Roghani M, Da Silva C, Guvelli D, Castagna M
Carcinogenesis. 1987 Aug;8(8):1105-7. doi: 10.1093/carcin/8.8.1105.
Protein kinase C plays a pivotal role in the transduction of signals controlling cell activation. A number of tumor promoters including phorbol esters activate the enzyme by substituting for diacylglycerol, the intracellular messenger of physiological ligands. In contrast, chloroform-induced protein kinase C activation does not appear to be mediated through the same mechanism. In vitro studies and experiments on intact platelets have revealed that benzene and toluene are also activators of protein kinase C. The data suggest that these drugs, which do not inhibit [3H]12-O-tetradecanoylphorbol-13-acetate binding to the enzyme, probably act in a chloroform-like manner.
蛋白激酶C在控制细胞活化的信号转导中起关键作用。包括佛波酯在内的多种肿瘤启动子通过替代二酰基甘油（生理配体的细胞内信使）来激活该酶。相比之下，氯仿诱导的蛋白激酶C活化似乎不是通过相同机制介导的。体外研究和对完整血小板的实验表明，苯和甲苯也是蛋白激酶C的激活剂。数据表明，这些不抑制[3H]12-O-十四酰佛波醇-13-乙酸酯与该酶结合的药物，可能以类似氯仿的方式起作用。
