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• W1556442394 startingPage "2112" @default.
• W1556442394 abstract "Abstract Cross-linking of Fc receptors for IgA, FcR (CD89), on monocytes/macrophages is known to enhance phagocytic activity and generation of oxygen free radicals. We provide evidence here that the FcR signals through the γ subunit of FcɛRI in U937 cells differentiated with interferon γ (IFNγ). Our results provide the first evidence that FcR-mediated signals modulate a multimolecular adaptor protein complex containing Grb2, Shc, SHIP, CrkL, Cbl, and SLP-76. Cross-linking of FcRI using anti-FcRI induces the phosphorylation of the γ subunit as detected by mobility retardation on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Stimulation of FcRI induced the tyrosine phosphorylation of Shc and increased the association of Grb2 with Shc and CrkL. Grb2 associates constitutively with Sos, and the latter undergoes mobility shift upon FcRI stimulation. The complex adapter proteins, Cbl and SLP-76, are physically associated in myeloid cells and both proteins undergo tyrosine phosphorylation upon FcR stimulation. These data indicate that the stimulation of FcR results in the modulation of adaptor complexes containing tyrosine-phosphorylated Cbl, Shc, SHIP, Grb2, and Crkl. Experiments performed with the Src kinase inhibitor, PP1, provide the first evidence that Src kinase activation is required for FcRI-induced production of superoxide anions and provide insight into the mechanism for FcR-mediated activation of downstream oxidant signaling in myeloid cells." @default.
• W1556442394 created "2016-06-24" @default.
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• W1556442394 date "1999-09-15" @default.
• W1556442394 modified "2023-10-13" @default.
• W1556442394 title "Role of Src in the Modulation of Multiple Adaptor Proteins in FcRI Oxidant Signaling" @default.
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• W1556442394 doi "https://doi.org/10.1182/blood.v94.6.2112" @default.
• W1556442394 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10477741" @default.
• W1556442394 hasPublicationYear "1999" @default.
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