Inhibition of FcgR-mediated phagocytosis by IVIg is independent of IgG-Fc sialylation and FcgRIIb in human macrophages

نویسندگان

  • Sietse Q. Nagelkerke
  • Gillian Dekkers
  • Iwan Kustiawan
  • Fleur S. van de Bovenkamp
  • Judy Geissler
  • Rosina Plomp
  • Manfred Wuhrer
  • Gestur Vidarsson
  • Theo Rispens
  • Timo K. van den Berg
  • Taco W. Kuijpers
چکیده

Department of Blood Cell Research, Department of Experimental Immunohematology, and Department of Immunopathology, Sanquin Research, and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands; Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands; and Emma Children’s Hospital, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands

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Inhibition of FcγR-mediated phagocytosis by IVIg is independent of IgG-Fc sialylation and FcγRIIb in human macrophages.

In immune thrombocytopenia and warm autoimmune hemolytic anemia, circulating immunoglobulin G (IgG)-opsonized blood cells are cleared from the circulation by macrophages. Administration of intravenous immunoglobulin (IVIg) can prevent uptake, but the exact working mechanism is not known. The prevailing theory from murine studies, which states that Fc-sialylated IgG alters the balance between ac...

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The Src homology 2 domain-containing inositol 5'-phosphatase (SHIP) is recruited to immunoreceptor tyrosine-based inhibition motif (ITIM)-containing proteins, thereby suppressing phosphatidylinositol 3-kinase (PI 3-kinase)-dependent pathways. The role of SHIP in phagocytosis, a PI 3-kinase-dependent pathway, is unknown. Overexpression of SHIP in macrophages led to an inhibition of phagocytosis ...

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تاریخ انتشار 2014