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Blood, Vol. 94 No. 6 (September 15), 1999:
pp. 2112-2120
Role of Src in the Modulation of Multiple Adaptor Proteins in
Fc RI Oxidant Signaling
Rae-Kil Park,
Kayvon D. Izadi,
Yashwant M. Deo, and
Donald L. Durden
From the Department of Pediatrics, Herman B. Wells Center for
Pediatric Research, Indiana University School of Medicine,
Indianapolis, IN; the Department of Microbiology and Immunology,
Wonkwang University School of Medicine, Iksan Jeonbuk, Korea; and
Medarex Inc, Annandale, NJ.
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
FcR signals through the  subunit of Fc RI in U937 cells
differentiated with interferon (IFN). Our results provide the
first evidence that FcR-mediated signals modulate a multimolecular
adaptor protein complex containing Grb2, Shc, SHIP, CrkL, Cbl, and
SLP-76. Cross-linking of FcRI using anti-FcRI induces the
phosphorylation of the subunit as detected by mobility retardation
on sodium dodecyl sulfate-polyacrylamide gel electrophoresis
(SDS-PAGE). Stimulation of FcRI 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 FcRI stimulation. The complex adapter proteins, Cbl and
SLP-76, are physically associated in myeloid cells and both proteins
undergo tyrosine phosphorylation upon FcR stimulation. These data
indicate that the stimulation of FcR 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 FcRI-induced production of superoxide anions and provide insight
into the mechanism for FcR-mediated activation of downstream oxidant
signaling in myeloid cells.
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