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FcRn: The Architect Behind the Immune and Nonimmune Functions of IgG and Albumin

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JOURNAL OF IMMUNOLOGY
卷 194, 期 10, 页码 4595-4603

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AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.1403014

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  1. National Institutes of Health [DK044319, DK051362, DK053056, DK088199]
  2. Harvard Digestive Diseases Center Grant [DK034854]

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The neonatal FcR (FcRn) belongs to the extensive and functionally divergent family of MHC molecules. Contrary to classical MHC family members, FcRn possesses little diversity and is unable to present Ags. Instead, through its capacity to bind IgG and albumin with high affinity at low pH, it regulates the serum half-lives of both of these proteins. In addition, FcRn plays an important role in immunity at mucosal and systemic sites through its ability to affect the lifespan of IgG, as well as its participation in innate and adaptive immune responses. Although the details of its biology are still emerging, the ability of FcRn to rescue albumin and IgG from early degradation represents an attractive approach to alter the plasma half-life of pharmaceuticals. We review some of the most novel aspects of FcRn biology, immune as well as nonimmune, and provide some examples of FcRn-based therapies.

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