The intracellular localization and association of porcine Ia-associated invariant chain with the MHC class I-related porcine neonatal Fc receptor for IgG

Gene ◽  
2015 ◽  
Vol 559 (1) ◽  
pp. 9-15
Author(s):  
Fazhi Xu ◽  
Hong Ye ◽  
Xuelan Liu ◽  
Fangfang Chen ◽  
Xiaoling Ding ◽  
...  
2018 ◽  
Vol 72 ◽  
pp. 701-727
Author(s):  
Joanna E. Mikulska

The neonatal Fc receptor, (FcRn) is a transmembrane, heterodimeric glycoprotein with a structure similar to MHC class I molecules. In contrast to MHC class I antigens, FcRn does not bind to peptides (antigens) but interacts with the Fc fragment of IgG and albumin. The FcRn-IgG interaction as well as the FcRn-albumin interaction occur at acidic pH (optimally at pH 5.0-6.5) but not in physiological environment. These two ligands bind to distinct binding sites on the receptor molecule and by different mechanisms. Now, it is known that the expression of FcRn is not restricted to sites involved in the transport of maternal IgG, and this receptor is not responsible only for transfer the passive immunity from mother to the offspring. But FcRn has a much broader range of expression and function, throughout life and in many different cell types and tissues of humans and animals. This review summarizes the status of our knowledge on the expression, interaction with ligands and functions of the neonatal Fc receptor. This article shows also the possibilities of utilizing a current knowledge on FcRn for therapeutic purposes.


1999 ◽  
Vol 112 (14) ◽  
pp. 2291-2299 ◽  
Author(s):  
A. Praetor ◽  
I. Ellinger ◽  
W. Hunziker

Transfer of passive immunity from mother to the fetus or newborn involves the transport of IgG across several epithelia. Depending on the species, IgG is transported prenatally across the placenta and yolk sac or is absorbed from colostrum and milk by the small intestine of the suckling newborn. In both cases apical to basolateral transepithelial transport of IgG is thought to be mediated by FcRn, an IgG Fc receptor with homology to MHC class I antigens. We have now expressed the human FcRn in polarized MDCK cells and analyzed the intracellular routing of the receptor. FcRn showed a predominant intracellular localization at steady state. Newly synthesized FcRn was delivered in a non-vectorial fashion to both the apical and basolateral surfaces of MDCK cell monolayers. Following internalization from the apical or basolateral domain, the receptor transcytosed to the opposite surface. These findings provide direct evidence for the transepithelial transport function of FcRn and indicate that the receptor undergoes multiple rounds of transcytosis.


2007 ◽  
Vol 179 (5) ◽  
pp. 2999-3011 ◽  
Author(s):  
Xindong Liu ◽  
Lilin Ye ◽  
Gregory J. Christianson ◽  
Jun-Qi Yang ◽  
Derry C. Roopenian ◽  
...  

2001 ◽  
Vol 166 (5) ◽  
pp. 3266-3276 ◽  
Author(s):  
Xiaoping Zhu ◽  
Gang Meng ◽  
Bonny L. Dickinson ◽  
Xiaotong Li ◽  
Emiko Mizoguchi ◽  
...  

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