Sand Kine Marita Knudsen, Bern Malin, Nilsen Jeannette, Noordzij Hanna Theodora, Sandlie Inger, Andersen Jan Terje
Department of Biosciences, Centre for Immune Regulation (CIR), University of Oslo , Oslo , Norway ; Department of Immunology, Centre for Immune Regulation (CIR), Oslo University Hospital Rikshospitalet , Oslo , Norway.
Department of Immunology, Centre for Immune Regulation (CIR), Oslo University Hospital Rikshospitalet , Oslo , Norway ; Institute of Clinical Medicine, University of Oslo , Oslo , Norway.
Front Immunol. 2015 Jan 26;5:682. doi: 10.3389/fimmu.2014.00682. eCollection 2014.
The neonatal Fc receptor (FcRn) was first found to be responsible for transporting antibodies of the immunoglobulin G (IgG) class from the mother to the fetus or neonate as well as for protecting IgG from intracellular catabolism. However, it has now become apparent that the same receptor also binds albumin and plays a fundamental role in homeostatic regulation of both IgG and albumin, as FcRn is expressed in many different cell types and organs at diverse body sites. Thus, to gain a complete understanding of the biological function of each ligand, and also their distribution in the body, an in-depth characterization of how FcRn binds and regulates the transport of both ligands is necessary. Importantly, such knowledge is also relevant when developing new drugs, as IgG and albumin are increasingly utilized in therapy. This review discusses our current structural and biological understanding of the relationship between FcRn and its ligands, with a particular focus on albumin and design of albumin-based therapeutics.
新生儿Fc受体（FcRn）最初被发现负责将免疫球蛋白G（IgG）类抗体从母体转运至胎儿或新生儿，同时保护IgG免受细胞内分解代谢的影响。然而，现在已经很明显，同一受体也能结合白蛋白，并且在IgG和白蛋白的稳态调节中发挥着重要作用，因为FcRn在身体不同部位的多种不同细胞类型和器官中都有表达。因此，为了全面了解每种配体的生物学功能及其在体内的分布，深入研究FcRn如何结合并调节这两种配体的转运是必要的。重要的是，在开发新药时，这些知识也具有相关性，因为IgG和白蛋白在治疗中的应用越来越广泛。本综述讨论了我们目前对FcRn与其配体之间关系的结构和生物学理解，特别关注白蛋白以及基于白蛋白的治疗药物的设计。
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