Functional polymorphism of IgG FcRII (CD32) on human neutrophils.
In this study we demonstrate that Fc gamma RII on polymorphonuclear cells (PMN) (i) mediates binding of immune complexes, and (ii) is polymorphic, similar to the polymorphism described for monocytes and platelets. This was demonstrated in an adherence assay of PMN to activated human umbilical vein endothelial cells (HUVEC). Precoating of activated HUVEC with a mouse IgG1 monoclonal antibody (mAb) ENA1, which is highly reactive with activated HUVEC, caused an enhanced adhesion in 11 of 15 experiments using PMN from different donors. Enhanced adhesion of the PMN corresponded with expression of a high-responder (HR) Fc gamma RII on monocytes isolated from the same donor, as identified by anti-CD3-induced T-cell proliferation. These data led to the conclusion that Fc gamma RII on PMN is polymorphic. This conclusion was, furthermore, supported by immunofluorescence (IF) studies using a new mAb 41H16, which selectively reacts with the HR allotype of Fc gamma RII.
Leeuwenberg
J F
JF
Department of Surgery, University of Limburg, Maastricht, The Netherlands.
Van de Winkel
J G
JG
Jeunhomme
T M
TM
Buurman
W A
WA
D000936:Antigen-Antibody Complex / Q000378:metabolism; D000943:Antigens, Differentiation / Q000276:immunology*; D004730:Endothelium, Vascular / Q000276:immunology; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism; D009504:Neutrophils / Q000276:immunology* / Q000378:metabolism; D017452:Receptors, IgG
D000936:Antigen-Antibody Complex; D000943:Antigens, Differentiation; D007074:Immunoglobulin G; D017452:Receptors, IgG