Specific binding of vascular permeability factor to endothelial cells.

Biochem Biophys Res Commun

Health Sciences Division, Monsanto Corporate Research, Monsanto Company, St. Louis, Missouri 63167.

Published: February 1991

Vascular permeability factor (VPF), also known as vascular endothelial cell growth factor, has recently been purified from guinea pig, human, and bovine sources. We show that various fetal or adult endothelial cell strains originating from either capillary or large vessels possess specific high affinity and saturable binding sites for guinea pig tumor-derived [125I]VPF. Two classes of sites with KDs of approximately 10 pM and 1 nM were detected for all endothelial cell types examined. Guinea pig [125I]VPF binding to endothelial cells was inhibited by human VPF (ID50 = 0.8 ng/ml) and by suramin (ID50 = 75 micrograms/ml) but not by heparin. Cross-linking experiments revealed specific [125I]VPF-receptor complexes of two types. Most of the complexes migrated very slowing in SDS-PAGE, indicating that they were of very high molecular weight and probably highly cross-linked. A portion of the molecules migrated as 270 kDa complexes, indicating that the molecular weight of the endothelial cell VPF receptor is about 230 kDa.

Download full-text PDF

Source
http://dx.doi.org/10.1016/s0006-291x(05)81201-xDOI Listing

Publication Analysis

Top Keywords

endothelial cell
16
guinea pig
12
vascular permeability
8
permeability factor
8
endothelial cells
8
molecular weight
8
endothelial
6
specific binding
4
binding vascular
4
factor endothelial
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!