Role of the extracellular domain of FcεRIα in intracellular processing and surface expression of the high affinity receptor for IgE FcεRI
Role of the extracellular domain of FcεRIα in intracellular processing and surface expression of the high affinity receptor for IgE FcεRI
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DOI:
10.1016/j.molimm.2007.11.017
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发表时间:
2008-04-01
影响因子:
3.6
通讯作者:
Kinet, Jean-Pierre
中科院分区:
文献类型:
--
作者:
Hartman, Mor-Li;Lin, Shih-Yao;Kinet, Jean-Pierre
The high affinity receptor for immunoglobulin E, Fc epsilon RI, is a critical component of IgE-mediated allergic reactions. It is expressed as a tetrarner (alpha beta gamma 2) made of an IgE-binding alpha chain and a signaling module formed by the beta chain and a dimer of gamma chains. It is expressed in humans and rodents on basophils and mast cells at a high level, and, upon activation, it induces the liberation of allergy mediators. In humans a trimeric form lacking the beta chain also exists (alpha beta gamma 2). This trimeric form is expressed on antigen presenting cells where it acts to facilitate antigen presentation via IgE. Both the expression and the signaling capacity of the trimer are lower than those of the tetramer. The differences between human (tetrameric and trimeric) and murine (tetrameric only) expression is explained in part by the fact that mouse alpha cannot be expressed at the cell surface in the absence of beta, while human alpha can. Here we demonstrate that the capacity of human a to be expressed at the cell surface in the absence of beta is encoded entirely in its extracellular domain. These findings show that the extracellular domain of the type I transmernbrane protein Fc epsilon RI alpha plays a role in Fc epsilon RI intracellular processing and expression at the cell surface. (C) 2007 Elsevier Ltd. All rights reserved.