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Studies on anti-von Willebrand factor (vWF) monoclonal antibody NMC-4,
which inhibits both ristocetin- and botrocetin-induced vWF binding to
platelet glycoprotein Ib
Y Fujimura, Y Usami, K Titani, K Niinomi, K Nishio, T Takase, A Yoshioka and H Fukui
Department of Blood Transfusion, Nara Medical College, Kashihara City,
Japan.
Anti-von Willebrand factor (vWF) monoclonal antibody NMC-4 completely
inhibited vWF binding to platelet glycoprotein (GP) lb induced by either
ristocetin or botrocetin at an IgG concentration of approximately 10
micrograms/mL, and also blocked binding of asialo-vWF to GP lb. NMC-4
coupled beads isolated a 97-Kd fragment (Fr) from a whole tryptic digest of
vWF. The N-terminal sequencing of the nonreduced 97-Kd Fr, in combination
with amino acid analysis, showed it to be a homodimer of residues 449
through 728 of the constituent subunit. Present data, together with the
results obtained from previous studies, confirm the existence of one or
three possible inter-subunit disulfide bonds between cysteine residues 459,
462, and 464. NMC-4 bound to reduced vWF Fr(s) more weakly than to
nonreduced Fr(s), but it did not react with Fr III-T2 of vWF, a
disulfide-linked twin heterodimer of residues 273 through 511 and 674
through 728 (Marti et al, Biochemistry 26:8099, 1987). Fr III-T2 completely
inhibited ristocetin-induced vWF binding at a concentration of 100 mumol/L
but had no effect on botrocetin-induced binding. In addition, both the N-
and C-terminal polypeptides, residues 449 through 549 and 674 through 728,
generated by subdigestion of the 52/48-Kd Fr (Fujimura et al, J Biol Chem
261:381, 1986), inhibited preferentially ristocetin-induced vWF binding
without affecting to botrocetin-induced vWF binding. These findings suggest
that amino acid residues 512 through 673 of the vWF subunit are involved in
botrocetin-induced vWF binding.
Volume 77,
Issue 1,
pp. 113-120,
01/01/1991
Copyright © 1991 by The American Society of Hematology
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