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A more recent version of this article appeared on September 1, 2007

Papers In Press, published online ahead of print June 3, 2007
J. Lipid Res., doi:10.1194/jlr.M700248-JLR200
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Submitted on May 30, 2007
Accepted on June 2, 2007

N-glycosylation regulates endothelial lipase-mediated phospholipid hydrolysis in apoE- and apoA-I-containing high density lipoproteins

Danielle Skropeta, Chatri Settasatian, Monica R. McMahon, Kate D. Shearston, Daniela Caiazza, Kristine C. McGrath, Weijun Jin, Daniel J. Rader, Philip J. Barter, and Kerry A. Rye

Lipid Research Group, The Heart Research Institute, Camperdown, New South Wales 2050

Corresponding Author: karye{at}ozemail.com.au

Endothelial lipase (EL) is a member of the triglyceride lipase gene family with high phospholipase and low triacylglycerol lipase activities, and a distinct preference for hydrolysing phospholipids in HDL. EL has five potential N-glycosylation sites, four of which are glycosylated. The aim of this study is to determine how glycosylation affects the phospholipase activity of EL in physiologically relevant substrates. Site-directed mutants of EL were generated by replacing asparagine (N) 62, 118, 375 and 473 with alanine (A). These glycan-deficient mutants were used to investigate the kinetics of phospholipid hydrolysis in fully characterized preparations of spherical reconstituted HDL (rHDL) containing apoE2, (E2)rHDL, apoE3, (E3)rHDL, apoE4, (E4)rHDL, or apoA-I, (A-I)rHDL, as the sole apolipoprotein. Wild-type EL hydrolysed the phospholipids in (A-I)rHDL, (E2)rHDL, (E3)rHDL and (E4)rHDL to a similar extent. The phospholipase activity of EL N118A, EL N375A and EL N473A was significantly diminished relative to wild-type EL, with the greatest reduction being apparent for (E3)rHDL. The phospholipase activity of EL N62A was increased up to 6-fold relative to wild-type EL, with the greatest enhancement of activity being observed for (E2)rHDL. These data show that individual N-linked glycans have unique and important effects on the phospholipase activity and substrate specificity of EL.


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N. Settasatian, P. J. Barter, and K.-A. Rye
Remodeling of apolipoprotein E-containing spherical reconstituted high density lipoproteins by phospholipid transfer protein
J. Lipid Res., January 1, 2008; 49(1): 115 - 126.
[Abstract] [Full Text] [PDF]


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