2006年1月
Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophages
JOURNAL OF LIPID RESEARCH
- ,
- ,
- ,
- ,
- 巻
- 47
- 号
- 1
- 開始ページ
- 78
- 終了ページ
- 86
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1194/jlr.M500425-JLR200
- 出版者・発行元
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
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.
- リンク情報
- ID情報
-
- DOI : 10.1194/jlr.M500425-JLR200
- ISSN : 0022-2275
- eISSN : 1539-7262
- Web of Science ID : WOS:000234291300008