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RII (CD32) Pivotally Regulates Survival of Human Eosinophils1
Departments of Immunology and Internal Medicine, Mayo Clinic and Mayo Foundation, Rochester, MN 55905
The low-affinity IgG Fc receptor, Fc
RII (CD32), mediates various
effector functions of lymphoid and myeloid cells and is the major IgG
Fc receptor expressed by human eosinophils. We investigated whether
FcRII regulates both cell survival and death of human eosinophils.
When cultured in vitro without growth factors, most eosinophils undergo
apoptosis within 96 h. Ligation of FcRII by anti-CD32 mAb
in solution inhibited eosinophil apoptosis and prolonged survival in
the absence of growth factors. Cross-linking of human IgG bound to
FcRII by anti-human IgG Ab or of unoccupied FcRII by
aggregated human IgG also prolonged eosinophil survival. The enhanced
survival with anti-CD32 mAb was inhibited by
anti-granulocyte-macrophage-CSF (GM-CSF) mAb, suggesting that
autocrine production of GM-CSF by eosinophils mediated survival. In
fact, mRNA for GM-CSF was detected in eosinophils cultured with
anti-CD32 mAb. In contrast to mAb or ligands in solution,
anti-CD32 mAb or human IgG, when immobilized onto tissue culture
plates, facilitated eosinophil cell death even in the presence of IL-5.
Cell death induced by these immobilized ligands was accompanied by DNA
fragmentation and was inhibited when eosinophil ß2
integrin was blocked by anti-CD18 mAb, suggesting that
ß2 integrins play a key role in initiating eosinophil
apoptosis. Thus, FcRII may pivotally regulate both survival and
death of eosinophils, depending on the manner of receptor ligation and
ß2 integrin involvement. Moreover, the FcRII could
provide a novel mechanism to control the number of eosinophils at
inflammation sites in human diseases.
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