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Partial characterization of a binding site for von Willebrand factor on
glycocalicin
AD Michelson, J Loscalzo, B Melnick, BS Coller and RI Handin
The binding of von Willebrand factor (vWF) to platelet membrane
glycoprotein Ib (GpIb) facilitates platelet adhesion to vascular
subendothelium. In this study, we provide evidence that the vWF binding
site is on glycocalicin (GC), a proteolytic fragment of GpIb, and we
examine the role of the carbohydrate portion of GC on that binding. The
binding to platelets of 6D1, a monoclonal antibody that recognizes an
epitope on GpIb and blocks ristocetin-induced vWF binding to platelets, was
inhibited by purified GC. In addition, purified GC inhibited
ristocetin-dependent binding of 125I-labeled vWF to platelets. Since GC
contains 60% carbohydrate by weight, we assessed the role of carbohydrate
sequences on its interaction with antibody 6D1 and vWF. Based on the known
sequence of the major oligosaccharide chain of GC--N- acetyl neuraminic
acid, galactose, N-acetyl glucosamine, N-acetyl galactosamine--we treated
GC sequentially with neuraminidase, beta- galactosidase, and
beta-N-acetylglucosaminidase. Removal of sialic acid and galactose residues
did not affect GC binding. Removal of N-acetyl glucosamine residues did not
affect GC binding to 6D1 but did decrease the ability of GC to inhibit vWF
binding to platelets, increasing the concentration needed to inhibit
binding by 50% (IC50) 40-fold. This suggests that a portion of the
oligosaccharide chains on GC contributes to the vWF binding activity of
this molecule.
Volume 67,
Issue 1,
pp. 19-26,
01/01/1986
Copyright © 1986 by The American Society of Hematology
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