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Modulation of Fcγ receptor‐mediated early events by the tyrosine phosphatase CD45 in primary human monocytes. Consequences for interleukin‐6 production
Author(s) -
Corvaïa Nathalie,
Reischl Ilona G.,
Kroemer Elisabeth,
Mudde Geert C.
Publication year - 1995
Publication title -
european journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.272
H-Index - 201
eISSN - 1521-4141
pISSN - 0014-2980
DOI - 10.1002/eji.1830250317
Subject(s) - protein tyrosine phosphatase , tyrosine phosphorylation , phosphorylation , biology , receptor , tyrosine , cytokine , microbiology and biotechnology , immunology , biochemistry
Abstract Stimulation of primary human monocytes from several donors by cross‐linking of Fcγ receptor type I (FcγRI) and FcγRII gave rise to calcium mobilization and protein tyrosine phosphorylation. These early events were not observed without cross‐linking. CD45, a transmembrane tyrosine phosphatase, when co‐cross‐linked with either FcγRI or FcγRII, could prevent FcγRI and FcγRII‐mediated calcium mobilization and protein tyrosine phosphorylation. When interleukin (IL)‐6 production was measured, we noted a strong IL‐6 production after activation of primary human monocytes by cross‐linking of FcγRI or FcγRII. In contrast to calcium mobilization and tyrosine phosphorylation of proteins, IL‐6 production was not affected by co‐cross‐linking of CD45 with either FcγRI or FcγRII. Interestingly, cross‐linking of the CD45 itself was sufficient to induce IL‐6 production. Our results show that the CD45 molecule is important in modulating early events following stimulation of primary human monocytes by cross‐linking of FcγRI or FcγRII. However, triggering of CD45 alone can also induce IL‐6 production, indicating that CD45 ligation itself can give signals and may have an important role in cytokine induction pathways.