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Characterization of vascular permeability factor/vascular endothelial
growth factor receptors on mononuclear phagocytes
H Shen, M Clauss, J Ryan, AM Schmidt, P Tijburg, L Borden, D Connolly, D Stern and J Kao
Department of Physiology, Columbia University-College of Physicians and
Surgeons, New York, NY 10032.
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.
Volume 81,
Issue 10,
pp. 2767-2773,
05/15/1993
Copyright © 1993 by The American Society of Hematology
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