FCGRT Antibody

1. As expected, recombinant factor IX (without albumin fusion) and an FcRn interaction-defective albumin variant localized to the lysosomal compartments of both FcRn-expressing and nonexpressing cells. These results indicate that FcRn-mediated recycling via the albumin moiety is a mechanism for the half-life extension of rIX-FP observed in clinical studies. PMID: 29523681
2. Regulation of the Human Fc-Neonatal Receptor alpha-Chain Gene FCGRT by MicroRNA-3181. PMID: 29302759
3. we have demonstrated that loss of FcRn expression promotes tumor cell growth and proliferation. Our data support a model in which FcRn-mediated recycling of albumin reduces amino acid availability to fuel metabolic pathways. PMID: 27974681
4. An arginine-to-histidine replacement at residue 435 in the binding domain of IgG3 to FcRn increases the transplacental transfer and half-life of malaria-specific IgG3 in young infants and is associated with reduced risk of clinical malaria during infancy. PMID: 28991911
5. these findings establish a novel mechanism of humoral protection in the eye involving FcRn and may facilitate vaccine and therapeutic development for other ocular surface diseases PMID: 28760885
6. Data suggest that, unlike albumin with low FcRn-binding affinity, albumin with high FcRn-binding affinity (due to genetic variation/genetic engineering) is directed less to lysosomes and more to endosomes, suggestive of FcRn-directed albumin salvage from lysosomal degradation. (FcRn = neonatal Fc receptor) PMID: 28637874
7. the localization of FcRn alpha-chain in fixed nasal tissue, was studied. PMID: 26634928
8. FcRn is involved in transport of aflibercept through REC in vitro. PMID: 27836572
9. this study shows that FcRn may be associated with the transport and metabolism of IgG in thyrocytes and that transport is independent of IgG type, and that FcRn may be involved in Hashimoto's thyroiditis pathogenesis PMID: 28081504
10. This review summarizes the main findings on Fc Receptor neonatal biology, function and distribution throughout different tissues. PMID: 27016466
11. The results suggest that regardless of hyperglycemia degree, it decreases FcRn expression in placenta and blood cells and compromises the production and transfer of antibodies from maternal blood to newborns. PMID: 27469170
12. Data indicate improved pharmacokinetics through enhanced neonatal Fc receptor (FcRn) interactions were apparent for a complementarity-determining region (CDR) charge-patch normalized monoclonal antibody (mAb) which was affected by non-specific clearance. PMID: 26337808
13. analysis of binding motifs in the hFCGRT promoter that interact with their corresponding (Sp1, Sp2, Sp3, c-Fos, c-Jun, YY1, and C/EBPbeta or C/EBPdelta) transcription factors (TFs) suggests their involvement in regulation of human FCGRT gene expression PMID: 26252948
14. These data indicate that human FcRn facilitates the transepithelial transport of IgE in the form of IgG anti-IgE/IgE ICs. PMID: 25652137
15. Critical Role of the Neonatal Fc Receptor (FcRn) in the Pathogenic Action of Antimitochondrial Autoantibodies Synergizing with Anti-desmoglein Autoantibodies in Pemphigus Vulgaris. PMID: 26260795
16. FcRn binding activity of a large set of Fc-fusion samples after thermal stress, was investigated. PMID: 26254986
17. The neonatal Fc receptor (FcRn) binds independently to both sites of the IgG homodimer with identical affinity. PMID: 25658443
18. These results suggest that hFcRn Tgm are a valuable and useful tool for pharmacokinetic screening of mAbs and Fc-fusion proteins in the preclinical stage. PMID: 25030041
19. The extents of IgG expression in 86 lung cancers were found to associate with clinical stage, pathological grade and lymph node metastasis. PMID: 24853685
20. Molecular dynamic simulations of human FcRn-Fc binding structures proposed that the protein-protein binding interface is composed of three subsites. PMID: 24057047
21. This mAb panel provides a powerful resource for probing the biology of human FcRn and for the evaluation of therapeutic FcRn blockade strategies. PMID: 22453095
22. domain I and III of albumin required for optimal pH-dependent binding to the neonatal Fc receptor PMID: 25344603
23. Characterization and screening of IgG binding to the neonatal Fc receptor. PMID: 24802048
24. In intestine, there was an increasing proximal-distal gradient of mucosal FcRn mRNA and protein expression. PMID: 24072267
