Taguchi M, Thomas T P, Anderson W B, Farrar W L
Biochem Biophys Res Commun. 1986 Feb 26;135(1):239-47. doi: 10.1016/0006-291x(86)90968-x.
Phorbol esters induce a rapid phosphorylation of the antigenic epitope of the human IL-2 receptor identified by anti-Tac monoclonal antibody. The physiological activator of protein kinase C, diacylglycerol also stimulated the phosphorylation of the Tac epitope in intact activated human T lymphocytes. Stable derivatives of cyclic nucleotides had no effect on the stimulation of Tac phosphorylation with cultured lymphocytes. Immunoprecipitated Tac derived from particulate membranes could serve as a direct substrate for purified protein kinase C in vitro. The Ca2+/phospholipid dependency of the in vitro phosphorylation reaction substantiated that the phosphorylation of Tac observed in intact cells stimulated by phorbol ester or diacylglycerol was the result of the physiological activation of protein kinase C.
佛波酯可诱导由抗 Tac 单克隆抗体识别的人白细胞介素 -2 受体抗原表位的快速磷酸化。蛋白激酶 C 的生理激活剂二酰基甘油也能刺激完整的活化人 T 淋巴细胞中 Tac 表位的磷酸化。环核苷酸的稳定衍生物对培养淋巴细胞中 Tac 磷酸化的刺激没有影响。从微粒体膜中免疫沉淀得到的 Tac 在体外可作为纯化蛋白激酶 C 的直接底物。体外磷酸化反应对 Ca2 + /磷脂的依赖性证实，在佛波酯或二酰基甘油刺激的完整细胞中观察到的 Tac 磷酸化是蛋白激酶 C 生理激活的结果。
