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Papers In Press, published online ahead of print February 1, 2005
J. Lipid Res., doi:10.1194/jlr.M400212-JLR200
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Lipid Research Group, Heart Research Institute, Sydney, New South Wales 2050
Corresponding Author: a.jahangiri{at}hri.org.au
Endothelial lipase (EL) is a triglyceride lipase gene family member that has high phospholipase and low triglyceride lipase activity. The aim of this study was to determine if the phospholipase activity of EL is sufficient to remodel high density lipoproteins (HDL) into small particles, and mediate the dissociation of apolipoprotein (apo) A-I. Spherical, reconstituted HDL (rHDL) containing either apoA-I only, (A-I)rHDL, apoA-II only, (A-II)rHDL, or both apoA-I and apoA-II, (A-I/A-II)rHDL, were prepared. The rHDL, which contained only cholesteryl esters in their core, and 1-palmitoyl-2-oleoyl phosphatidylcholine (POPC) on the surface, were incubated with EL. As the rHDL did not contain triacylglycerol, only the POPC was hydrolysed. Hydrolysis was greater in the (A-I/A-II)rHDL than in the (A-I)rHDL. The (A-II)rHDL phospholipids were not hydrolysed by EL. EL remodelled the (A-I)rHDL and (A-I/A-II)rHDL, but not the (A-II)rHDL, into smaller particles. The reduction in particle size was related to the amount of phospholipid hydrolysis, with the diameter of the (A-I/A-II)rHDL decreasing more than that of the (A-I)rHDL. These changes did not affect the conformation of apoA-I, and neither apoA-I nor apoA-II dissociated from the rHDL. Comparable results were obtained when human plasma HDL were incubated with EL. These results establish that the phospholipase activity of EL remodels plasma HDL and rHDL into smaller particles without mediating dissociation of apolipoproteins.
Revised on January 19, 2005
Accepted on January 20, 2005
Evidence that endothelial lipase remodels high density lipoproteins without mediating the dissociation of apolipoprotein A-I
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