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Role of the glycoprotein Ib-binding A1 repeat and the RGD sequence in
platelet adhesion to human recombinant von Willebrand factor
H Lankhof, YP Wu, T Vink, ME Schiphorst, HG Zerwes, PG de Groot and JJ Sixma
Department of Hematology, University Hospital, Utrecht, The Netherlands.
To assess the relative importance of the glycoprotein (GP) Ib binding
domain and the RGDS binding site in platelet adhesion to isolated von
Willebrand factor (vWF) and to collagen preincubated with vWF, we deleted
the A1 domain yielding delta A1-vWF and introduced an aspartate- to-glycine
substitution in the RGDS sequence by site-directed mutagenesis (RGGS-vWF).
Recombinant delta A1-vWF and RGGS-vWF, purified from transfected baby
hamster kidney cells, were compared with recombinant wild-type vWF (WT-vWF)
in platelet adhesion under static and flow conditions. Purified mutants
were coated on glass or on a collagen type III surface and exposed to
circulating blood in a perfusion system. Platelet adhesion under static
condition, under flow conditions, and in vWF-dependent adhesion to collagen
has an absolute requirement for GPIb-vWF interaction. The GPIIb/IIIa-vWF
interaction is required for adhesion to coated vWF under flow conditions.
Under static condition and vWF-dependent adhesion to collagen, platelet
adhesion to RGGS-vWF is similar as to WT-vWF, but platelet spreading and
aggregation are abolished.
Volume 86,
Issue 3,
pp. 1035-1042,
08/01/1995
Copyright © 1995 by The American Society of Hematology
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