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An oxygen-dependent mechanism of neutrophil-mediated cytotoxicity
SJ Weiss and AF LoBuglio
Human neutophils stimulated with phorbol myristate acetate were able to
rapidly destroy autologous red blood cell targets. Neutrophil-mediated
cytotoxicity was related to phorbol myristate acetate concentration and
neutrophil number. The ability of stimulated neutrophils to lyse red blood
cell targets was markedly impaired by catalase or superoxide dismutase but
not by heat-inactivated enzymes or albumin. Despite a simultaneous
requirement for O2.- and H2O2 in the cytotoxic event, a variety of OH. and
1O2 did not effect cytolysis. The myeloperoxidase inhibitor cyanide did not
reduce red blood destruction, while azide consistently impaired cytolysis.
The inability of cyanide to reduce cytotoxicity coupled with the protective
effect of superoxide dismutase suggests that cytotoxicity is independent of
the classic myeloperoxidase-H2O2-halide system. We propose that
neutrophils, stimulated with phorbol myristate acetate, generate O2.- and
H2O2, which play an integral role in a novel cytotoxic mechanism.
Volume 55,
Issue 6,
pp. 1020-1024,
06/01/1980
Copyright © 1980 by The American Society of Hematology
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