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Cited by 19Cholesterol and Lipid MetabolismAtherosclerosis and Cardiovascular DiseasesLipoproteins and Cardiovascular Health

Apolipoprotein E Mediates the Retention of High-Density Lipoproteins by Mouse Carotid Arteries and Cultured Arterial Smooth Muscle Cell Extracellular Matrices

Olin-Lewis, Katherine, Benton, Jeana L., Rutledge, John C., Baskin, Denis G., Wight, Thomas N., Chait, Alan·2002·Circulation Research
DOI 10.1161/01.res.0000024691.82864.f0
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Abstract

Lipoprotein retention in the vascular extracellular matrix (ECM) plays a critical role in atherogenesis. Previous studies demonstrated the presence of apo A-I and E in atherosclerotic lesions, suggesting that HDL may be trapped by the artery wall. We sought to determine mechanisms by which HDL could be bound and retained by the arterial wall, and whether apo E was a principal determinant of this binding. We evaluated in situ accumulation of fluorescently labeled DiI-human HDL±apo E in perfused carotid arteries from apo E–null mice. Apo E was important in mediating HDL binding to the vascular wall, with a 48±16% increase in accumulation of DiI-labeled apo E–containing HDL (HDL 3 +E) compared with DiI-apo E–free HDL (HDL 3 −E) ( P =0.003). To investigate possible mechanisms responsible for retention, we assessed binding of unlabeled HDL 3 −E and HDL 3 +E to ECM generated by cultured arterial smooth muscle cells. Similar to the in situ carotid artery data, HDL 3 +E bound better to the ECM than did HDL 3 −E (3-fold lower K a and 3.5-fold higher B max for HDL 3 +E versus HDL 3 −E). These differences were eliminated after either neutralization of arginine residues on apo E or digestion of matrix with chondroitin ABC lyase, suggesting that chondroitin and/or dermatan sulfate proteoglycans were responsible for apo E–mediated increased binding. These findings demonstrate that HDL can bind to both intact murine carotid arteries and smooth muscle cell–derived ECM, and that apo E is a principal determinant in mediating the ability of HDL to be trapped and retained via its interaction with ECM proteoglycans.

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Authors
Olin-Lewis, K., Benton, J. L., Rutledge, J. C., Baskin, D. G., Wight, T. N., & Chait, A.
Affiliations
  • From the Departments of Medicine (K.O.-L., D.G.B., A.C.) and Pathology (T.N.W.), University of Washington, Seattle, Wash; and the Department of Medicine (J.L.B., J.C.R.), University of California, Davis, Calif. Present address for T.N.W. is The Hope Heart Institute, Seattle, Wash.
  • University of Washington (US)
ORCID
Venue
Circulation Research
Publisher
Ovid Technologies (Wolters Kluwer Health)
Published
2002-06-28
Volume
90
Issue
12
Pages
1333-1339
ISSN
  • 0009-7330 (ISSN-L)
  • 1524-4571
DOI
10.1161/01.res.0000024691.82864.f0
OpenAlex
W2163426832
Cited by
19
References
38
Citations by year
2022: 1 · 2017: 1 · 2016: 2 · 2015: 1 · 2014: 2 · 2013: 1
FWCI
1.59
Type
journal article
Language
en
Open access
closed
Locations
  • Circulation Research (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health
  • National Heart, Lung, and Blood Institute (HL-18645, P01HL030086, HL3-0086, HL07028, P01HL018645, HL03045, T32HL007028)
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK 02456, DK07247, DK-17047, P30DK017047, T32DK007247)
Topics
  • Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
  • Life Sciences › Immunology and Microbiology › Immunology › Atherosclerosis and Cardiovascular Diseases
  • Health Sciences › Medicine › Surgery › Lipoproteins and Cardiovascular Health
Keywords
apolipoprotein E, high-density lipoprotein, vascular wall, carotid artery, arterial smooth muscle cells, extracellular matrix, proteoglycans, chondroitin sulfate, dermatan sulfate, atherogenesis, HDL binding, arginine residues
MeSH terms
Animals, Haplorhini, Apolipoproteins E, Arteries, Carotid Arteries, Cells, Cultured, Extracellular Matrix, Lipoproteins, HDL, Mice, Inbred C57BL, Microscopy, Fluorescence, Muscle, Smooth, Vascular, Proteoglycans, Mice, Knockout, Mice

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