Nishizumi H, Yamamoto T
Department of Oncology, Institute of Medical Science, University of Tokyo, Japan.
J Immunol. 1997 Mar 1;158(5):2350-5.
Signaling through the high affinity IgE receptor (Fc epsilon RI) on mast cells and basophils results in rapid increases in tyrosine phosphorylation on a number of proteins. Fc epsilon RI associates with two classes of the tyrosine kinases, the Src family kinases, such as Lyn, c-Yes, and c-Src, and the Syk kinase. In this work, using primary mast cells derived from wild-type (lyn +/+) and lyn-deficient (lyn -/-) mice, we report that Lyn plays a part in signaling via Fc epsilon RI. Unlike lyn +/+ mast cells, cross-linking of Fc epsilon RI in lyn -/- mast cells failed to induce protein-tyrosine phosphorylation of various substrates, and evoked a delayed and slow Ca2+ mobilization. However, degranulation, adhesion, and production of cytokines occurred normally in lyn -/- mast cells. Our data suggest that the activity of the other Src family kinases, such as c-Src, can complement the role of Lyn in inducing most, but not all, biologic and biochemical responses to Fc epsilon RI cross-linking.
通过肥大细胞和嗜碱性粒细胞上的高亲和力IgE受体（FcεRI）发出的信号导致多种蛋白质上的酪氨酸磷酸化迅速增加。FcεRI与两类酪氨酸激酶相关联，即Src家族激酶，如Lyn、c-Yes和c-Src，以及Syk激酶。在这项研究中，我们使用源自野生型（lyn +/+）和lyn缺陷型（lyn -/-）小鼠的原代肥大细胞，报告Lyn在通过FcεRI的信号传导中发挥作用。与lyn +/+肥大细胞不同，lyn -/-肥大细胞中FcεRI的交联未能诱导各种底物的蛋白质酪氨酸磷酸化，并引发延迟且缓慢的Ca2+动员。然而，lyn -/-肥大细胞中的脱颗粒、黏附和细胞因子产生正常发生。我们的数据表明，其他Src家族激酶，如c-Src的活性，可以补充Lyn在诱导对FcεRI交联的大多数但不是全部生物学和生化反应中的作用。
