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Neutrophil activation through high-affinity Fc gamma receptor using a
monomeric antibody with unique properties
WL Akerley , PM Guyre and BH Davis
Department of Pathology, Dartmouth-Hitchcock Medical Center, Hanover, NH
03756.
The high-affinity, type I Ig Fc receptor (Fc gamma RI) for human IgG1,
human IgG3, murine IgG2a, and murine IgG3 is highly expressed on monocytes,
neutrophils (PMN) in certain disease states, and phagocytes treated with
interferon-gamma (IFN-gamma). We studied the activation of the human PMN
oxidative burst and stimulated fluid pinocytosis induced by three
monoclonal antibodies (MoAbs) directed against Fc gamma RI (CD64) to study
the role of this receptor in Fc-mediated cellular activation. All three
MoAbs were capable of triggering PMN activation from IFN-gamma-treated PMN
when cross-linked with goat antimurine Ig reagents. However, MoAb 197 alone
demonstrated a concentration- dependent activation of the oxidative burst
without the use of a second cross-linking antibody. The oxidative burst and
stimulated fluid pinocytosis responses induced by monomeric MoAb 197 could
be elicited only after the IFN-gamma induction of approximately 8,000 Fc
gamma RI receptor equivalents and did not occur in freshly isolated or
control- cultured PMN. Competitive blocking of Fc binding of MoAb 197 by
human IgG or purified Fc fragments inhibited cellular activation. We
believe the ability of MoAb 197 to activate these oxidative burst and fluid
pinocytic responses was because of its murine IgG2a subclass, which allowed
it to function as a trivalent anti-Fc gamma RI antibody binding through the
combination of its two FAB regions and the Fc domain. This study
demonstrates that the cross-linking of CD64 can activate PMN oxidative and
endocytic responses and supports a role for Fc gamma RI in the human
neutrophil inflammatory response.
Volume 77,
Issue 3,
pp. 607-615,
02/01/1991
Copyright © 1991 by The American Society of Hematology
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