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Human platelet aggregation by murine monoclonal antiplatelet antibodies is
subtype-dependent
S De Reys, C Blom, B Lepoudre, PJ Declerck, M De Ley, J Vermylen and H Deckmyn
Center for Thrombosis and Vascular Research, Faculty of Medicine,
University of Leuven, Belgium.
Twenty murine monoclonal antibodies (MoAbs) generated against different
human platelet antigens induced clumping of human platelets in plasma and
buffer. Whereas one MoAb could agglutinate platelets, clumping for 19 MoAbs
was blocked by metabolic inhibitors, indicating that these induce platelet
activation. Fifteen MoAbs were of IgG1, two of IgG2a, and two of IgG2b
subtype. F(ab')2 fragments of these did not evoke an aggregatory response,
but specifically inhibited aggregations by and binding of their respective
intact MoAbs to platelets. Single-platelet counting technology indicated
that the MoAbs bind through their antigen- binding and Fc domains mainly to
the surface of the same platelet, rather than cause interplatelet-binding.
Despite these similarities, the mechanism of action was nevertheless
subtype-dependent. Aggregation induced by all IgG1 antibodies could
consistently be prevented by blocking the Fc gamma II-receptor, whereas
aggregations induced by all IgG2 antibodies still occurred with blocked
Fc-receptor, provided functional complement was present. We therefore
conclude that platelet activation by MoAb-binding is initiated by antigen
recognition followed by an Fc domain-dependent step, which involves the Fc
gamma II-receptor for IgG1-type MoAbs and complement-binding for IgG2-type
MoAbs. Thus, antibodies of different subtypes can aggregate platelets via
different pathways.
Volume 81,
Issue 7,
pp. 1792-1800,
04/01/1993
Copyright © 1993 by The American Society of Hematology
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