La Jolla Institute for Allergy & Immunology, La Jolla, Calif.
La Jolla Institute for Allergy & Immunology, La Jolla, Calif.
J Allergy Clin Immunol. 2016 Jun;137(6):1646-1650. doi: 10.1016/j.jaci.2015.12.1343. Epub 2016 Apr 15.
Progress in protein chemistry in the 1950s revealed that the biologic activities of proteins, such as hemoglobin and enzymes, are based on partial structures in the protein molecules. This principle suggested to us the possibility that the human antibodies responsible for induction of reaginic hypersensitivity reactions might have unique structures that are lacking in the antibody molecules involved in immunity and that the differences in the structures of human antibody molecules can be recognized by the immune systems of experimental animals. Our studies were based on the hypothesis that reaginic antibody activity is associated with a unique immunoglobulin isotype, which is now called IgE. As expected, identification of IgE facilitated the analysis of immunologic mechanisms of reaginic hypersensitivity. Subsequent studies revealed that IgE specifically bound to basophilic granulocytes and mast cells through the Fc portion of the molecules and that cross-linking of the cell-bound IgE antibody molecules by allergen induced the release of bioactive mediators, such as histamine and leukotrienes, which initiate allergic reactions.
20 世纪 50 年代蛋白质化学的进展表明，蛋白质的生物活性，如血红蛋白和酶，是基于蛋白质分子中的部分结构。这一原理使我们想到，引起过敏反应的人类抗体可能具有独特的结构，而这些结构在参与免疫的抗体分子中是缺失的，并且人类抗体分子结构的差异可以被实验动物的免疫系统识别。我们的研究基于这样一种假设，即过敏抗体活性与一种独特的免疫球蛋白同种型有关，这种同种型现在被称为 IgE。正如预期的那样，IgE 的鉴定促进了过敏反应过敏机制的分析。随后的研究表明，IgE 通过分子的 Fc 部分特异性结合到嗜碱性粒细胞和肥大细胞上，并且通过过敏原交联细胞结合的 IgE 抗体分子诱导生物活性介质的释放，如组胺和白三烯，从而引发过敏反应。
