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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Fc fragment of IgG, receptor, transporter, alpha

FcRn, neonatal Fc receptor
This gene encodes a receptor that binds the Fc region of monomeric immunoglobulin G. The encoded protein transfers immunoglobulin G antibodies from mother to fetus across the placenta. This protein also binds immunoglobulin G to protect the antibody from degradation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2009] (from NCBI)
Top mentioned proteins: CAN, IgG1, MHC, Serum albumin, V1a
Papers on FcRn
Quantitative Investigation on Correlation Between IgG and FcRn During Gestation and Lactating Periods in Rat.
Zhang et al., China. In Am J Reprod Immunol, Feb 2016
PROBLEM: IgG is transformed from maternal serum into the offspring as passive immunization by FcRn expressed in placenta and/or infant intestine.
Bisalbuminaemia due to novel mutation at a critical residue involved in recycling; Albumin Lyon (510His→Arg).
Hanss et al., Christchurch, New Zealand. In Clin Biochem, Feb 2016
However the highly conserved His510 residue is recognised as being of critical importance in albumin recycling through interaction with its savaging neonatal Fc receptor.
The role of Fc-receptors in the uptake and transport of therapeutic antibodies in the retinal pigment epithelium.
Klettner et al., Kiel, Germany. In Exp Eye Res, Feb 2016
In this study, we investigated the involvement of Fc-receptors, both Fcγ-receptors and the neonatal Fc-receptor (FcRn) in the uptake and intracellular trafficking of the VEGF-antagonists bevacizumab, aflibercept and the anti-CD20 antibody rituximab in three different model systems, primary porcine RPE cells, ARPE-19 cells and porcine RPE/choroid explants.
Recombinant factor VIII Fc (rFVIIIFc) fusion protein reduces immunogenicity and induces tolerance in hemophilia A mice.
Jiang et al., Cambridge, United States. In Cell Immunol, Jan 2016
Disruption of Fc interactions with either FcRn or Fcγ receptors diminished tolerance induction, suggesting the involvement of these pathways.
Enhanced FcRn-dependent transepithelial delivery of IgG by Fc-engineering and polymerization.
Andersen et al., Oslo, Norway. In J Control Release, Jan 2016
In both cases, the Fc secures a long serum half-life and favourable pharmacokinetics due to its pH-dependent interaction with the neonatal Fc receptor (FcRn).
The multiple facets of FcRn in immunity.
Vidarsson et al., Amsterdam, Netherlands. In Immunol Rev, Nov 2015
The neonatal Fc receptor, FcRn, is best known for its role in transporting IgG in various tissues, providing newborns with humoral immunity, and for prolonging the half-life of IgG.
Accelerating antibody discovery using transgenic animals overexpressing the neonatal Fc receptor as a result of augmented humoral immunity.
Kacskovics et al., Hungary. In Immunol Rev, Nov 2015
We have developed transgenic (Tg) mice and rabbits that overexpress the neonatal Fc receptor (FcRn), resulting in an augmented humoral immune response even if challenging antigens are used for immunization.
The role of albumin receptors in regulation of albumin homeostasis: Implications for drug delivery.
Andersen et al., Oslo, Norway. In J Control Release, Sep 2015
Here, we review our current understanding of albumin homeostasis with a particular focus on the impact of the cellular receptors, namely the neonatal Fc receptor (FcRn) and the cubilin-megalin complex, and we discuss their importance on uses of albumin in drug delivery.
Pharmacokinetic characteristics of therapeutic antibodies.
Wohlrab, Halle, Germany. In J Dtsch Dermatol Ges, Jun 2015
Also relevant is the elimination through target antigens (especially in the case of cell-bound target antigens) as well as a recycling process through binding to the neonatal Fc receptor that provides protection from lysosomal degradation.
[Nonclinical Evaluation of Next-generation Therapeutic Monoclonal Antibodies].
Kawasaki et al., In Yakugaku Zasshi, 2014
With regard to neonatal Fc receptor (FcRn), related molecules comprising the FcRn family are not known; however, critical amino acid residues involved in IgG binding are different between human and mouse.
Enhanced neonatal Fc receptor function improves protection against primate SHIV infection.
Nabel et al., Bethesda, United States. In Nature, 2014
The localization and persistence of antibodies at these sites is influenced by the neonatal Fc receptor (FcRn), whose role in protecting against infection in vivo has not been defined.
Neonatal Fc receptor expression in dendritic cells mediates protective immunity against colorectal cancer.
Blumberg et al., Boston, United States. In Immunity, 2014
Immunoglobulin G (IgG) and the neonatal Fc receptor for IgG (FcRn) have an important function in the mucosal immune system that we have now shown extends to the induction of CD8(+) T cell-mediated antitumor immunity.
The adaptable major histocompatibility complex (MHC) fold: structure and function of nonclassical and MHC class I-like molecules.
Luoma et al., Chicago, United States. In Annu Rev Immunol, 2012
Well adapted for antigen presentation, as seen for peptides in the classical MHC molecules and for lipids in CD1 molecules, the MHC fold has also been modified to perform Fc-receptor activity (e.g., FcRn) and for roles in host homeostasis (e.g., with HFE and ZAG).
Electron tomography of late stages of FcRn-mediated antibody transcytosis in neonatal rat small intestine.
Bjorkman et al., Pasadena, United States. In Mol Biol Cell, 2012
multivesicular bodies function in IgG transport while FcRn is expressed but switch to degradative functions after weaning, when the jejunum does not express FcRn or transport IgG.
Anti-carcinoembryonic antigen single-chain variable fragment antibody variants bind mouse and human neonatal Fc receptor with different affinities that reveal distinct cross-species differences in serum half-life.
Sandlie et al., Oslo, Norway. In J Biol Chem, 2012
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.
Investigation of the mechanism of clearance of AMG 386, a selective angiopoietin-1/2 neutralizing peptibody, in splenectomized, nephrectomized, and FcRn knockout rodent models.
Sun et al., Thousand Oaks, United States. In Pharm Res, 2012
AMG 386 clearance in FcRn-knockout mice was 18-fold faster at the 3-mg/kg dose.
Neonatal Fc receptor for IgG (FcRn) expressed in the gastric epithelium regulates bacterial infection in mice.
Azuma et al., Kōbe, Japan. In Mucosal Immunol, 2012
an increase in lymphoid follicles and Helicobacter bacterial load in knock-out mice
Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor.
Sandlie et al., Oslo, Norway. In Nat Commun, 2011
Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor
Efficient mucosal vaccination mediated by the neonatal Fc receptor.
Zhu et al., College Park, United States. In Nat Biotechnol, 2011
The neonatal Fc receptor (FcRn) mediates the transport of IgG across polarized epithelial cells lining mucosal surfaces.
Enhanced antibody half-life improves in vivo activity.
Desjarlais et al., Monrovia, United States. In Nat Biotechnol, 2010
Improved affinity for the neonatal Fc receptor (FcRn) is known to extend antibody half-life in vivo.
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