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Specific binding of vascular permeability factor to endothelial cells
J V Olander1, D T Connolly, J E DeLarco
1Health Sciences Division, Monsanto Corporate Research, Monsanto Company, St. Louis, Missouri 63167.
Biochemical and Biophysical Research Communications
|February 28, 1991
Summary
Researchers identified specific binding sites for vascular permeability factor (VPF), also known as vascular endothelial cell growth factor, on endothelial cells. These findings reveal the molecular characteristics of the VPF receptor.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Vascular permeability factor (VPF), also known as vascular endothelial cell growth factor, has been purified from multiple sources.
- Endothelial cells play a crucial role in vascular functions.
Purpose of the Study:
- To investigate the presence and characteristics of VPF binding sites on endothelial cells.
- To identify the molecular properties of the VPF receptor.
Main Methods:
- Radioligand binding assays using [125I]VPF with various endothelial cell strains.
- Inhibition studies with human VPF and suramin.
- Cross-linking experiments followed by SDS-PAGE analysis.
Main Results:
- Endothelial cells from fetal and adult sources, including capillary and large vessels, exhibit specific, high-affinity binding sites for VPF.
- Two classes of binding sites were identified with dissociation constants (KDs) of approximately 10 pM and 1 nM.
- VPF binding was inhibited by human VPF and suramin, but not by heparin.
- Cross-linking experiments revealed two types of VPF-receptor complexes, with some migrating at 270 kDa, suggesting a receptor molecular weight of approximately 230 kDa.
Conclusions:
- Endothelial cells possess specific receptors for vascular permeability factor.
- The VPF receptor is approximately 230 kDa and exhibits high affinity for VPF.