Avissar S, Stenzel K H, Novogrodsky A
Cell Immunol. 1985 Dec;96(2):462-71. doi: 10.1016/0008-8749(85)90378-8.
Protein kinase C activity was demonstrated in murine thymocytes and the effects of TPA and IL-1 on this enzyme were studied. TPA, but not IL-1, could substitute for diacylglycerol in protein kinase C activation. Although TPA and IL-1 are both potent comitogens for murine thymocytes they markedly differ in their effects on protein phosphorylation and protein kinase C activation. Treatment of intact thymocytes with TPA resulted in a marked increase in the phosphorylation of an endogenous protein with Mr approximately 44,000. Enhanced phosphorylation of this protein was also observed when protein kinase C was activated in thymocyte extracts. In contrast to TPA, IL-1 neither induced phosphorylation of the 44,000-Da protein nor activated protein kinase C. The data suggests that protein kinase C does not mediate the comitogenic effect of IL-1 in murine thymocytes.
在小鼠胸腺细胞中证实了蛋白激酶C的活性,并研究了佛波酯(TPA)和白细胞介素-1(IL-1)对该酶的影响。TPA而非IL-1可在蛋白激酶C激活过程中替代二酰甘油。尽管TPA和IL-1都是小鼠胸腺细胞的强效辅有丝分裂原,但它们对蛋白质磷酸化和蛋白激酶C激活的影响明显不同。用TPA处理完整的胸腺细胞会导致一种分子量约为44,000的内源性蛋白质的磷酸化显著增加。当在胸腺细胞提取物中激活蛋白激酶C时,也观察到该蛋白质的磷酸化增强。与TPA相反,IL-1既不诱导44,000道尔顿蛋白质的磷酸化,也不激活蛋白激酶C。数据表明,蛋白激酶C不介导IL-1在小鼠胸腺细胞中的辅有丝分裂作用。