J. Lipid Res.  Neurobiology of Lipids (ISSN1683-5506)
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Originally published In Press as doi:10.1194/jlr.M200322-JLR200 on September 1, 2002

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Journal of Lipid Research, Vol. 43, 1969-1977, November 2002
Copyright © 2002 by Lipid Research, Inc.

ApoC-III content of apoB-containing lipoproteins is associated with binding to the vascular proteoglycan biglycan

Katherine Olin-Lewis*, Ronald M. Krauss§, Michael La Belle§, Patricia J. Blanche§, P. Hugh R. Barrett**, Thomas N. Wight1,{dagger} and Alan Chait2,*

* Departments of Medicine, University of Washington, Seattle, WA
{dagger} Pathology, University of Washington, Seattle, WA
§ Donner Laboratory, Lawrence Berkeley National Laboratory, University of California, Berkeley, CA
** Department of Medicine, University of Western Australia and the Western Australia Institute for Medical Research, Perth 6847, Australia

2 To whom correspondence should be addressed. e-mail: achait{at}u.washington.edu

Retention of apolipoprotein (apo)B and apoE-containing lipoproteins by extracellular vascular proteoglycans is critical in atherogenesis. Moreover, high circulating apoC-III levels are associated with increased atherosclerosis risk. To test whether apoC-III content of apoB-containing lipoproteins affects their ability to bind to the vascular proteoglycan biglycan, we evaluated the impact of apoC-III on the interaction of [35S]SO4-biglycan derived from cultured arterial smooth muscle cells with lipoproteins obtained from individuals across a spectrum of lipid concentrations. The extent of biglycan binding correlated positively with apoC-III levels within VLDL (r = 0.78, P < 0.01), IDL (r = 0.67, P < 0.01), and LDL (r = 0.52, P < 0.05). Moreover, the biglycan binding of VLDL, IDL, and LDL was reduced after depletion of apoC-III-containing lipoprotein particles in plasma by anti-apoC-III immunoaffinity chromatography. Since apoC-III does not bind biglycan directly, enhanced biglycan binding may result from a conformational change associated with increased apo C-III content by which apoB and/or apoE become more accessible to proteoglycans. This may be an intrinsic property of lipoproteins, since exogenous apoC-III enrichment of LDL and VLDL did not increase binding.

ApoC-III content may thus be a marker for lipoproteins characterized as having an increased ability to bind proteoglycans.

Supplementary key words apolipoprotein C-III • very low density lipoproteins • intermediate density lipoproteins • low density lipoproteins • atherosclerosis • charge density


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