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The neonatal Fc receptor is expressed by human retinal pigment epithelial cells and is downregulated by tumour necrosis factor-alpha
  1. Kiki van Bilsen1,2,
  2. P Martin van Hagen1,2,
  3. Jeroen Bastiaans2,3,
  4. Jan C van Meurs3,
  5. Tom Missotten3,
  6. Robert W Kuijpers4,
  7. Herbert Hooijkaas2,
  8. Gemma M Dingjan2,
  9. G Seerp Baarsma3,
  10. Willem A Dik2
  1. 1Department of Internal Medicine, Erasmus University Medical Center, Rotterdam, The Netherlands
  2. 2Department of Immunology, Erasmus University Medical Center, Rotterdam, The Netherlands
  3. 3Rotterdam Eye Hospital, Rotterdam, The Netherlands
  4. 4Department of Ophthalmology, Erasmus University Medical Center, Rotterdam, The Netherlands
  1. Correspondence to Kiki van Bilsen, Department of Internal Medicine/Clinical Immunology, Erasmus MC, University Medical Center, s-Gravendijkwal 230, 3015 CE, Rotterdam, The Netherlands; c.vanbilsen{at}erasmusmc.nl

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Introduction

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 …

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