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A more recent version of this article appeared on July 1, 2003

Papers In Press, published online ahead of print April 16, 2003
J. Lipid Res., doi:10.1194/jlr.M200374-JLR200
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Submitted on September 19, 2002
Revised on April 15, 2003
Accepted on April 16, 2003

The amino acid sequences of the carboxyl termini of human and mouse hepatic lipase influence cell surface association

Robert J. Brown, Joshua R. Schultz, Kerry W.S. Ko, John S. Hill, Tanya A. Ramsamy, Ann L. White, Daniel L. Sparks, and Zemin Yao

Department of Lipoprotein and Atherosclerosis, University of Ottawa Heart Institute, Ottawa, Ontario K2J 3A4

Corresponding Author: zyao{at}ottawaheart.ca

Human hepatic lipase (hHL) exists mainly cell surface bound, whereas mouse HL (mHL) circulates in the bloodstream. Studies have suggested that the carboxyl terminus of HL mediates cell surface binding. We prepared recombinant hHL, mHL, and chimeric proteins (hHLmt and mHLht) in which the carboxyl-terminal 70 amino acids of hHL were exchanged with the corresponding sequence from mHL. The hHL, mHL, and hHLmt proteins were catalytically active using triolein and tributyrin as substrates. In transfected cells, the majority of hHL bound to the cell surface with only 4% of total extracellular hHL released into heparin-free media, whereas under the same conditions, 61% of total extracellular mHL were released. Like mHL, hHLmt showed decreased cell surface binding with 68% of total extracellular hHLmt released. To determine the precise amino acid residues involved in cell surface binding, we prepared a truncated hHL mutant (hHL471) by deleting the carboxyl-terminal five residues (KRKIR). The hHL471 also retained hydrolytic activity with triolein and tributyrin, and showed decreased cell surface binding with 40% of total extracellular protein released into the heparin-free media. These data suggest that the determinants of cell surface binding exist within the carboxyl-terminal 70 amino acids of hHL, of which the last five residues play an important role.


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