Open AccessAssociation of immunoglobulin G Fc receptor II with Src-like protein-tyrosine kinase Fgr in neutrophils.
Author(s) -
Fumihiko Hamada,
Masahiro Aoki,
Tetsu Akiyama,
Kumao Toyoshima
Publication year - 1993
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.90.13.6305
Subject(s) - proto oncogene tyrosine protein kinase src , tyrosine kinase , tyrosine phosphorylation , receptor tyrosine kinase , signal transduction , fc receptor , microbiology and biotechnology , receptor , biology , antibody , tyrosine , phosphorylation , chemistry , biochemistry , immunology
The interaction of Fc receptors with antibody-antigen complexes activates multiple biological functions in hematopoietic cells. Recently, protein-tyrosine phosphorylation has been suggested to be involved in Fc receptor-mediated cell signaling. Here we show that the Src-like protein-tyrosine kinase Fgr, which is specifically expressed in mature myelomonocytic cells, coimmunoprecipitates with IgG Fc receptor II (Fc gamma RII), but not with Fc gamma RIII from detergent lysates of human peripheral neutrophils. Crosslinking of Fc gamma RII induced a rapid increase in the tyrosine kinase activity and comodulation of Fgr. These results suggest that Fgr is physically and functionally associated with Fc gamma RII and involved in Fc gamma RII-mediated signal transduction pathways.