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M302181200v1
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Papers In Press, published online ahead of print June 16, 2003
J. Biol. Chem, 10.1074/jbc.M302181200
Submitted on March 3, 2003
Revised on May 23, 2003
Accepted on June 16, 2003

Endogenously produced endothelial lipase enhances binding and cellular processing of plasma lipoproteins via HSPG-mediated pathway

Ilia V. Fuki, Nadine Blanchard, Weijun Jin, Dawn H.L. Marchadier, John S. Millar, Jane M. Glick, and Daniel J. Rader

Department of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6100

Corresponding Author: iliaf{at}mail.med.upenn.edu

Endothelial lipase (EL) is a new member of the triglyceride lipase gene family, which includes lipoprotein lipase (LpL) and hepatic lipase (HL). Enzymatic activity of EL has been studied before. Here we characterized the ability of EL to bridge lipoproteins to the cell surface. Expression of EL in wild-type CHO-K1 but not in heparan sulfate proteoglycan (HSPG)-deficient CHO-677 cells resulted in 3 to 4.4 fold increases of 125I-LDL and 125I-HDL3 binding. Inhibition of proteoglycan sulfation by sodium chlorate or incubation of cells with labeled lipoproteins in the presence of heparin (100 mu g/ml) abolished bridging effects of EL. An enzymatically inactive EL, EL-S149A, was equally effective in facilitating lipoprotein bridging as native EL. Processing of LDL and HDL differed notably after initial binding via EL to the cell surface. More than 90% of the surface-bound 125I-LDL was destined for internalization and degradation, while about 70% of the surface-bound 125I-HDL3 was released back into the medium. These differences were significantly attenuated after HDL clustering was promoted using antibody against apolipoprotein AI. At equal protein concentration of added lipoproteins the ratio of HDL3 to VLDL bridging via EL was 0.092 compared to 0.174 via HL and 0.002 via LpL. In summary, EL mediates binding and uptake of plasma lipoproteins via a process that is independent of its enzymatic activity, requires cellular HSPGs and is regulated by ligand clustering.


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