作者: U. Blank , C. Ra , L. Miller , K. White , H. Metzger
DOI: 10.1038/337187A0
关键词:
摘要: The high-affinity receptor for immunoglobulin E, Fcɛ RI, is found exclusively on mast cells and basophils. When multivalent aller-gens bind to the receptor-bound IgE, consequent aggregation of receptors leads release mediators responsible allergic symptoms. In rodents RI a tetrameric complex non-covalently attached subunits: one IgE-binding α subunit, β subunit dimer disulphide-linked γ subunits1. Com-plementary DNA encoding subunits has recently been isolated2–5, but expression by transfected not yet achieved2–5. Here we report cloning cDNA propose model αβγ2 tetramer which accounts many structural features receptor. rodent surface COS 7 was expressed only when cDNAs all three were cotransfected. Successful human IgE should now be possible, eventually permit detailed analysis IgE-receptor interaction assist search therapeutically effective inhibitors.