Endostatin's heparan sulfate-binding site is essential for inhibition of angiogenesis and enhances in situ binding to capillary-like structures in bone explants |
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Authors: | Sabine Gaetzner, Martine M.L. Deckers, Sonja Stahl, Clemens L wik, Bjorn R. Olsen,Ute Felbor |
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Affiliation: | Department of Human Genetics, University of Würzburg, Biozentrum, Am Hubland, D-97074 Würzburg, Germany. |
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Abstract: | 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 homologue were ineffective. The ability of mutant endostatin to bind to capillary structures was reduced when compared to endostatin. Endostatin-XV completely failed to bind to endothelial cells. Our data indicate that endostatin's angiostatic function is heparan sulfate-dependent, and that in situ-binding of endostatin to endothelial cells is increased by heparan sulfates. |
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Keywords: | Endostatin Collagen XVIII Collagen XV Heparan sulfate Bone angiogenesis |
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