Structural features in heparin that interact with VEGF165 and modulate its biological activity.

@article{Ono1999StructuralFI,
  title={Structural features in heparin that interact with VEGF165 and modulate its biological activity.},
  author={Katsuhiro Ono and Hiroyuki Hattori and Shunji Takeshita and Akira Kurita and Motoko Ishihara},
  journal={Glycobiology},
  year={1999},
  volume={9 7},
  pages={
          705-11
        }
}
The 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS… CONTINUE READING
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