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J Biol Chem, Vol. 274, Issue 16, 10816-10822, April 16, 1999
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From the Glypican-1 is a member of a family of
glycosylphosphatidylinositol anchored cell surface heparan sulfate
proteoglycans implicated in the control of cellular growth and
differentiation. The 165-amino acid form of vascular endothelial growth
factor (VEGF165) is a mitogen for endothelial cells
and a potent angiogenic factor in vivo. Heparin binds to
VEGF165 and enhances its binding to VEGF receptors.
However, native HSPGs that bind VEGF165 and modulate its
receptor binding have not been identified. Among the glypicans, glypican-1 is the only member that is expressed in the vascular system.
We have therefore examined whether glypican-1 can interact with
VEGF165. Glypican-1 from rat myoblasts binds specifically to VEGF165 but not to VEGF121. The binding has
an apparent dissociation constant of 3 × 10 Department of Biology, Technion-Israel
Institute of Technology, Haifa 32000, Israel, the § Center
for Human Genetics, University of Leuven and Flanders Interuniversity,
Institute for Biotechnology, Campus Gasthuisberg O & N6, Herestraat,
B-3000 Leuven, Belgium, and the ¶ ImClone Systems Inc.,
New York, New York 10014
10
M. The binding of glypican-1 to VEGF165 is
mediated by the heparan sulfate chains of glypican-1, because
heparinase treatment abolishes this interaction. Only an excess of
heparin or heparan sulfates but not other types of glycosaminoglycans
inhibited this interaction. VEGF165 interacts specifically
not only with rat myoblast glypican-1 but also with human endothelial
cell-derived glypican-1. The binding of
125I-VEGF165 to heparinase-treated human
vascular endothelial cells is reduced following heparinase treatment,
and addition of glypican-1 restores the binding. Glypican-1 also
potentiates the binding of 125I-VEGF165 to a
soluble extracellular domain of the VEGF receptor KDR/flk-1. Furthermore, we show that glypican-1 acts as an
extracellular chaperone that can restore the receptor binding ability
of VEGF165, which has been damaged by oxidation. Taken
together, these results suggest that glypican-1 may play an important
role in the control of angiogenesis by regulating the activity of
VEGF165, a regulation that may be critical under conditions
such as wound repair, in which oxidizing agents that can impair the
activity of VEGF are produced, and in situations were the
concentrations of active VEGF are limiting.
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