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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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 |
work_keys_str_mv |
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