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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1992 Oct 15;89(20):9524–9528. doi: 10.1073/pnas.89.20.9524

Association of protein-tyrosine kinase with phospholipase C-gamma 1 in bone marrow-derived mouse mast cells.

H Fukamachi 1, Y Kawakami 1, M Takei 1, T Ishizaka 1, K Ishizaka 1, T Kawakami 1
PMCID: PMC50164  PMID: 1384056

Abstract

Bone marrow-derived mouse mast cells contain phospholipase C-gamma 1 (PLC-gamma 1), which is phosphorylated at tyrosine residues upon cross-linking of cell-bound IgE antibodies with multivalent antigen. It was found that immune complexes formed from digitonin lysates of the mast cells by monoclonal anti-PLC-gamma 1 antibodies contained protein-tyrosine kinase (PTK), which phosphorylated PLC-gamma 1 in vitro. The tyrosine kinase activity coprecipitated with PLC-gamma 1-anti-PLC-gamma 1 complexes markedly increased when the cell lysates were obtained immediately after antigen challenge. The results indicate that PTK is associated with PLC-gamma 1 in the mast cells and that the kinase is activated upon cross-linking of Fc epsilon RI. Neither beta nor gamma subunit of Fc epsilon RI nor src family PTK was coprecipitated with the PLC-gamma 1-anti-PLC-gamma 1 complexes. In situ denaturation/renaturation experiments, which detect autophosphorylated kinases, indicated that the PTK associated with PLC-gamma 1 was a 44-kDa protein.

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Selected References

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