Journal
MOLECULAR CELL
Volume 7, Issue 4, Pages 811-822Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(01)00225-8
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Endostatin, a collagen XVIII fragment, is a potent antiangiogenic 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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