn-1 (16:0) and sn-2 FA (18:1, 18:2 and 20:4, respectively) were liberated by EL. The higher rate of sn-1 FA cleavage compared with sn-2 FA release generated corresponding sn-2 acyl lyso-species as determined by MS analysis. EL failed to release sn-2 FA from rHDL containing plasmalogen-PC, whose sn-1 position contained a non-hydrolyzable alkyl ether linkage. The lack of phospholipase A2 (PLA2) activity of EL and its ability to liberate [14C]-FA from [14C]-lyso-PC, led us to conclude that EL-mediated deacylation of PC is initiated at the sn-1 position followed by the release of the remaining FA from the lyso-PC intermediate. TLC analysis of cellular lipids obtained from EL-overexpressing cells revealed a pronounced accumulation of 14C-PL and 14C-triglycerides (TAG) upon incubation with 1-palmitoyl-2- [1-14C]-linoleoyl-PC-labeled HDL3, indicating the ability of EL to supply cells with unsaturated FAs.
Revised on March 30, 2005
Accepted on April 11, 2005
Endothelial lipase releases saturated and unsaturated fatty acids of high density lipoprotein phosphatidylcholine
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