Kiss Z, Garamszegi N
Hormel Institute, University of Minnesota, Austin 55912.
Lipids. 1993 Jun;28(6):479-81. doi: 10.1007/BF02536077.
Treatment of [14C]choline- or [14C]ethanolamine-labeled NIH 3T3 fibroblasts with Bacillus cereus phosphatidyl-choline-specific phospholipase C (PLC) enhanced phospholipase D (PLD)-mediated hydrolysis of the respective 14C-labeled phospholipids. PLD activity was stimulated by 1.5 U/mL of PLC and by 100 nM of the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) to similar extents. Treatment of [14C]palmitic acid-labeled fibroblasts with PLC in the presence of ethanol also enhanced PLD-mediated formation of phosphatidylethanol; the effects of PLC and PMA were nonadditive. PLC had no effect on PLD activity in fibroblasts in which PKC was down-regulated by prolonged (24 h) treatment with 300 nM PMA. These data indicate that treatment of fibroblasts with exogenous PLC results in PKC-dependent activation of PLD.
用蜡样芽孢杆菌磷脂酰胆碱特异性磷脂酶C（PLC）处理[14C]胆碱或[14C]乙醇胺标记的NIH 3T3成纤维细胞，可增强磷脂酶D（PLD）介导的相应14C标记磷脂的水解。1.5 U/mL的PLC和100 nM的蛋白激酶C（PKC）激活剂佛波醇12-肉豆蔻酸酯13-乙酸酯（PMA）对PLD活性的刺激程度相似。在乙醇存在下，用PLC处理[14C]棕榈酸标记的成纤维细胞也增强了PLD介导的磷脂酰乙醇形成；PLC和PMA的作用无相加性。在用300 nM PMA长时间（24小时）处理使PKC下调的成纤维细胞中，PLC对PLD活性无影响。这些数据表明，用外源性PLC处理成纤维细胞会导致PKC依赖的PLD激活。
