Abstract
Abstract Surface receptors for IgG immunoglobulins have been demonstrated on a mouse mast cell tumor growing in tissue culture. Inhibition of rosette formation between mastocytoma cells and IgG-coated SRBC by purified mouse immunoglobulins indicated receptor specificity for all known IgG globulin classes but not for IgM, IgA or light chain immunoglobulins. Pepsin-digested IgG antibody-coated SRBC did not bind to the mast cell. Mast cell receptors appear to react with immunoglobulin-antigen complexes more strongly than with immunoglobulin alone. Receptor activity was unaffected by phospholipase D, neuraminidase or azide and was reduced by phospholipase C, iodoacetamide and fluorescein isothiocyanate. Actinomycin D had no effect for periods up to 9 hr. Treatment of mast cells with trypsin enhanced receptor activity but did not alter specificity. Our initial conclusion is that the mastocytoma IgG-receptor is a stable phospholipid or phospholipoprotein which is protease-resistant.
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