Association of protein-tyrosine kinase with phospholipase C-γ1 in bone marrow-derived mouse mast cells

Hiromi Fukamachi, Yuko Kawakami, Masao Takei, Teruko Ishizaka, Kimishige Ishizaka, Toshiaki Kawakami

Research output: Contribution to journalArticle

Abstract

Bone marrow-derived mouse mast cells contain phospholipase C-γ1 (PLC-γ1), 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-γ1 antibodies contained protein-tyrosine kinase (PTK), which phosphorylated PLC-γ1 in vitro. The tyrosine kinase activity coprecipitated with PLC-γ1-anti-PLC-γ1 complexes markedly increased when the cell lysates were obtained immediately after antigen challenge. The results indicate that PTK is associated with PLC-γ1 in the mast cells and that the kinase is activated upon cross-linking of FcεRI. Neither β nor γ subunit of FcεRI nor src family PTK was coprecipitated with the PLC-γ1-anti-PLC-γ1 complexes. In situ denaturation/renaturation experiments, which detect autophosphorylated kinases, indicated that the PTK associated with PLC-γ1 was a 44-kDa protein.

Original languageEnglish (US)
Pages (from-to)9524-9528
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number20
DOIs
StatePublished - Oct 15 1992

Keywords

  • FcRI
  • Signal transduction

ASJC Scopus subject areas

  • General

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