Article
Endostatin's heparan sulfate-binding site is essential for inhibition of angiogenesis and enhances in situ binding to capillary-like structures in bone explants.
Matrix biology : journal of the International Society for Matrix Biology - 1 Jan 2005
Gaetzner Sabine, Deckers Martine M L, Stahl Sonja, Löwik Clemens, Olsen Bjorn R, Felbor Ute
Abstract excerpt
The functional role of endostatin's affinity for heparan sulfates was addressed using an ex vivo bone angiogenesis model. Capillary-like sprouts showed prominent expression of collagen XVIII/endostatin. Outgrowth of endothelial cells was not altered in the absence of collagen XVIII but inhibited by the addition of recombinant endostatin. Mutant non-heparan sulfate binding endostatin and the collagen XV endostatin...
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