DOI: 10.1161/01.atv.17.11.2350. High-Density Lipoprotein-Binding Protein (HBP)/Vigilin Is Expressed in Human Atherosclerotic Lesions and Colocalizes With Apolipoprotein E

High-Density Lipoprotein-Binding Protein (HBP)/Vigilin Is Expressed in Human Atherosclerotic Lesions and Colocalizes With Apolipoprotein E

10.1161/01.atv.17.11.2350

Crossref journal-article

Ovid Technologies (Wolters Kluwer Health)

Arteriosclerosis, Thrombosis, and Vascular Biology (276)

Abstract

Abstract Accumulation of cholesteryl esters within cells of the arterial intima is a hallmark of atherosclerosis. A small number of proteins have been shown in vitro to be upregulated by cellular cholesterol loading, including apolipoprotein E (apoE) and the recently cloned HDL-binding protein (HBP), but only apoE has been shown to be upregulated in cholesterol-loaded cells in atherosclerosis. To determine whether HBP (also called vigilin) might be expressed in human atherosclerosis, immunohistochemistry and in situ hybridization were performed on coronary arteries of 18 patients. HBP/vigilin was detected on all endothelial cells. HBP/vigilin mRNA and protein also were detected on a subset of macrophages and occasionally on smooth muscle cells (SMC) in atherosclerotic plaques but were not detected on these cell types in nondiseased coronary intima. The majority of HBP/vigilin-expressing macrophages were foam cells, but HBP/vigilin expression also was detected rarely in nonfoam cell macrophages. Foam cell macrophage HBP/vigilin expression was present in 100% of atherosclerotic quadrants, and nonfoam cell macrophage HBP/vigilin expression was present in 6% of atherosclerotic quadrants. HBP/vigilin-expressing human plaque cells also expressed apoE. However, HBP/vigilin was detected in cardiac myocyte foam cells of an apoE-deficient mouse, demonstrating that HBP/vigilin expression can occur independently of apoE. These results suggest that in vivo HBP/vigilin expression is upregulated by intracellular cholesterol loading but also that other factors present in atherosclerotic plaques may upregulate HBP/vigilin. Although the exact function of HBP/vigilin is unknown, its expression in plaque macrophages suggests a role for this molecule in atherogenesis.

Bibliography

Chiu, D. S., Oram, J. F., LeBoeuf, R. C., Alpers, C. E., & OâBrien, K. D. (1997). High-Density Lipoprotein-Binding Protein (HBP)/Vigilin Is Expressed in Human Atherosclerotic Lesions and Colocalizes With Apolipoprotein E. Arteriosclerosis, Thrombosis, and Vascular Biology, 17(11), 2350â2358.

Authors 5

Diane S. Chiu (first)
John F. Oram (additional)
Renee C. LeBoeuf (additional)
Charles E. Alpers (additional)
Kevin D. O’Brien (additional)

References 34 Referenced 25

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Nazih-Sanderson F Lestavel S Nion S Rouy D Denefle P Fruchart JC Clavey V Delbart C. HDL3 binds to glycosylphosphatidylinositol-anchored proteins to activate signalling pathways. Biochim Biophys Acta . 1997. In Press. (10.1016/S0167-4889(97)00055-4)

Dates

Type	When
Created	14 years, 2 months ago (June 17, 2011, 3:44 p.m.)
Deposited	3 years, 5 months ago (March 17, 2022, 2:48 p.m.)
Indexed	4 months ago (April 22, 2025, 2:46 a.m.)
Issued	27 years, 9 months ago (Nov. 1, 1997)
Published	27 years, 9 months ago (Nov. 1, 1997)
Published Print	27 years, 9 months ago (Nov. 1, 1997)

Funders 0

None

BibTeX

@article{Chiu_1997, title={High-Density Lipoprotein-Binding Protein (HBP)/Vigilin Is Expressed in Human Atherosclerotic Lesions and Colocalizes With Apolipoprotein E}, volume={17}, ISSN={1524-4636}, url={http://dx.doi.org/10.1161/01.atv.17.11.2350}, DOI={10.1161/01.atv.17.11.2350}, number={11}, journal={Arteriosclerosis, Thrombosis, and Vascular Biology}, publisher={Ovid Technologies (Wolters Kluwer Health)}, author={Chiu, Diane S. and Oram, John F. and LeBoeuf, Renee C. and Alpers, Charles E. and O’Brien, Kevin D.}, year={1997}, month=nov, pages={2350–2358} }

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