Ca2+-dependent and phorbol ester activating phosphorylation of a 36K-dalton protein of rat basophilic leukemia cell membranes and immunoprecipitation of the phosphorylated protein with IgE-anti IgE system.
Endogeneous phosphorylation of rat basophilic leukemia cell membranes was investigated. EGTA specifically inhibited the phosphorylation of a protein having an approximate molecular weight of 36,000 dalton (36K-Da protein). Phosphorylation of this protein was enhanced by phorbol-12-myristate-13-acetate in the presence of phosphatidylserine. The phosphorylated 36K-Da protein was specifically immunoprecipitated with IgE and anti IgE antibody. These results suggest that the phosphorylated 36K-Da protein is the beta-chain of the receptor for IgE and that protein kinase C is involved in the phosphorylation mechanism.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000888:Antibodies, Anti-Idiotypic; D001491:Basophils / Q000378:metabolism; D002118:Calcium / Q000378:metabolism*; D004789:Enzyme Activation; D007073:Immunoglobulin E / Q000276:immunology; D007938:Leukemia / Q000378:metabolism*; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000378:metabolism*; D010704:Phorbols / Q000494:pharmacology*; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D000596:Amino Acids; D000888:Antibodies, Anti-Idiotypic; D009363:Neoplasm Proteins; D010704:Phorbols; D007073:Immunoglobulin E; D011494:Protein Kinases; D013755:Tetradecanoylphorbol Acetate; D002118:Calcium