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A murine antiglycoprotein Ib complex monoclonal antibody, SZ 2, inhibits
platelet aggregation induced by both ristocetin and collagen
CG Ruan, XP Du, XD Xi, PA Castaldi and MC Berndt
A new monoclonal antibody (MoAb), SZ 2, reactive with the human platelet
glycoprotein Ib complex has been produced by the hybridoma technique. SZ 2
immunoprecipitated the components of the glycoprotein Ib complex,
glycoprotein Ib and glycoprotein IX, from Triton-X-100- solubilized,
periodate-labeled platelets. Western blot analysis indicated that the
epitope for SZ 2 was on the alpha-subunit of glycoprotein Ib. Scatchard
analysis of SZ 2 binding to formaldehyde- fixed, washed platelets revealed
a single class of binding sites with Kd = 6.6 +/- 3.3 X 10(-10) mol/L and
15,200 +/- 4,100 binding sites per platelet (mean +/- SD, n = 10). Intact
antibody and its purified (Fab')2 fragments not only inhibited the
ristocetin-dependent binding of von Willebrand factor to platelets and
ristocetin-induced platelet agglutination but also inhibited platelet
aggregation induced by Type I collagen and platelet-activating factor
(PAF). SZ 2 inhibited platelet serotonin and beta-thromboglobulin release
in response to these stimuli and also platelet thromboxane A2 formation in
response to ristocetin and collagen. SZ 2 was without effect on platelet
aggregation or release in response to other platelet stimuli such as ADP,
thrombin, or arachidonic acid. The inhibition by SZ 2 of collagen- and
PAF-induced platelet aggregation is surprising in that Bernard-Soulier
syndrome platelets, which lack the glycoprotein Ib complex, respond
normally to both these stimuli. SZ 2 was unreactive toward Bernard-Soulier
syndrome platelets, as evaluated by fluorescence-associated cell sorting,
and had no effect on the collagen- and PAF-induced aggregation of Bernard-
Soulier syndrome platelets. The combined results suggest that the
inhibition by SZ 2 of collagen- and PAF-induced aggregation of normal
platelets is steric and are consistent with the glycoprotein Ib complex and
the platelet collagen and PAF receptor(s) being adjacent in the human
platelet plasma membrane.
Volume 69,
Issue 2,
pp. 570-577,
02/01/1987
Copyright © 1987 by The American Society of Hematology
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