Kato M, Kita H, Tokuyama K, Morikawa A
Department of Pediatrics, Gunma University School of Medicine, Maebashi, Gunma, Japan.
Int Arch Allergy Immunol. 1998 Sep;117 Suppl 1:68-71. doi: 10.1159/000053576.
Adhesion molecules, including integrins, play an important role in the selective recruitment of eosinophils. It has recently been shown that integrins also modulate the functions of eosinophils. Here, we tested the hypothesis that cross-linking of the beta2 integrin, alphaMbeta2Mac-/, leads to intracellular signaling events such as activation of protein tyrosine kinases leading to eosinophil degranulation. Cross-of cell surface CD11b/with anti-tibody and goat anti-G immobilized onto the plate triggered tyrosine phosphorylation of several intracellular proteins, including the one with a 115-kD mass (pp115). The same stimulus also provoked degranulation of eosinophils. These findings suggest that engagement of beta2 integrin on eosinophils triggers the activation of intracellular signaling cascade which leads to cellular degranulation.
包括整合素在内的黏附分子在嗜酸性粒细胞的选择性募集中起重要作用。最近有研究表明，整合素还可调节嗜酸性粒细胞的功能。在此，我们验证了以下假说：β2整合素αMβ2（Mac-1）的交联会引发细胞内信号转导事件，如蛋白酪氨酸激酶的激活，进而导致嗜酸性粒细胞脱颗粒。将抗CD11b/抗体与固定在平板上的山羊抗IgG进行交联，可触发几种细胞内蛋白的酪氨酸磷酸化，包括一种分子量为115kD的蛋白（pp115）。相同的刺激也会引发嗜酸性粒细胞的脱颗粒。这些发现表明，嗜酸性粒细胞上β2整合素的结合会触发细胞内信号级联反应的激活，从而导致细胞脱颗粒。
