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J. Biochem, 1990, Vol. 108, No. 1 66-71
© 1990 Japanese Biochemical Society

research-article

Characterization of the Fc Receptor for IgG2 on Guinea Pig Polymorphonuclear Leukocytes by the Use of a Monoclonal Antibody1

Masaki Sato and Jiro Koyama

Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University Kita-ku, Sapporo, Hokkaido 060

Guinea pig polymorphonuclear leukocytes (PMNs) possess two distinct types of Fe{gamma} receptor (Fc{gamma}R): Fc{gamma}1/{gamma}2R for both IgG1 and IgG2, and Fc{gamma}2R for IgG2 alone. The Fc{gamma}2R was previously shown to differ antigenically from homologous macrophage (M{varphi}) Fc{gamma}2R by the use of a monoclonal antibody to M{varphi} Fc{gamma}2R (VIIAI IgG1), though the Fc{gamma}1/{gamma}2R cross-reacts with a monoclonal antibody to homologous M{varphi} Fc{gamma}/2R (VIA2 IgG1). Recently, we obtained a monoclonal antibody (MP-2) secreted by a hybridoma prepared by fusion of the splenic cells of mice immunized with guinea pig PMNs with a myeloma cell line. This antibody completely inhibited both the Fc{gamma}2R-mediated rosette formation of PMNs with IgG2 antibody-sensitized sheep erythrocytes and the Fc{gamma}2R-mediated binding of oval-bumin (OA)-complexed IgG2 antibody to PMNs. When the antigen of MP-2 was isolated by affinity chromatography with the antibody-Sepharose, it gave a single band with a molecular weight of 120,000 on SDS-PAGE. The number of antigen molecules per PMN was estimated to be 9x104by measuring the binding of 125I-MP-2 Fab. This value was essentially the same as that obtained by measuring the binding of OA-complexed IgG2 antibody to the PMNs treated with the Fab' of VIA2 IgG1. These results strongly suggest that MP-2 is a monoclonal antibody to PMN Fc{gamma}2R.

1This study was supported in part by Fellowships from the Japan Society for the Promotion of Science for Japanese Junior Scientists.


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