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J Biol Chem, Vol. 274, Issue 49, 34629-34636, December 3, 1999
From the Departments of Retention of low density lipoproteins (LDL) by
vascular proteoglycans and their subsequent oxidation are important in
atherogenesis. Lipoprotein lipase (LPL) can bind LDL and proteoglycans,
although the effect of different proteoglycans to influence the ability of LPL to act as a bridge in the formation of LDL-proteoglycan complexes is unknown. Using an electrophoretic gel mobility shift assay, [35S]SO4-labeled versican and
biglycan, two extracellular proteoglycans secreted by vascular cells,
bound native LDL in a saturable fashion. The addition of bovine milk
LPL dose-dependently increased the binding of native LDL to
both versican and biglycan, approaching saturation at 30-40 µg/ml
LPL for versican and 20 µg/ml LPL for biglycan. LDL was oxidized by
several methods, including copper, 2,2-azo-bis(2-amidinopropane)-2HCl
and hypochlorite. Extensively copper- and hypochlorite-oxidized LDL
bound poorly to versican and biglycan. Proteoglycan binding to LDL was
correlated inversely with the extent of LDL; however, the addition of
LPL to oxidized LDL together with biglycan or versican allowed the
oxidized LDL to bind the proteoglycans in an LPL
dose-dependent manner. Addition of LPL had a greater
relative effect on the binding of extensively oxidized LDL to
proteoglycans compared with native LDL. LPL had a slightly greater
effect on increasing the binding of native and oxidized LDL to biglycan
than versican. Thus, LPL in the artery wall might increase the
atherogenicity of oxidized LDL, since it enables its binding to
vascular biglycan and versican.
Lipoprotein Lipase Enhances the Binding of Native and Oxidized
Low Density Lipoproteins to Versican and Biglycan Synthesized by
Cultured Arterial Smooth Muscle Cells
,
Medicine and
§ Pathology, University of Washington,
Seattle, Washington 98195 and the ¶ Department of Medicine,
University of Western Australia, Perth 6001, Australia
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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