Source:http://linkedlifedata.com/resource/pubmed/id/16251720
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2005-12-30
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein A-I,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/moesin
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-2275
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
47
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
78-86
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16251720-Amino Acid Sequence,
pubmed-meshheading:16251720-Antibodies, Monoclonal,
pubmed-meshheading:16251720-Apolipoprotein A-I,
pubmed-meshheading:16251720-Biological Transport, Active,
pubmed-meshheading:16251720-Carrier Proteins,
pubmed-meshheading:16251720-Cell Differentiation,
pubmed-meshheading:16251720-Cell Line,
pubmed-meshheading:16251720-Cell Membrane,
pubmed-meshheading:16251720-Cholesterol,
pubmed-meshheading:16251720-Glycosylphosphatidylinositols,
pubmed-meshheading:16251720-Humans,
pubmed-meshheading:16251720-Lipoproteins, HDL,
pubmed-meshheading:16251720-Macrophages,
pubmed-meshheading:16251720-Membrane Proteins,
pubmed-meshheading:16251720-Microfilament Proteins,
pubmed-meshheading:16251720-Molecular Weight,
pubmed-meshheading:16251720-Monocytes
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pubmed:year |
2006
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pubmed:articleTitle |
Cell surface-expressed moesin-like HDL/apoA-I binding protein promotes cholesterol efflux from human macrophages.
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pubmed:affiliation |
Medical Center for Translational Research, Osaka University Hospital, 2-15 Yamada-oka, Suita.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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