Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophages

HDL and its major component, apolipoprotein A-I (apoA-I), play a central role in reverse cholesterol transport. We recently reported the involvement of a glycosylphosphatidylinositol anchor (GPI anchor) in the binding of HDL and apoA-I on human macrophages, and purified an 80 kDa HDL/apoA-I binding...

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Main Authors: Akifumi Matsuyama, Naohiko Sakai, Hisatoyo Hiraoka, Ken-ichi Hirano, Shizuya Yamashita
Format: Article
Language:English
Published: Elsevier 2006-01-01
Series:Journal of Lipid Research
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S0022227520336579
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spelling doaj-e04b360bd2934a0d8243b58e74663ff52021-04-27T04:45:38ZengElsevierJournal of Lipid Research0022-22752006-01-014717886Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophagesAkifumi Matsuyama0Naohiko Sakai1Hisatoyo Hiraoka2Ken-ichi Hirano3Shizuya Yamashita4Medical Center for Translational Research, Osaka University Hospital, 2-15 Yamada-oka, Suita; Department of Cardiology, Osaka University Graduate School of Medicine, B5, 2-2 Yamada-oka, Suita, Osaka 565-0871, JapanMedical Center for Translational Research, Osaka University Hospital, 2-15 Yamada-oka, Suita; Department of Cardiology, Osaka University Graduate School of Medicine, B5, 2-2 Yamada-oka, Suita, Osaka 565-0871, JapanMedical Center for Translational Research, Osaka University Hospital, 2-15 Yamada-oka, Suita; Department of Cardiology, Osaka University Graduate School of Medicine, B5, 2-2 Yamada-oka, Suita, Osaka 565-0871, JapanMedical Center for Translational Research, Osaka University Hospital, 2-15 Yamada-oka, Suita; Department of Cardiology, Osaka University Graduate School of Medicine, B5, 2-2 Yamada-oka, Suita, Osaka 565-0871, JapanMedical Center for Translational Research, Osaka University Hospital, 2-15 Yamada-oka, Suita; Department of Cardiology, Osaka University Graduate School of Medicine, B5, 2-2 Yamada-oka, Suita, Osaka 565-0871, JapanHDL and its major component, apolipoprotein A-I (apoA-I), play a central role in reverse cholesterol transport. We recently reported the involvement of a glycosylphosphatidylinositol anchor (GPI anchor) in the binding of HDL and apoA-I on human macrophages, and purified an 80 kDa HDL/apoA-I binding protein. In the present study, we characterized the GPI-anchored HDL/apoA-I binding protein from macrophages. The HDL/apoA-I binding protein was purified from macrophages and digested with endopeptidase, and the resultant fragments were sequenced. Cholesterol efflux, flow cytometry, immunoblotting, and immunohistochemical analyses were performed to characterize the HDL/apoA-I binding protein. Two parts of seven amino acid sequences completely matched those of moesin. Flow cytometry, immunoblotting, and immunohistochemistry using anti-moesin antibody showed that the HDL/apoA-I binding protein was N-glycosylated and expressed on the cell surface. It was termed moesin-like protein. Treatment of macrophages with anti-moesin antibody blocked the binding of HDL/apoA-I and suppressed cholesterol efflux. The moesin-like protein was exclusively expressed on macrophages and was upregulated by cholesterol loading and cell differentiation. Our results indicate that the moesin-like HDL/apoA-I binding protein is specifically expressed on the surface of human macrophages and promotes cholesterol efflux from macrophages.—Matsuyama, A, N. Sakai, H. Hiraoka, K-i. Hirano, and S. Yamashita. Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophages.http://www.sciencedirect.com/science/article/pii/S0022227520336579apolipoprotein A-Iglycosylphosphatidylinositol-anchored proteinmoesin-like proteinatherosclerosis
collection DOAJ
language English
format Article
sources DOAJ
author Akifumi Matsuyama
Naohiko Sakai
Hisatoyo Hiraoka
Ken-ichi Hirano
Shizuya Yamashita
spellingShingle Akifumi Matsuyama
Naohiko Sakai
Hisatoyo Hiraoka
Ken-ichi Hirano
Shizuya Yamashita
Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophages
Journal of Lipid Research
apolipoprotein A-I
glycosylphosphatidylinositol-anchored protein
moesin-like protein
atherosclerosis
author_facet Akifumi Matsuyama
Naohiko Sakai
Hisatoyo Hiraoka
Ken-ichi Hirano
Shizuya Yamashita
author_sort Akifumi Matsuyama
title Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophages
title_short Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophages
title_full Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophages
title_fullStr Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophages
title_full_unstemmed Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophages
title_sort cell surface-expressed moesin-like hdl/apoa-i binding protein promotes cholesterol efflux from human macrophages
publisher Elsevier
series Journal of Lipid Research
issn 0022-2275
publishDate 2006-01-01
description HDL and its major component, apolipoprotein A-I (apoA-I), play a central role in reverse cholesterol transport. We recently reported the involvement of a glycosylphosphatidylinositol anchor (GPI anchor) in the binding of HDL and apoA-I on human macrophages, and purified an 80 kDa HDL/apoA-I binding protein. In the present study, we characterized the GPI-anchored HDL/apoA-I binding protein from macrophages. The HDL/apoA-I binding protein was purified from macrophages and digested with endopeptidase, and the resultant fragments were sequenced. Cholesterol efflux, flow cytometry, immunoblotting, and immunohistochemical analyses were performed to characterize the HDL/apoA-I binding protein. Two parts of seven amino acid sequences completely matched those of moesin. Flow cytometry, immunoblotting, and immunohistochemistry using anti-moesin antibody showed that the HDL/apoA-I binding protein was N-glycosylated and expressed on the cell surface. It was termed moesin-like protein. Treatment of macrophages with anti-moesin antibody blocked the binding of HDL/apoA-I and suppressed cholesterol efflux. The moesin-like protein was exclusively expressed on macrophages and was upregulated by cholesterol loading and cell differentiation. Our results indicate that the moesin-like HDL/apoA-I binding protein is specifically expressed on the surface of human macrophages and promotes cholesterol efflux from macrophages.—Matsuyama, A, N. Sakai, H. Hiraoka, K-i. Hirano, and S. Yamashita. Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophages.
topic apolipoprotein A-I
glycosylphosphatidylinositol-anchored protein
moesin-like protein
atherosclerosis
url http://www.sciencedirect.com/science/article/pii/S0022227520336579
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