Yamaguchi T, Baba H, Fukase M, Kinoshita Y, Fujimi T, Fujita T
Biochem Biophys Res Commun. 1987 Mar 13;143(2):539-44. doi: 10.1016/0006-291x(87)91387-8.
The effects of 12-O-tetraadecanoyl phorbol-13-acetate (TPA), 1-oleoyl-2-acetyl-glycerol (OAG), and 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H-7) on the parathyroid hormone (PTH) degrading activity in a PTH-responsive osteoblast-like rat osteosarcoma cell line UMR106 were investigated to assess the role of Ca2+-activated. Phospholipid dependent protein kinase (protein kinase C) on the degradation of hormones. TPA and OAG, activators of protein kinase C, enhanced the PTH degrading activity dose-dependently, whereas H-7, an inhibitor of protein kinase C, exhibited a dose-dependent inhibition on this activity. These data suggest that protein kinase C activation may enhance PTH degrading activity by UMR106 cells as a possible regulator of PTH degradation.
研究了12 - O - 十四烷酰佛波醇 - 13 - 乙酸酯（TPA）、1 - 油酰基 - 2 - 乙酰甘油（OAG）和1 -（5 - 异喹啉磺酰基）- 2 - 甲基哌嗪（H - 7）对甲状旁腺激素（PTH）反应性成骨细胞样大鼠骨肉瘤细胞系UMR106中PTH降解活性的影响，以评估Ca2 + 激活的磷脂依赖性蛋白激酶（蛋白激酶C）在激素降解中的作用。蛋白激酶C的激活剂TPA和OAG剂量依赖性地增强了PTH降解活性，而蛋白激酶C的抑制剂H - 7对该活性表现出剂量依赖性抑制。这些数据表明，蛋白激酶C激活可能通过UMR106细胞增强PTH降解活性，作为PTH降解的一种可能调节因子。
