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

Papers In Press, published online ahead of print January 16, 2003
J. Lipid Res., doi:10.1194/jlr.M200444-JLR200
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Submitted on November 25, 2002
Revised on January 16, 2003
Accepted on January 15, 2003

Lack of a direct role for macrosialin in oxidized LDL metabolism

Maria C. de Beer, Zhenzhe Zhao, Nancy R. Webb, Deneys R. van der Westhuyzen, and Willem J. S. de Villiers

Internal Medicine, University of Kentucky Medical Center, Lexington, KY 40536

Corresponding Author: wdevil0{at}uky.edu

Murine macrosialin, a scavenger receptor family member, is a heavily glycosylated transmembrane protein expressed predominantly in macrophage (Mf) late endosomes. Macrosialin is also found on the cell surface where it is suggested, on the basis of ligand blotting, to bind oxidized LDL (oxLDL). Here we report on the regulation of macrosialin by an atherogenic high-fat diet and oxLDL, and on the inability of macrosialin in transfected cells to bind oxLDL. Macrosialin expression was markedly increased in the livers of atherosclerosis-susceptible C57BL/6 and atherosclerosis-resistant C3H/HeJ mice fed an atherogenic high-fat diet. In resident mouse peritoneal Mf, treatment with oxLDL up-regulated macrosialin mRNA and protein expression 1.5 to 3-fold. Macrosialin, overexpressed in COS-7 cells through adenovirus mediated gene transfer, bound oxLDL by ligand blotting. However, no binding of oxLDL to macrosialin was observed in intact transfected COS-7 and CHO cells, despite significant cell surface expression of macrosialin. Furthermore, inhibition of macrosialin through gene silencing did not affect the binding of oxLDL to Mf. We conclude that although macrosialin expression in Mf and Kupffer cells is responsive to a pro-atherogenic inflammatory diet and to oxLDL, macrosialin does not function as an oxLDL receptor on the cell surface.


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