Specific binding of vasculotropin to bovine brain capillary endothelial cells.

Recently, a new growth factor was purified to homogeneity; its biological activity appeared to be restricted to vascular endothelial derived cells. As it was also angiogenic in vivo, it was provisionally named vasculotropin. An iodination procedure used to label vasculotropin did not damage the molecule; it was thus possible to undertake binding studies. The binding of iodinated vasculotropin to bovine brain capillary endothelial cells reached saturation at 7 ng/ml and half maximal binding occurred at 1.5 ng/ml. Scatchard analysis of the data demonstrated 2 classes of binding sites with apparent dissociation constants of 4 and 41 pM and 600 and 4,100 sites per cell respectively. The interaction was specific since an excess of unlabelled vasculotropin, but no Fibroblast Growth Factor or Transforming Growth Factor Beta almost totally abolished the binding of the tracer. A sensitive radioreceptor-assay convenient for measuring vasculotropin in biological samples is described.