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Gpib binding domain of vwf comparison of botrocetin with ristocetin


, : Gpib binding domain of vwf comparison of botrocetin with ristocetin. Acta Haematologica Japonica 53(5): 793-799

We examined botrocetin, a Bothrops jararaca venom factor, that induces platelet aggregation is dependent on von Willebrand factor (vWF). The 116 kDa tryptic fragment as well as its 52/48 kDa constituent subunit of vWF inhibited botrocetin-induced binding of vWF to platelets, while fragment III-T2 had no inhibitory effect as high as 12.mu. M. The 52/48 kDa fragment extended from amino acid residue 449 to 728. Fragment III-T2, a dimer, was composed of two pairs of disulfide-linked subunits, two 35 kDa heavy chains (residues 273-511) and two 10 kDa light chains (residues 674-728). Two peptides corresponding to residues 474-488 (G10) and 694-708 (D5), which exhibited the greatest inhibitory activity on ristocetin-dependent vWF binding to platelets, had no inhibitory effect on botrocetin-induced binding. Moreover, the murine monoclonal anti-WF antibodies (RG-46 and 52K-2), selected because of their ability to block ristocetin-induced vWF-GPIb interaction, did not inhibit botrocetin mediated vWF binding to platelets. These findings suggest that the binding domain of vWF to platelets in the presence of botrocetin differs from that in the presence of ristocetin, and that the sequence comprising residues 512-673 plays a role in botrocetin-induced vWF binding to glycoprotein Ib.

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