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Cell Surface Glypicans Are Low-Affinity Endostatin Receptors

Authors
Journal
Molecular Cell
1097-2765
Publisher
Elsevier
Publication Date
Volume
7
Issue
4
Identifiers
DOI: 10.1016/s1097-2765(01)00225-8
Disciplines
  • Biology
  • Chemistry

Abstract

Abstract Endostatin, a collagen XVIII fragment, is a potent anti-angiogenic protein. We sought to identify its endothelial cell surface receptor(s). Alkaline phosphatase– tagged endostatin bound endothelial cells revealing two binding affinities. Expression cloning identified glypican, a cell surface proteoglycan as the lower-affinity receptor. Biochemical and genetic studies indicated that glypicans' heparan sulfate glycosaminoglycans were critical for endostatin binding. Furthermore, endostatin selected a specific octasulfated hexasaccharide from a sequence in heparin. We have also demonstrated a role for endostatin in renal tubular cell branching morphogenesis and show that glypicans serve as low-affinity receptors for endostatin in these cells, as in endothelial cells. Finally, antisense experiments suggest the critical importance of glypicans in mediating endostatin activities.

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