Is IgE-Fc?RI binding and induction of target cell triggering a process involving different Fc? domains and conformational rearrangement?

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• 作者：Kricek ; F. ; Ruf ; C. ; Nechansky ; A. ; Pursch ; E. ; Rudolf ; M.P. ; Stadler ; B.M.
• 刊名：Immunology Letters
• 出版年：1997
• 出版时间：May, 1997
• 年：1997
• 卷：56
• 期：1-3
• 页码：398
• 全文大小：153 K

文摘

Introduction: Binding of IgE to its high affinity receptor (Fc?RI) is a crucial event in the pathogenesis of allergic reactions. Crosslinking of receptor-bound IgE by specific allergens triggers degranulation and modulates cytokine production of target cells (e.g. mast cells, basophils, eosinophils). IgE binds to Fc?RI via the C?3 domain in a 1:1 complex. Conformational rearrangements within FC? have been proposed to accompany the binding process (1). Furthermore, though not being directly involved in receptor binding, amino acid sequences belonging to the C?4 domain of IgE have also been speculated to play a role in the induction of anaphylactic reactions (2). Here we present experiments which support these speculations and provide tools to further evaluate this hypothesis.