Sato M, Nakamura T, Koyama J
Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
FEBS Lett. 1987 Nov 16;224(1):29-32. doi: 10.1016/0014-5793(87)80416-7.
The nature of signals transmitted by two Fc gamma receptors (Fc gamma 2R for IgG2 and Fc gamma 1/gamma 2R for both IgG2 and IgG1) on guinea pig polymorphonuclear leukocytes was investigated. The specific binding of hen ovalbumin (OA)-complexed IgG1 antibody to Fc gamma 1/gamma 2R did not seem to trigger the release of [3H]arachidonic acid from the cells prelabeled with [3H]arachidonic acid. In contrast, marked release occurred on the binding of OA-complexed IgG2 antibody to the cells. This reaction was not inhibited, but rather enhanced, by the Fab' of a monoclonal antibody to Fc gamma 1/gamma 2R. Therefore, a signal for the activation of the arachidonic acid metabolic cascade was found to be transmitted by Fc gamma 2R, but scarcely by Fc gamma 1/gamma 2R.
对豚鼠多形核白细胞上两种Fcγ受体(IgG2的Fcγ2R以及IgG2和IgG1的Fcγ1/γ2R)所传递信号的性质进行了研究。鸡卵清蛋白(OA)复合IgG1抗体与Fcγ1/γ2R的特异性结合似乎并未触发预先用[3H]花生四烯酸标记的细胞释放[3H]花生四烯酸。相反,OA复合IgG2抗体与细胞结合时出现了明显的释放。针对Fcγ1/γ2R的单克隆抗体的Fab'并未抑制这一反应,反而增强了该反应。因此,发现花生四烯酸代谢级联反应激活信号是由Fcγ2R传递的,而Fcγ1/γ2R几乎不传递该信号。