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The neonatal Fc receptor (FcRn) structurally resembles major histocompatibility complex class I molecules: it comprises a heavy (α) chain—the glycosylated FcRn (40–45 kDa)—and a beta-2-microglobulin (β2M) light chain.1 Unlike the other Fcγ receptors, the FcRn does not act as a signalling receptor. Instead, it plays a pivotal role in mediating transplacental immunoglobulin G (IgG) transport from mother to fetus and IgG transport from mothermilk to breast-fed infants, hence its name. Additionally, the FcRn mediates recycling and transport of albumin and IgG throughout life.2 In vascular endothelial cells, the FcRn …
Funding Supported by ‘Stichting Wetenschappelijk Onderzoek Oogziekenhuis—Professor Dr Flieringa’ (SWOO-Flieringa), grant 2008-05.
Competing interests None.
Provenance and peer review Not commissioned; externally peer reviewed.