HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: M500425-JLR200v1 47/1/78    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Matsuyama, A. Articles by Yamashita, S. Search for Related Content PubMed PubMed Citation Articles by Matsuyama, A. Articles by Yamashita, S. Social Bookmarking                      What's this?

Journal of Lipid Research, Vol. 47, 78-86, January 2006
Copyright © 2006 by American Society for Biochemistry and Molecular Biology

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

Akifumi Matsuyama^*, Naohiko Sakai, Hisatoyo Hiraoka, Ken-ichi Hirano and Shizuya Yamashita^,1

^* Medical 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, Japan

Published, JLR Papers in Press, October 26, 2005.

¹ To whom correspondence should be addressed. e-mail: shizu{at}imed2.med.osaka-u.ac.jp

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.

Abbreviations: AcLDL, acetylated LDL; apoA-I, apolipoprotein A-I; GPI, glycosylphosphatidylinositol; IEF, isoelectric focusing; MIF, mean intensity of fluorescence; PI-PLC, phosphatidylinositol-specific phospholipase C

Supplementary key words apolipoprotein A-I • glycosylphosphatidylinositol-anchored protein • moesin-like protein • atherosclerosis

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?