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- W2024972268 abstract "Abstract Here, we report that the MHC class I-related neonatal Fc receptor (FcRn) is expressed within azurophilic and specific granules of neutrophils and relocates to phagolysosomes on phagocytosis of IgG-opsonized bacteria. We found FcRn to enhance phagocytosis in a pH-dependent manner which was independent of IgG recycling. IgG-opsonized bacteria were inefficiently phagocytosed by neutrophils from β2M knock-out or FcRn α-chain knock-out mice, which both lack expression of FcRn. Similarly, low phagocytic activity was also observed with mutated IgG (H435A), which is incapable of binding to FcRn, while retaining normal binding to classical leukocyte Fcγ receptors. Finally, a TAT peptide representing intracellular endocytosis and transport motifs within FcRn strongly inhibited IgG-mediated phagocytosis. These findings support a novel concept in which FcRn fulfills a major role in IgG-mediated phagocytosis." @default.
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- W2024972268 date "2006-11-15" @default.
- W2024972268 modified "2023-10-17" @default.
- W2024972268 title "FcRn: an IgG receptor on phagocytes with a novel role in phagocytosis" @default.
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- W2024972268 doi "https://doi.org/10.1182/blood-2006-05-024539" @default.
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