The immunologic functions of the neonatal Fc receptor for IgG.

Document Type

Article

Publication Date

1-2013

Keywords

Albumins, Animals, Antigen Presentation, Antigen-Presenting Cells, Antigens, Histocompatibility Antigens Class I, Humans, Immunoglobulin G, Mutation, Protein Binding, Protein Engineering, Protein Transport, Receptors, Fc, Receptors, IgG

JAX Location

Reprint Collection

JAX Source

J Clin Immunol 2013 Jan; 33(Suppl 1); 1:9-17.

Volume

33 Suppl 1

First Page

9

Last Page

17

ISSN

1573-2592

PMID

22948741

Abstract

Careful regulation of the body's immunoglobulin G (IgG) and albumin concentrations is necessitated by the importance of their respective functions. As such, the neonatal Fc receptor (FcRn), as a single receptor, is capable of regulating both of these molecules and has become an important focus of investigation. In addition to these essential protection functions, FcRn possesses a number of other functions that are equally as critical and are increasingly coming to attention. During the very first stages of life, FcRn mediates the passive transfer of IgG from mother to offspring both before and after birth. In the adult, FcRn regulates the persistence of both IgG and albumin in the serum as well as the movement of IgG, and any bound cargo, between different compartments of the body via transcytosis across polarized cells. FcRn is also expressed by hematopoietic cells; consistent with this, FcRn regulates MHC class II presentation and MHC class I cross-presentation by dendritic cells. As such, FcRn plays an important role in immune surveillance throughout adult life. The increasing appreciation for FcRn in both homeostatic and pathological conditions is generating an intense interest in the potential for therapeutic modulation of FcRn binding to IgG and albumin. J Clin Immunol 2013 Jan; 33(Suppl 1); 1:9-17.

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