Park M H, Chae Q
Department of Biochemistry, Chungbuk National University, Republic of Korea.
Biochem Biophys Res Commun. 1990 Jun 29;169(3):1185-90. doi: 10.1016/0006-291x(90)92021-q.
Phosphorylations of two proteins (27 KDa, 32 KDa) in oat cells were dependent on phytochrome action. To determine which kinase system(s) for the phosphorylation of these two proteins are controlled by the phytochrome, involvement of the Ca2+/DG dependent protein kinase (protein kinase C) was first investigated. When a protein kinase C inhibitor (1-(5-isoquinoline sulfonyl)-2-methylpiperazine:H-7) or the inositol phospholipid metabolic blocker Li+ was added into the cell suspension, respectively, the phosphorylations of these two proteins were substantially reduced. On the other hand, an addition of 1-oleoyl-2-acetyl-sn-glycerol (OAG:activator of protein kinase C) or phorbol 12-myristate 13-acetate (TPA: tumor promoting phorbol ester) enhanced the phosphorylations of these proteins. These results suggest that phytochrome action is certainly connected with the protein phosphorylation via the activation of protein kinase C or a similar molecule with protein kinase C.
燕麦细胞中两种蛋白质（27千道尔顿、32千道尔顿）的磷酸化依赖于光敏色素的作用。为了确定这两种蛋白质磷酸化的哪种激酶系统受光敏色素控制，首先研究了Ca2+/DG依赖性蛋白激酶（蛋白激酶C）的参与情况。当分别向细胞悬液中加入蛋白激酶C抑制剂（1-(5-异喹啉磺酰基)-2-甲基哌嗪：H-7）或肌醇磷脂代谢阻滞剂Li+时，这两种蛋白质的磷酸化显著降低。另一方面，加入1-油酰基-2-乙酰基-sn-甘油（OAG：蛋白激酶C激活剂）或佛波醇12-肉豆蔻酸酯13-乙酸酯（TPA：促肿瘤佛波酯）可增强这些蛋白质的磷酸化。这些结果表明，光敏色素的作用肯定通过蛋白激酶C或与蛋白激酶C类似的分子的激活与蛋白质磷酸化相关。
