FCGRT Membrane Protein Introduction

Introduction of FCGRT

FCGRT is encoded by the FCGRT gene which is located at 19q13.3. It belongs to the immunoglobulin superfamily which contains cell surface and soluble proteins participating in the recognition, binding, or adhesion processes of cells. FCGRT is a single-pass type I membrane protein, with its N-terminus on the extracellular side of the membrane and removal of its signal sequence. The molecular mass is about 39 KDa. FCGRT is like the MHC class I molecule in structure and related to beta-2-microglobulin.

Function of FCGRT Membrane Protein

FCGRT is a Fc receptor binding to the Fc region of monomeric immunoglobulins gamma. It is expressed in full-term placenta, heart, lung, liver, muscle, kidney, pancreas, and both fetal and adult small intestine. FCGRT is found in rodents for the first, it mediates the selective uptake and transport IgG, which bounds at the newborn rodent's apical surface of the intestinal epithelium, from milk. And the resultant FcRn-IgG complexes will release IgG into blood or tissue fluids. At the same time, it will help newborn animals to acquire passive immunity. Accordingly, FCGRT is possibly related to transfer of immunoglobulin G from mother to fetus. FCGRT also takes part in IgG immunoglobulin transcytosis in epithelial cells mediated by FcRn immunoglobulin receptor. Another important role of FCGRT is the protection of IgG from normal serum protein catabolism. Beyond that, FcRn can extend the half-life of IgG and serum albumin by reducing lysosomal degradation in endothelial cell.

Fig.1 Structures of human FCGRT, rat FCGRT, and the class I MHC molecule HLA-A2 (West, 2000).

Application of FCGRT Membrane Protein in Literature

1. Shubin Z., et al. Functional polymorphisms in rhesus macaque FCGRT and β2-m. Immunogenetics. 2017, 70(3): 1-5. PubMed ID: 28785825
   
   

   Authors in this article focus on genomic polymorphisms in rhesus macaque FCGRT. They test 75 animals and report the presence of a VNTR polymorphism in the promoter of FCGRT as well as a single nucleotide polymorphism in the signal peptide of β2-m.

2. Lambrecht B.N. FcRn is mother's milk to allergen tolerance. Journal of Experimental Medicine. 2017. PubMed ID: 29196507
   
   

   This article reveals the relationship between breastfeeding and the onset of food allergies in offspring by instructing T reg formation via neonatal Fc receptor (FCGRT)-mediated transfer and uptake of allergen-containing IgG immune complexes (Ig-ICs) by gut dendritic cells (DCs).

3. Chia J, et al. Half-life extended recombinant coagulation factor IX albumin fusion protein is recycled via the FcRn-mediated pathway. Journal of Biological Chemistry. 2018, 293(17): 6363-6373. PubMed ID: 29523681
   
   

   Authors in this group focus on the FCGRRT-mediated recycling of albumin and the albumin fusion protein rIX-FP. The results reveal that FCGRT-mediated recycling via the albumin moiety is a mechanism for the half-life extension of rIX-FP observed in clinical studies.

4. Egw S., et al. Direct demonstration of a neonatal Fc receptor (FcRn)-driven endosomal sorting pathway for cellular recycling of albumin. Journal of Biological Chemistry. 2017, 292(32). PubMed ID: 28637874
   
   

   This article suggests an FCGRT-dependent endosomal cellular-sorting pathway that plays a very important role in describing fundamental mechanisms of intracellular albumin recycling and the possibility to tune albumin-based therapeutic effects by FCGRT-binding affinity.

5. Pyzik M., et al. FcRn: The Architect Behind the Immune and Nonimmune Functions of IgG and Albumin. Journal of Immunology. 2015, 194(10): 4595-603. PubMed ID: 25934922
   
   

   Authors in this article summarize some of the most novel results about FCGRT biology, immune as well as nonimmune, and provide some examples of FcRn-based therapies.

FCGRT Preparation Options

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Reference

1. West, J. A. and Bjorkman P. J. (2000). Crystal structure and immunoglobulin g binding properties of the human major histocompatibility complex-related fc receptor. Biochemistry, 39(32), 9698-708.

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