| pubmed-article:8490183 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8490183 | lifeskim:mentions | umls-concept:C0031307 | lld:lifeskim |
| pubmed-article:8490183 | lifeskim:mentions | umls-concept:C0078058 | lld:lifeskim |
| pubmed-article:8490183 | lifeskim:mentions | umls-concept:C0148199 | lld:lifeskim |
| pubmed-article:8490183 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8490183 | lifeskim:mentions | umls-concept:C1513475 | lld:lifeskim |
| pubmed-article:8490183 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:8490183 | pubmed:dateCreated | 1993-6-11 | lld:pubmed |
| pubmed-article:8490183 | pubmed:abstractText | Vascular permeability factor/vascular endothelial growth factor (VPF/VEGF) is a polypeptide mediator, elaborated by certain tumors and other cell types, that exerts multiple effects on endothelium via interaction with a class of high-affinity binding sites. In this report, the interaction of VPF/VEGF with human mononuclear phagocytes (MPs) is characterized. Radioligand binding studies at 4 degrees C showed the presence of a single class of binding sites, kd approximately 300 to 500 pmol/L (approximately 20 times lower affinity than the high-affinity binding site on endothelial cells [ECs]), the occupancy of which correlated with VPF/VEGF-induced MP migration and expression of tissue factor. These binding results were paralleled by functional experiments which indicated that the same VPF/VEGF preparations were about an order of magnitude less effective in stimulating MP chemotaxis than in inducing EC proliferation. When MPs with surface-bound 125I-VPF/VEGF were warmed to 37 degrees C, endocytosis and degradation occurred. Occupancy of VPF/VEGF binding site resulted in subsequent activation of intracellular signal transduction mechanisms, as shown by an increase in MP intracellular calcium concentration. Cross-linking studies with 125I-VPF/VEGF showed a new high-molecular weight band (corresponding to putative 125I-VPF/VEGF-receptor complex), the appearance of which was blocked by excess unlabeled VPF/VEGF. Consistent with these results, immunoprecipitation of 32PO4-labeled MPs exposed to VPF/VEGF showed a single band of similar mobility, not seen in untreated controls. These results demonstrate that the interaction of VPF/VEGF with MPs, though of lower affinity than that observed with ECs, also results from interaction of the polypeptide with a specific cell-surface protein and leads to activation of intracellular transduction mechanisms. | lld:pubmed |
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| pubmed-article:8490183 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8490183 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8490183 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:8490183 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8490183 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8490183 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8490183 | pubmed:month | May | lld:pubmed |
| pubmed-article:8490183 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:8490183 | pubmed:author | pubmed-author:REESW HWH | lld:pubmed |
| pubmed-article:8490183 | pubmed:author | pubmed-author:SterzHH | lld:pubmed |
| pubmed-article:8490183 | pubmed:author | pubmed-author:KanKK | lld:pubmed |
| pubmed-article:8490183 | pubmed:author | pubmed-author:ShenHH | lld:pubmed |
| pubmed-article:8490183 | pubmed:author | pubmed-author:SchmidtA MAM | lld:pubmed |
| pubmed-article:8490183 | pubmed:author | pubmed-author:ConnollyDD | lld:pubmed |
| pubmed-article:8490183 | pubmed:author | pubmed-author:ClaussMM | lld:pubmed |
| pubmed-article:8490183 | pubmed:author | pubmed-author:BordetJJ | lld:pubmed |
| pubmed-article:8490183 | pubmed:author | pubmed-author:TijburgPP | lld:pubmed |
| pubmed-article:8490183 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8490183 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8490183 | pubmed:volume | 81 | lld:pubmed |
| pubmed-article:8490183 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8490183 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8490183 | pubmed:pagination | 2767-73 | lld:pubmed |
| pubmed-article:8490183 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8490183 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8490183 | pubmed:articleTitle | Characterization of vascular permeability factor/vascular endothelial growth factor receptors on mononuclear phagocytes. | lld:pubmed |
| pubmed-article:8490183 | pubmed:affiliation | Department of Physiology, Columbia University-College of Physicians and Surgeons, New York, NY 10032. | lld:pubmed |
| pubmed-article:8490183 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8490183 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8490183 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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