| Scavenger receptors, oxidized LDL, and atherosclerosis. | |
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MedLine Citation:
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PMID: 11795269 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Oxidized LDL (OxLDL) competes with oxidatively damaged and apoptotic cells for binding to mouse peritoneal macrophages, implying the presence of one or more common domains. However, the nature of the ligands involved has not been determined. Studies in this laboratory over the last several years provide evidence that oxidized phospholipids, present in OxLDL and also in the membrane of apoptotic cells, represent one such ligand. These oxidized phospholipids, either in the lipid phase of OxLDL or becoming attached covalently to apoprotein B during LDL oxidation, have been shown to play a major role in the binding of OxLDL to CD36 and to SR-B1 expressed in transfected cells. The lipid and protein moieties compete with each other to some extent, indicating that they are binding to at least one common site. A monoclonal antibody selected because of its reactivity with OxLDL proved to be an antibody against oxidized phospholipids (but not native phospholipids). This antibody (EO6) blocked the uptake of OxLDL by CD36 and by SR-B1 in transfected cells by as much as 80%; it also inhibited macrophage phagocytosis of apoptotic cells by about 40%. Thus, the persistence of receptors for OxLDL during evolution is probably accounted for by their role in recognition of ligands on the surfaces of oxidatively damaged or apoptotic cells. This has important implications in biology generally and specifically in atherogenesis, because apoptosis is a prominent feature of late lesions. |
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Authors:
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A Boullier; D A Bird; M K Chang; E A Dennis; P Friedman; K Gillotre-Taylor; S Hörkkö; W Palinski; O Quehenberger; P Shaw; D Steinberg; V Terpstra; J L Witztum |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review |
Journal Detail:
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Title: Annals of the New York Academy of Sciences Volume: 947 ISSN: 0077-8923 ISO Abbreviation: Ann. N. Y. Acad. Sci. Publication Date: 2001 Dec |
Date Detail:
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Created Date: 2002-01-17 Completed Date: 2002-02-01 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 7506858 Medline TA: Ann N Y Acad Sci Country: United States |
Other Details:
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Languages: eng Pagination: 214-22; discussion 222-3 Citation Subset: IM |
Affiliation:
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Department of Medicine, University of California, San Diego, La Jolla 92093, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Antigens, CD36 Apoptosis Arteriosclerosis / etiology, pathology, physiopathology* Humans Lipoproteins, LDL / blood, physiology* Membrane Proteins* Receptors, Immunologic / physiology* Receptors, Lipoprotein* Receptors, Scavenger Scavenger Receptors, Class B |
| Grant Support | |
ID/Acronym/Agency:
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HL56989/HL/NHLBI NIH HHS; HL57505/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Antigens, CD36; 0/Lipoproteins, LDL; 0/Membrane Proteins; 0/Receptors, Immunologic; 0/Receptors, Lipoprotein; 0/Receptors, Scavenger; 0/SCARB1 protein, human; 0/Scarb1 protein, mouse; 0/Scavenger Receptors, Class B; 0/oxidized low density lipoprotein |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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