Binding of endostatin to endothelial heparan sulphate shows a differential requirement for specific sulphates.

@article{Blackhall2003BindingOE,
  title={Binding of endostatin to endothelial heparan sulphate shows a differential requirement for specific sulphates.},
  author={Fiona Blackhall and Catherine L. R. Merry and Malcolm Lyon and Gordon C. Jayson and Judah M Folkman and Kashi Javaherian and John Thomas Gallagher},
  journal={The Biochemical journal},
  year={2003},
  volume={375 Pt 1},
  pages={131-9}
}
Endostatin is a naturally occurring proteolytic fragment of the C-terminal domain of collagen XVIII. It inhibits angiogenesis by a mechanism that appears to involve binding to HS (heparan sulphate). We have examined the molecular interaction between endostatin and HS from micro- and macrovessel endothelial cells. Two discrete panels of oligosaccharides were prepared from metabolically radiolabelled HS, using digestion with either heparinase I or III, and then examined for their endostatin… CONTINUE READING
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