Open AccessFcR γ-Chain Dependent Signaling in Immature Neutrophils Is Mediated by FcαRI, but Not by FcγRI
Author(s) -
Marielle A. Otten,
Jeanette H.W. Leusen,
Esther Rudolph,
Joke A. van der Linden,
Robert H.J. Beelen,
Jan G. J. van de Winkel,
Marjolein van Egmond
Publication year - 2007
Publication title -
the journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.737
H-Index - 372
eISSN - 1550-6606
pISSN - 0022-1767
DOI - 10.4049/jimmunol.179.5.2918
Subject(s) - cd64 , internalization , microbiology and biotechnology , cytolysis , immunoprecipitation , immunoglobulin light chain , lysis , transmembrane protein , chemistry , cytotoxicity , receptor , biology , immunology , flow cytometry , antibody , biochemistry , in vitro
Neutrophil-mediated tumor cell lysis is more efficiently triggered by FcalphaRI (CD89), than by FcgammaRI (CD64). This difference is most evident in immature neutrophils in which FcgammaRI-mediated tumor cell lysis is absent. In this study, we show that FcR gamma-chain-dependent functions (such as Ab-dependent cellular cytotoxicity and respiratory burst), as well as signaling (calcium mobilization and MAPK phosphorylation), were potently triggered via FcalphaRI, but not via FcgammaRI, in immature neutrophils. Internalization, an FcR gamma-chain-independent function, was, however, effectively initiated via both receptors. These data suggest an impaired functional association between FcgammaRI and the FcR gamma-chain, which prompted us to perform coimmunoprecipitation experiments. As a weaker association was observed between FcgammaRI and FcR gamma-chain, compared with FcalphaRI and FcR gamma-chain, our data support that differences between FcalphaRI- and FcgammaRI-mediated functions are attributable to dissimilarities in association with the FcR gamma-chain.
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