| pubmed-article:9857015 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9857015 | lifeskim:mentions | umls-concept:C0017837 | lld:lifeskim |
| pubmed-article:9857015 | lifeskim:mentions | umls-concept:C1366645 | lld:lifeskim |
| pubmed-article:9857015 | lifeskim:mentions | umls-concept:C0162768 | lld:lifeskim |
| pubmed-article:9857015 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9857015 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9857015 | lifeskim:mentions | umls-concept:C0178587 | lld:lifeskim |
| pubmed-article:9857015 | lifeskim:mentions | umls-concept:C0205251 | lld:lifeskim |
| pubmed-article:9857015 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9857015 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9857015 | pubmed:issue | 52 | lld:pubmed |
| pubmed-article:9857015 | pubmed:dateCreated | 1999-2-3 | lld:pubmed |
| pubmed-article:9857015 | pubmed:abstractText | CD36 is a multifunctional cell-surface receptor that binds adhesion molecules such as thrombospondin-1 and collagen and modified lipids and/or lipoproteins. It participates in cellular uptake of photoreceptor outer segments and scavenging of apoptotic cells and oxidized low density lipoprotein (Ox-LDL). Recognition and internalization of Ox-LDL by mononuclear phagocytes may play an important role in the development of atherosclerotic lesions. We have utilized a series of recombinant bacterial glutathione S-transferase/CD36 fusion proteins that span nearly all of the CD36 molecule to characterize the structural domain on CD36 that recognizes Ox-LDL. We found that the Ox-LDL-binding domain is different from the thrombospondin-1-binding domain located at amino acids 93-120. A fusion protein containing the region extending from amino acids 5 to 143 formed specific, saturable, and reversible complexes with Ox-LDL. As with intact CD36, binding was blocked by excess unlabeled Ox-LDL and antibodies to CD36. The stoichiometry and affinity of the fusion protein for Ox-LDL were similar to those of the intact protein. We also demonstrated that this fusion protein competitively inhibited binding of Ox-LDL to purified platelet CD36 and to CD36 expressed on peripheral blood monocytes and CD36 cDNA-transfected melanoma cells. The use of smaller peptides and fusion proteins including those spanning amino acids 28-93 and 5-93 has further narrowed the binding site to a region from amino acids 28 to 93, although participation of a sequence in the noncontiguous region 120-155 cannot be excluded. This study, for the first time, demonstrates unique regions of the scavenger receptor CD36 that bind the Ox-LDL ligand. Our structural analysis of the receptor provides information as to potential control of the trafficking of modified lipoproteins into the blood vessel wall. | lld:pubmed |
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| pubmed-article:9857015 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9857015 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9857015 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9857015 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9857015 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9857015 | pubmed:author | pubmed-author:RoyPP | lld:pubmed |
| pubmed-article:9857015 | pubmed:author | pubmed-author:SilversteinR... | lld:pubmed |
| pubmed-article:9857015 | pubmed:author | pubmed-author:HajjarD PDP | lld:pubmed |
| pubmed-article:9857015 | pubmed:author | pubmed-author:NicholsonA... | lld:pubmed |
| pubmed-article:9857015 | pubmed:author | pubmed-author:PearceS FSF | lld:pubmed |
| pubmed-article:9857015 | pubmed:author | pubmed-author:FebbraioMM | lld:pubmed |
| pubmed-article:9857015 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9857015 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:9857015 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9857015 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9857015 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9857015 | pubmed:pagination | 34875-81 | lld:pubmed |
| pubmed-article:9857015 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:9857015 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9857015 | pubmed:articleTitle | Recombinant glutathione S-transferase/CD36 fusion proteins define an oxidized low density lipoprotein-binding domain. | lld:pubmed |
| pubmed-article:9857015 | pubmed:affiliation | Department of Medicine, Division of Hematology-Oncology, Cornell University Medical College, New York, New York 10021, USA. | lld:pubmed |
| pubmed-article:9857015 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9857015 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9857015 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9857015 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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