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Release of Fc gamma RIIa2 by activated platelets and inhibition of anti-
CD9-mediated platelet aggregation by recombinant Fc gamma RIIa2
C Gachet, A Astier, H de la Salle, C de la Salle, WH Fridman, JP Cazenave, D Hanau and JL Teillaud
INSERM Unite 311, Centre Regional de Transfusion Sanguine de Strasbourg,
France.
Thrombin-activated human platelets and megakaryocyte cell lines release
soluble Fc gamma RII (Fc gamma RIIa2) containing the extracellular and
intracellular regions of Fc gamma RIIa1, but lacking the transmembrane
domain. Use of polyclonal antibodies directed either against the entire
intracytoplasmic tail, or against a peptide located near the C-terminal
part of the intracellular region of Fc gamma RIIa2, showed the presence of
both a complete form of Fc gamma RIIa2 and a C-terminal truncated form in
supernatants of platelets after release of their alpha granule contents and
in culture supernatants of megakaryocyte cell lines. Furthermore,
recombinant Fc gamma RIIa2 inhibited in a dose-dependent manner
Fc-dependent anti-CD9 antibody-induced platelet aggregation. Thus, release
of Fc gamma RIIa2 by activated platelets could play an important role in
the regulation of platelet activation by immune complexes.
Volume 85,
Issue 3,
pp. 698-704,
02/01/1995
Copyright © 1995 by The American Society of Hematology
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