K. Miklos et al., RAT IGG SUBCLASSES MEDIATING BINDING AND PHAGOCYTOSIS OF TARGET-CELLSBY HOMOLOGOUS MACROPHAGES, Molecular immunology, 30(14), 1993, pp. 1273-1278
Attachment and ingestion of Cr-51-labelled TNP-SRBC sensitized by rat
IgG1, IgG2a or IgG2b-type antibodies by homologous, elicited peritonea
l macrophages were studied. IgG1 was found to be the most efficient is
otype in mediating these functions. The antibody doses required for a
significant attachment were found to differ with the isotype of Ab, wh
ile doses needed for a significant phagocytosis and antibody-dependent
cellular cytotoxicity (ADCC) varied between 400-700 Ab/SRBC with all
the isotypes studied. Both binding and phagocytosis were also influenc
ed by the degree of hapten conjugation when target cells were sensitiz
ed by IgG1. Inhibition of these functions by soluble immune complexes
and monomeric immunoglobulins suggests the involvement of two Fcgamma
in binding of the three isotypes. Based on the present work and on pre
vious results we conclude that IgG2a interacts with a receptor binding
complexed IgG only (Fcgamma RII), IgG2b binds to a different receptor
which appears to bind monomeric ligand as well (Fcgamma RI), while Ig
G1 seems to interact with both types of receptor. We propose that phag
ocytosis can be mediated by both FcgammaRI and FcgammaRII.