Distinct heparin binding sites on VEGF165 and its receptors revealed by their interaction with a non sulfated glycoaminoglycan (NaPaC).

@article{Benedetto2008DistinctHB,
  title={Distinct heparin binding sites on VEGF165 and its receptors revealed by their interaction with a non sulfated glycoaminoglycan (NaPaC).},
  author={M{\'e}lanie Di Benedetto and Anna Starzec and Roger Vassy and G Perret and Michel Cr{\'e}pin},
  journal={Biochimica et biophysica acta},
  year={2008},
  volume={1780 4},
  pages={723-32}
}
We previously demonstrated that a non sulfated analogue of heparin, phenylacetate carboxymethyl benzylamide dextran (NaPaC) inhibited angiogenesis. Here, we observed that NaPaC inhibited the VEGF165 binding to both VEGFR2 and NRP-1 and abolished VEGFR2 activity. Further, we explored the effects of NaPaC on VEGF165 interactions with its receptors, VEGFR2 and NRP-1, co-receptor of VEGFR2. Surface plasmon resonance and affinity gel electrophoresis showed that NaPaC interacted directly with VEGF165… CONTINUE READING
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Vascular endothelial 732 M

  • Y. Hamma-Kourbali, R. Vassy, +5 authors M. Crepin
  • Di Benedetto et al. / Biochimica et Biophysica…
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