Kvanta A, Nordstedt C, Jondal M, Fredholm B B
Department of Pharmacology, Karolinska Institutet, Stockholm, Sweden.
Naunyn Schmiedebergs Arch Pharmacol. 1989 Dec;340(6 Pt 2):715-7. doi: 10.1007/BF00169679.
We have recently shown that activation of protein kinase C by tumour promoting phorbolesters, such as 4 beta-phorbol-12,13-dibutyrate, stimulates adenosine-induced accumulation of cAMP in Jurkat cells, a human T-leukaemia line. Activating the CD3 complex associated with the T-cell receptor by means of the monoclonal antibody OKT3 caused a concentration-dependent accumulation of inositol phosphates and an increase in the phosphorylation of an endogenous protein kinase C substrate. OKT3 also mimicked the previously reported effects of protein kinase C since it potentiated the cAMP stimulation by either an adenosine analogue, NECA, or cholera toxin. Thus, our results indicate that stimulation of a receptor activating phospholipase C and protein kinase C can secondarily enhance the action of agonists that act on adenylate cyclase-coupled receptors.
我们最近发现，肿瘤促进剂佛波酯（如4β-佛波醇-12,13-二丁酸酯）激活蛋白激酶C，可刺激腺苷诱导人T淋巴细胞白血病细胞系Jurkat细胞中cAMP的积累。通过单克隆抗体OKT3激活与T细胞受体相关的CD3复合物，会导致肌醇磷酸浓度依赖性积累，并使内源性蛋白激酶C底物的磷酸化增加。OKT3还模拟了先前报道的蛋白激酶C的作用，因为它增强了腺苷类似物NECA或霍乱毒素对cAMP的刺激作用。因此，我们的结果表明，刺激激活磷脂酶C和蛋白激酶C的受体，可继而增强作用于腺苷酸环化酶偶联受体的激动剂的作用。
