Binding to the neonatal Fc receptor enhances the pathogenicity of anti-desmoglein-3 antibodies in keratinocytes.

ABSTRACT: The neonatal Fc receptor (FcRn) is important for numerous cellular processes that involve antibody recycling and trafficking. A major function of FcRn is IgG recycling and half-life prolongation, and FcRn blockade results in a reduction of autoantibodies in IgG-mediated autoimmune diseases. In epithelial cells, FcRn functions in processes different from IgG recycling, such as antibody transcytosis in intestinal cells. In pemphigus vulgaris, an autoimmune disease of the epidermis, IgG autoantibodies directed against desmosomal adhesion proteins, especially desmoglein-3 and -1, cause loss of keratinocyte adhesion. We have previously demonstrated that FcRn blockade with efgartigimod, a human Fc fragment with enhanced FcRn binding, significantly reduces the keratinocyte monolayer fragmentation

SUBMITTER: Zakrzewicz A 

PROVIDER: S-EPMC11499148 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature