Impaired tyrosine phosphorylation and Ca2+ mobilization, but not degranulation, in lyn-deficient bone marrow-derived mast cells.
Impaired tyrosine phosphorylation and Ca2+ mobilization, but not degranulation, in lyn-deficient bone marrow-derived mast cells.
复制标题
在 lyn 缺陷的骨髓来源的肥大细胞中，酪氨酸磷酸化和 Ca2+ 动员受损，但脱粒不受影响。
作者：
H. Nishizumi;T. Yamamoto
通过肥大细胞和嗜碱性细胞上的高亲和力IgE受体（Fc epsilon RI）的信号传导导致许多蛋白质上酪氨酸磷酸化的快速增加。Fc epsilon RI与两类酪氨酸激酶结合，Src家族激酶，如Lyn、c-Yes和c-Src，以及Syk激酶。在这项工作中，我们使用野生型（lyn +/+）和lyn缺陷（lyn -/-）小鼠的原代肥大细胞，报告了lyn通过Fc epsilon RI参与信号传导。与lyn +/+肥大细胞不同，lyn -/-肥大细胞中的Fc epsilon RI交联不能诱导各种底物的蛋白酪氨酸磷酸化，并引起延迟和缓慢的Ca2+动员。然而，在lyn -/-肥大细胞中，脱颗粒、粘附和细胞因子的产生是正常的。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的作用，诱导大部分（但不是全部）对Fc epsilon RI交联的生物和生化反应。
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.