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J. Lipid Res.
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A more recent version of this article appeared on August 1, 2006 Originally published In Press as doi:10.1194/jlr.M500552-JLR200 on May 10, 2006

Papers In Press, published online ahead of print May 8, 2006
J. Lipid Res., doi:10.1194/jlr.M500552-JLR200
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Submitted on December 21, 2005
Revised on April 25, 2006
Accepted on May 8, 2006

Substrate specificity of lipoprotein lipase and endothelial lipase: Studies of lid chimeras

Nathalie Griffon, Elaine C. Budreck, Christopher J. Long, Uli C. Brodel, Dawn H. L. Marchadier, Jane M. Glick, and Daniel J. Rader

ITMAT, University of Pennsylvania, Philadelphia, PA 19104

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

The triglyceride (TG) lipase gene subfamily, consisting of lipoprotein lipase (LPL), hepatic lipase (HL), and endothelial lipase (EL), plays a central role in plasma lipoprotein metabolism. Compared with LPL and HL, EL is relatively more active as a phospholipase than a TG lipase. The amino acid loop or “lid” covering the catalytic site has been implicated as the basis for the difference in substrate specificity between HL and LPL. To determine the role of the lid in the substrate specificity of EL, we studied EL in comparison to LPL by mutating specific residues of the EL lid and by exchanging their lids. Mutation studies showed that amphipathic properties of the lid contribute to substrate specificity. Exchanging lids between LPL and EL only partially shifted the substrate specificity of the enzymes. Studies of a double chimera possessing both the lid and C-domain of EL in the LPL backbone showed that the role of the lid in determining substrate specificity does not depend on the nature of the C-domain of the lipase. Using a kinetic assay, we showed an additive effect of the EL lid on the apparent affinity for HDL3 in the presence of the EL C-domain.


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