Fc (IgG) receptors on rat basophilic leukemia cells.
Receptors for IgG and IgE on rat basophilic leukemia cells (the 2H3 subline of RBL-IV) were detected by their ability bind IgE and IgG in fluorescence or radioactive assays. The 2H3 cells have approximately two-thirds as many receptors for IgG as for IgE. The IgE receptors bind monomeric IgE with high affinity and IgE binding is uninhibited by high concentrations of monomeric or oligomeric IgG. In contrast, the IgG receptors bind both (rabbit and rat)  IgG and (rat) IgE. The affinity of IgG receptors for monomeric IgG and IgE is much lower than that of the IgE receptor for its ligand; binding of radiolabeled IgG or IgE to IgG receptors can be detected only with cross-linked oligomers. Although both receptors are sensitive to tryptic digestion than IgE receptors. Dual laser flow microfluorometric studies revealed that the numbers of IgG and IgE receptors per cell varied considerably among 2H3 cells and that the distributions of the 2 types of receptors were independent of each other. 2H3 cells released histamine through an IgE-mediated system, but cross-linked IgG, even in saturating amounts, did not elicit histamine release, nor have any effect upon IgE-induced release. Moreover, 2H3 cells would not mediate ADCC of IgG-coated chicken red blood cells.
D000818:Animals; D001491:Basophils; D001666:Binding Sites, Antibody; D001667:Binding, Competitive; D006636:Histamine Release; D007073:Immunoglobulin E; D007074:Immunoglobulin G; D007938:Leukemia / Q000276:immunology*; D010447:Peptide Hydrolases / Q000494:pharmacology; D011817:Rabbits; D051381:Rats; D011961:Receptors, Fc
D007074:Immunoglobulin G; D011961:Receptors, Fc; D007073:Immunoglobulin E; D010447:Peptide Hydrolases