
doi: 10.1111/imr.12331
pmid: 26497526
Summary The neonatal Fc receptor, FcRn, is best known for its role in transporting IgG in various tissues, providing newborns with humoral immunity, and for prolonging the half‐life of IgG. Recent findings implicate the involvement of FcRn in a far wider range of biological and immunological processes, as FcRn has been found to bind and extend the half‐life of albumin; to be involved in IgG transport and antigen sampling at mucosal surfaces; and to be crucial for efficient IgG‐mediated phagocytosis. Herein, the function of FcRn will be reviewed, with emphasis on its recently documented significance for IgG polymorphisms affecting the half‐life and biodistribution of IgG3, on its role in phagocyte biology, and the subsequent role for the presentation of antigens to lymphocytes.
Models, Molecular, Antigen Presentation, Protein Conformation, Histocompatibility Antigens Class I, Age Factors, Immunity, Receptors, Fc, Protein Transport, Structure-Activity Relationship, Phagocytosis, Immunoglobulin G, Host-Pathogen Interactions, Animals, Humans, Transcytosis, Protein Binding, Signal Transduction
Models, Molecular, Antigen Presentation, Protein Conformation, Histocompatibility Antigens Class I, Age Factors, Immunity, Receptors, Fc, Protein Transport, Structure-Activity Relationship, Phagocytosis, Immunoglobulin G, Host-Pathogen Interactions, Animals, Humans, Transcytosis, Protein Binding, Signal Transduction
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