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J. Biol. Chem., Vol. 269, Issue 17, 12456-12461, Apr, 1994
S Tessler, P Rockwell, D Hicklin, T Cohen, BZ Levi, L Witte, IR Lemischka and G Neufeld
The 165-amino acid form of vascular endothelial growth factor (VEGF165) is
a mitogen for vascular endothelial cells and a potent angiogenic factor.
Expression of a chimeric receptor containing the extracellular domain of
the flk-1 receptor fused to the transmembrane and intracellular domains of
the human c-fms receptor in NIH-3T3 cells, resulted in the appearance of
high affinity binding sites for 125I- VEGF165 on transfected cells. The
binding of 125I-VEGF165 to the flk- 1/fms chimeric receptor of the
transfected cells as well as the VEGF165- induced autophosphorylation of
the chimeric receptors were inhibited in the presence of low concentrations
of heparin (1-10 micrograms/ml). In contrast, similar concentrations of
heparin potentiated the binding of 125I-VEGF165 to the endogenous VEGF
receptors of the transfected cells, indicating that to some extent, the
effect of heparin on 125I-VEGF165 binding is receptor type-dependent. A
soluble fusion protein containing the extracellular domain of flk-1 fused
to alkaline phosphatase (flk- 1/SEAP) was used to study the effects of
heparin on the binding of 125I- VEGF165 to flk-1 in a cell-free
environment. The fusion protein specifically inhibited VEGF165-induced
proliferation of vascular endothelial cells, but bound 125I-VEGF165
inefficiently in the absence of heparin. Addition of low concentrations of
heparin or heparan sulfate (0.1-1 microgram/ml) resulted in a strong
potentiation of 125I- VEGF165 binding, whereas higher heparin or heparan
sulfate concentrations inhibited the binding. The effect of heparin on the
binding of 125I-VEGF165 to flk-1/SEAP could not be mimicked by desulfated
heparin or by chondroitin sulfate. Both bFGF and aFGF inhibited the binding
when low concentrations of heparin were added to the binding reaction.
However, higher concentrations of heparin abolished the inhibition,
indicating that the inhibition is probably caused by competition for
available heparin. Taken as a whole, these results indicate that
heparin-like molecules regulate the binding of VEGF165 to its receptors in
complex ways which depend on the heparin binding properties of VEGF165, on
the specific VEGF receptor type involved, and on the amount and composition
of heparin-like molecules that are present on the cell surface of VEGF
receptor containing cells.
Heparin modulates the interaction of VEGF165 with soluble and cell associated flk-1 receptors
Department of Biology, Technion, Israel Institute of Technology, Haifa.
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