25. A cluster of conserved tryptophan residues of FcRn is required for binding to albumin and anti-FcRn albumin blocking antibodies. PMID: 24764301
26. Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding. PMID: 24652290
27. The Neonatal Fc receptor (FcRn) enhances human immunodeficiency virus type 1 (HIV-1) transcytosis across epithelial cells. PMID: 24278022
28. analysis of neonatal Fc receptor-based recycling mechanisms through identification of the human Fc interaction with human FcRn PMID: 24469444
29. FcRn has the potential to interact with IgG-Fc domains in the ciliary epithelium and retinal and choroidal vasculature, which might affect the half-life and distribution of intravitreally injected Fc-carrying molecules. PMID: 24550358
30. Only the unbound receptor or FcRn bound to monomeric IgG is sorted into recycling tubules emerging from early endosomes. PMID: 23741050
31. Analytical FcRn chromatography allows differentiation of IgG samples and variants by peak pattern and retention time profile. PMID: 23765230
32. The FCGRT promoter VNTR may influence mAbs' distribution in the body. CNV of FCGRT cannot be used as a relevant pharmacogenetic marker because of its low frequency. PMID: 23751752
33. Studies indicate that high levels of endogenous IgG can compete with the monoclonal antibodies (mAbs) for binding to the neonatal Fc receptor (FcRn). PMID: 23917469
34. Data indicate that Fc-neonatal Fc receptor (FcRn) interaction is pH dependent. PMID: 23384837
35. Human FcRn was visualized in epithelial cells of Tg276 mice, but low serum hIgG levels were obtained PMID: 23220220
36. genetic polymorphism is associated with the efficiency of Ig replacement therapy in common variable immunodeficiency PMID: 23286945
37. Serum half-life of IgG is controlled by the neonatal Fc receptor (FcRn) that interacts with the IgG Fc region and may be increased or decreased as a function of altered FcRn binding. PMID: 22570488
38. Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor PMID: 22215085
39. FcRn transgene blockade is a primary contributing factor toward reduction in arthritis severity; engineering of antibody Fc regions to generate potent FcRn blockers holds promise for the therapy of antibody-mediated autoimmunity in experimental arthritis. PMID: 21690327
40. Thirty-three genetic variations of FCGRT, including 17 novel ones, were found. PMID: 20930418
41. These studies demonstrate that FcRn-mediated transport is a mechanism by which IgG can act locally in the female genital tract in immune surveillance and in host defense against sexually transmitted diseases. PMID: 21368166
42. Methionine (Met) oxidation can result in a significant reduction of the serum circulation half-life and the magnitude of the change correlates well with the extent of Met oxidation and changes in FcRn binding affinities. PMID: 21256596
43. promoter polymorphism is not associted with the rate of maternal-fetal IgG transfer PMID: 20452034
44. the x-ray crystal structure of a representative monomeric peptide in complex with human FcRn PMID: 20592032
45. influence of FcRn expression on disease phenotype and the catabolism of therapeutically administered intravenous immunoglobulins in 28 patients with common variable immunodeficiency PMID: 20627700
46. No binding of albumin was observed at physiological pH to neonatal Fc receptor. At acidic pH, a 100-fold difference in binding affinity was observed. PMID: 20018855
47. A recombinant truncated HSA variant, HSA(Bartin), does not interact with FcRn, which gives a molecular explanation for the low serum levels. PMID: 20006594
48. Affinities to FcRn of clinically used therapeutic proteins are closely correlated with the serum half-lives reported from clinical studies, and suggest an important role of FcRn in regulating the serum half-lives of the therapeutic proteins. PMID: 20083659
49. Human FcRn binds selectively to human, rabbit and guinea pig IgG but not significantly to rat, bovine, sheep or mouse IgG (except for weak binding to mouse IgG2b). PMID: 11717196
50. Assembly of the FcRn alpha-chain with beta(2)microglobulin is important for both transport of FcRn from the ER to the cell surface and efficient pH-dependent IgG binding. PMID: 12006623

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HGNC: 3621

OMIM: 601437

KEGG: hsa:2217

STRING: 9606.ENSP00000221466

UniGene: Hs.111903