Linked Life Data

8490183

Source:http://linkedlifedata.com/resource/pubmed/id/8490183

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1993-6-11
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2767-73
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8490183-Cell Division, pubmed-meshheading:8490183-Cells, Cultured, pubmed-meshheading:8490183-Chemotaxis, Leukocyte, pubmed-meshheading:8490183-Dose-Response Relationship, Drug, pubmed-meshheading:8490183-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8490183-Endothelial Growth Factors, pubmed-meshheading:8490183-Endothelium, Vascular, pubmed-meshheading:8490183-Humans, pubmed-meshheading:8490183-Iodine Radioisotopes, pubmed-meshheading:8490183-Kinetics, pubmed-meshheading:8490183-Lymphokines, pubmed-meshheading:8490183-Molecular Weight, pubmed-meshheading:8490183-Monocytes, pubmed-meshheading:8490183-Phosphorylation, pubmed-meshheading:8490183-Protein-Tyrosine Kinases, pubmed-meshheading:8490183-Radioligand Assay, pubmed-meshheading:8490183-Receptors, Vascular Endothelial Growth Factor, pubmed-meshheading:8490183-Time Factors, pubmed-meshheading:8490183-Umbilical Veins, pubmed-meshheading:8490183-Vascular Endothelial Growth Factor A, pubmed-meshheading:8490183-Vascular Endothelial Growth Factors
pubmed:year
1993
pubmed:articleTitle
Characterization of vascular permeability factor/vascular endothelial growth factor receptors on mononuclear phagocytes.
pubmed:affiliation
Department of Physiology, Columbia University-College of Physicians and Surgeons, New York, NY 10032.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't