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. Wight; Alan Chait

Journal of Lipid Research (Nov 2002)

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. Wight,
Alan Chait

Affiliations

Katherine Olin-Lewis: Departments of Medicine, University of Washington, Seattle, WA; 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
Ronald M. Krauss: Departments of Medicine, University of Washington, Seattle, WA; 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
Michael La Belle: Departments of Medicine, University of Washington, Seattle, WA; 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
Patricia J. Blanche: Departments of Medicine, University of Washington, Seattle, WA; 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
P.Hugh R. Barrett: Departments of Medicine, University of Washington, Seattle, WA; 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
Thomas N. Wight: Departments of Medicine, University of Washington, Seattle, WA; 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
Alan Chait: Departments of Medicine, University of Washington, Seattle, WA; 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

Journal volume & issue: Vol. 43, no. 11
pp. 1969 – 1977

Abstract

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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.

Published in Journal of Lipid Research

ISSN: 0022-2275 (Print); 1539-7262 (Online)
Publisher: Elsevier
Country of publisher: United States
LCC subjects: Science: Chemistry: Organic chemistry: Biochemistry
Website: https://www.journals.elsevier.com/journal-of-lipid-research

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