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J Biol Chem, Vol. 274, Issue 49, 34884-34892, December 3, 1999
From the Ludwig Institute for Cancer Research, Post Office
Box 2008, Royal Melbourne Hospital, Victoria 3050 Australia
Vascular endothelial growth factor (VEGF) is a
major mediator of vasculogenesis and angiogenesis both during
development and in pathological conditions. VEGF has a variety of
effects on vascular endothelium, including the ability to stimulate
endothelial cell mitogenesis, and the potent induction of vascular
permeability. These activities are at least in part mediated by binding
to two high affinity receptors, VEGFR-1 and VEGFR-2. In this study we have made mutations of mouse VEGF in order to define the regions that
are required for VEGFR-2-mediated functions. Development of a bioassay,
which responds only to signals generated by cross-linking of VEGFR-2,
has allowed evaluation of these mutants for their ability to activate
VEGFR-2. One mutant (VEGF0), which had amino acids 83-89 of VEGF
substituted with the analogous region of the related placenta growth
factor, demonstrated significantly reduced VEGFR-2 binding compared
with wild type VEGF, indicating that this region was required for
VEGF-VEGFR-2 interaction. Intriguingly, when this mutant was evaluated
in a Miles assay for its ability to induce vascular permeability, no
difference was found when compared with wild type VEGF. In addition we
have shown that the VEGF homology domain of the structurally related
growth factor VEGF-D is capable of binding to and activating VEGFR-2
but has no vascular permeability activity, indicating that VEGFR-2
binding does not correlate with permeability activity for all VEGF
family members. These data suggest different mechanisms for
VEGF-mediated mitogenesis and vascular permeability and raise the
possibility of an alternative receptor mediating vascular permeability.
A Mutant Form of Vascular Endothelial Growth Factor (VEGF)
That Lacks VEGF Receptor-2 Activation Retains the Ability to Induce
Vascular Permeability
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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