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- W4313333831 abstract "Abstract Previously, we have demonstrated that phagocytosis of IgG1-coated particles by macrophages in vitro is impaired by deletion of FcγRIII in mice, suggesting that IgG1 may interact preferentially with FcγRIII. In the present study, the biologic relevance of this observation was addressed by triggering various effector functions of the immune system in FcγRIII−/− mice, using panels of mAbs of different IgG subclasses. Both binding and phagocytosis of IgG1-coated sheep or human erythrocytes by FcγRIII−/− macrophages in vitro were strongly impaired, indicating that the impaired ingestion of complexed IgG1 by FcγRIII−/−macrophages is due to a defect in binding. An in vivo consequence of the defective phagocytosis was observed by resistance of FcγRIII-deficient mice to experimental autoimmune hemolytic anemia, as shown by a lack of IgG1-mediated erythrophagocytosis in vivo by liver macrophages. Furthermore, trapping of soluble IgG1-containing immune complexes by follicular dendritic cells in mesenteric lymph nodes from FcγRIII−/− mice was abolished. Whole blood from FcγRIII−/− mice was unable to induce lysis of tumor cells in the presence of IgG1 antitumor Abs. Finally, IgG1 mAbs proved unable to mount a passive cutaneous anaphylaxis in FcγRIII−/− mice. Together, these results demonstrate that IgG1 complexes, either in particulate or in soluble form, trigger in vitro and in vivo immune effector functions in mice predominantly via FcγRIII." @default.
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- W4313333831 date "1998-09-15" @default.
- W4313333831 modified "2023-10-16" @default.
- W4313333831 title "Murine IgG1 Complexes Trigger Immune Effector Functions Predominantly via FcγRIII (CD16)" @default.
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- W4313333831 doi "https://doi.org/10.4049/jimmunol.161.6.3026" @default.
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