COMPLETE STRUCTURE AND EXPRESSION IN TRANSFECTED CELLS OF HIGH-AFFINITY IGE RECEPTOR
COMPLETE STRUCTURE AND EXPRESSION IN TRANSFECTED CELLS OF HIGH-AFFINITY IGE RECEPTOR
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DOI：
10.1038/337187a0
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发表时间：
1989-01-12
期刊：
影响因子：
64.8
通讯作者：
KINET, JP
中科院分区：
文献类型：
--
作者：
BLANK, U;RA, C;KINET, JP
免疫球蛋白E的高亲和力受体Fc ε RI仅在肥大细胞和嗜碱性粒细胞上发现。当多价过敏原与受体结合的IgE结合时，随后的受体聚集导致释放引起过敏症状的介质。在啮齿类动物中，Fc β RI是非共价连接亚基的四聚体复合物：一个IgE结合α亚基、一个β亚基和二硫键连接的γ亚基的二聚体1。编码α和β亚基的互补DNA最近已被分离2 -5，但转染细胞的IgE结合表达尚未被证实2 -5。本文报道了γ亚基cDNA的克隆，并提出了αβγ 2四聚体的模型，该模型解释了受体的许多结构特征。COS 7细胞表面的啮齿类受体只有在三个亚基的cDNA共转染时才表达。人IgE受体的成功表达现在应该是可能的，最终允许人IgE-受体相互作用的详细分析，并协助寻找治疗有效的抑制剂。
The high-affinity receptor for immunoglobulin E, FcɛRI, is found exclusively on mast cells and basophils. When multivalent aller-gens bind to the receptor-bound IgE, the consequent aggregation of the receptors leads to the release of mediators responsible for allergic symptoms. In rodents FcɛRI is a tetrameric complex of non-covalently attached subunits: one IgE-bindingαsubunit, oneβsubunit and a dimer of disulphide-linkedγsubunits1. Com-plementary DNA encoding theαand theβsubunits has recently been isolated2–5, but expression of IgE-binding by transfected cells has not yet been achieved2–5. Here we report the cloning of cDNA for theγsubunit, and propose a model for theαβγ2tetramer which accounts for many of the structural features of the receptor. The rodent receptor on the surface of COS 7 cells was expressed only when the cDNAs for all three subunits were cotransfected. Successful expression of human IgE receptors should now be possible, eventually to permit the detailed analysis of the human IgE-receptor interaction and assist the search for therapeutically effective inhibitors.