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Cancer Research Institute and Department of Medicine, University of California School of Medicine, San Francisco, California and Walter and Eliza Hall Institute, Royal Melbourne Hospital, Victoria, Australia
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.
Footnotes
1 This work was supported in part by United States Public Health Service Grants AM 11234-04, CA 11067 and CA 18034.
2 Cancer Research Institute and Department of Medicine, University of California School of Medicine, San Francisco, California.
3 Walter and Eliza Hall Institute, Royal Melbourne Hospital, Victoria, Australia.
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