Brockenbrough J S, Korc M
Life Sci. 1987 Apr 20;40(16):1625-31. doi: 10.1016/0024-3205(87)90129-9.
1-oleoyl-2-acetyl glycerol (OAG), a potent activator of protein kinase C, inhibited the binding of 125I-labelled epidermal growth factor (EGF) in isolated rat pancreatic acini. Unlike cholecystokinin-octapeptide (CCK8) and the C-kinase activator 12-O-tetradecanoyl phorbol-13-acetate (TPA), two inhibitors of 125I-EGF endocytosis in the pancreas, OAG had no effect on the distribution of bound ligand between the cell surface and intracellular compartments. Unlike TPA, OAG failed to potentiate the inhibitory effects of the calcium ionophore A23187 on 125I-EGF cell-associated radioactivity and had no effect on either basal or carbachol-stimulated amylase release in acini. These data suggest that the actions of the synthetic diacyl-glycerol OAG are not fully equivalent with the action of other known activators of protein kinase C in the pancreatic acinar cell.
1-油酰基-2-乙酰甘油（OAG）是一种有效的蛋白激酶C激活剂，它能抑制分离的大鼠胰腺腺泡中125I标记的表皮生长因子（EGF）的结合。与胆囊收缩素八肽（CCK8）和C激酶激活剂12-O-十四酰佛波醇-13-乙酸酯（TPA）这两种胰腺中125I-EGF内吞作用的抑制剂不同，OAG对结合配体在细胞表面和细胞内区室之间的分布没有影响。与TPA不同，OAG不能增强钙离子载体A23187对125I-EGF细胞相关放射性的抑制作用，并且对腺泡中基础或卡巴胆碱刺激的淀粉酶释放均无影响。这些数据表明，合成二酰基甘油OAG的作用与胰腺腺泡细胞中其他已知的蛋白激酶C激活剂的作用并不完全相同。
