ApoC-III content of apoB-containing lipoproteins is associated with binding to the vascular proteoglycan biglycan
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 af...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2002-11-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520327723 |
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doaj-c54eff958931418696c12da01c32b029 |
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Article |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Katherine Olin-Lewis Ronald M. Krauss Michael La Belle Patricia J. Blanche P.Hugh R. Barrett Thomas N. Wight Alan Chait |
| spellingShingle |
Katherine Olin-Lewis Ronald M. Krauss Michael La Belle Patricia J. Blanche P.Hugh R. Barrett Thomas N. Wight Alan Chait ApoC-III content of apoB-containing lipoproteins is associated with binding to the vascular proteoglycan biglycan Journal of Lipid Research apolipoprotein C-III very low density lipoproteins intermediate density lipoproteins low density lipoproteins atherosclerosis charge density |
| author_facet |
Katherine Olin-Lewis Ronald M. Krauss Michael La Belle Patricia J. Blanche P.Hugh R. Barrett Thomas N. Wight Alan Chait |
| author_sort |
Katherine Olin-Lewis |
| title |
ApoC-III content of apoB-containing lipoproteins is associated with binding to the vascular proteoglycan biglycan |
| title_short |
ApoC-III content of apoB-containing lipoproteins is associated with binding to the vascular proteoglycan biglycan |
| title_full |
ApoC-III content of apoB-containing lipoproteins is associated with binding to the vascular proteoglycan biglycan |
| title_fullStr |
ApoC-III content of apoB-containing lipoproteins is associated with binding to the vascular proteoglycan biglycan |
| title_full_unstemmed |
ApoC-III content of apoB-containing lipoproteins is associated with binding to the vascular proteoglycan biglycan |
| title_sort |
apoc-iii content of apob-containing lipoproteins is associated with binding to the vascular proteoglycan biglycan |
| publisher |
Elsevier |
| series |
Journal of Lipid Research |
| issn |
0022-2275 |
| publishDate |
2002-11-01 |
| description |
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. |
| topic |
apolipoprotein C-III very low density lipoproteins intermediate density lipoproteins low density lipoproteins atherosclerosis charge density |
| url |
http://www.sciencedirect.com/science/article/pii/S0022227520327723 |
| work_keys_str_mv |
AT katherineolinlewis apociiicontentofapobcontaininglipoproteinsisassociatedwithbindingtothevascularproteoglycanbiglycan AT ronaldmkrauss apociiicontentofapobcontaininglipoproteinsisassociatedwithbindingtothevascularproteoglycanbiglycan AT michaellabelle apociiicontentofapobcontaininglipoproteinsisassociatedwithbindingtothevascularproteoglycanbiglycan AT patriciajblanche apociiicontentofapobcontaininglipoproteinsisassociatedwithbindingtothevascularproteoglycanbiglycan AT phughrbarrett apociiicontentofapobcontaininglipoproteinsisassociatedwithbindingtothevascularproteoglycanbiglycan AT thomasnwight apociiicontentofapobcontaininglipoproteinsisassociatedwithbindingtothevascularproteoglycanbiglycan AT alanchait apociiicontentofapobcontaininglipoproteinsisassociatedwithbindingtothevascularproteoglycanbiglycan |
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1721506728103641088 |
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doaj-c54eff958931418696c12da01c32b0292021-04-27T04:43:00ZengElsevierJournal of Lipid Research0022-22752002-11-01431119691977ApoC-III content of apoB-containing lipoproteins is associated with binding to the vascular proteoglycan biglycanKatherine Olin-Lewis0Ronald M. Krauss1Michael La Belle2Patricia J. Blanche3P.Hugh R. Barrett4Thomas N. Wight5Alan Chait6Departments 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, AustraliaDepartments 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, AustraliaDepartments 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, AustraliaDepartments 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, AustraliaDepartments 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, AustraliaDepartments 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, AustraliaDepartments 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, AustraliaRetention 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.http://www.sciencedirect.com/science/article/pii/S0022227520327723apolipoprotein C-IIIvery low density lipoproteinsintermediate density lipoproteinslow density lipoproteinsatherosclerosischarge density |