| pubmed-article:15748999 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15748999 | lifeskim:mentions | umls-concept:C0530678 | lld:lifeskim |
| pubmed-article:15748999 | lifeskim:mentions | umls-concept:C0596087 | lld:lifeskim |
| pubmed-article:15748999 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:15748999 | lifeskim:mentions | umls-concept:C1366645 | lld:lifeskim |
| pubmed-article:15748999 | lifeskim:mentions | umls-concept:C0243518 | lld:lifeskim |
| pubmed-article:15748999 | lifeskim:mentions | umls-concept:C0127400 | lld:lifeskim |
| pubmed-article:15748999 | lifeskim:mentions | umls-concept:C0443264 | lld:lifeskim |
| pubmed-article:15748999 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15748999 | pubmed:dateCreated | 2005-3-7 | lld:pubmed |
| pubmed-article:15748999 | pubmed:abstractText | Thrombospondins-1 and -2 (TSP-1, TSP-2) are matricellular glycoproteins with potent antiangiogenic activity. We have previously shown that the antiangiogenic activity of TSP-1 is mediated by the interaction of the type I repeats (TSR) with the receptor CD36, although other domains of TSP-1 have also been implicated. We now show that the antiangiogenic activity of TSP-2, which contains three TSRs but, unlike TSP-1, lacks the capacity to activate TGF-beta, is similarly dependent on CD36. Using the corneal pocket assay we found that TSP-2 did not inhibit bFGF-induced angiogenesis in CD36 null mice. We then demonstrated that (125)[I]-TSP-2 bound to murine macrophages and that binding was diminished by 70% by anti-CD36 antibody or by using cells from CD36 null animals. Solid-phase binding studies revealed that (125)[I]-TSP-2 bound to CD36/glutathione-S-transferase (GST) fusion proteins encoding the region spanning amino acids 93-120, but not amino acids 298-439. This 93-120 amino acid region, previously identified as the TSP-1 binding site, is homologous to domains on other TSP binding proteins, such as LIMP-2 and histidine-rich glycoprotein (HRGP). Finally, we showed with an immunoabsorbent binding assay that TSP-2 bound HRGP with high affinity and that HRGP blocked the antiangiogenic activity of TSP-2, acting like a "decoy" receptor. These data suggest that modulation of the TSR/CD36 system may play an important role in the regulation of the angiogenic "switch," and may provide a target for therapeutic interventions. | lld:pubmed |
| pubmed-article:15748999 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15748999 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15748999 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15748999 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15748999 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:15748999 | pubmed:issn | 0945-053X | lld:pubmed |
| pubmed-article:15748999 | pubmed:author | pubmed-author:SimantovRR | lld:pubmed |
| pubmed-article:15748999 | pubmed:author | pubmed-author:SilversteinR... | lld:pubmed |
| pubmed-article:15748999 | pubmed:author | pubmed-author:FebbraioMM | lld:pubmed |
| pubmed-article:15748999 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15748999 | pubmed:volume | 24 | lld:pubmed |
| pubmed-article:15748999 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15748999 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15748999 | pubmed:pagination | 27-34 | lld:pubmed |
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| pubmed-article:15748999 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15748999 | pubmed:articleTitle | The antiangiogenic effect of thrombospondin-2 is mediated by CD36 and modulated by histidine-rich glycoprotein. | lld:pubmed |
| pubmed-article:15748999 | pubmed:affiliation | Division of Hematology, Department of Medicine, Weill Medical College of Cornell University, New York, NY, USA. | lld:pubmed |
| pubmed-article:15748999 | pubmed:publicationType | Journal Article | lld:pubmed |
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