Saito T, Suzuki N, Hosoya T
Faculty of Pharmaceutical Sciences, Chiba University, Japan.
Biochem Int. 1988 May;16(5):895-901.
When rat liver nucleoli were incubated with [gamma-32P] ATP, it was found that 110k proteins were predominantly phosphorylated. The phosphorylation of 110k proteins was decreased by thyroidectomy to about 80% of the normal level and restored 12 h after the injection of triiodothyronine. The activity of nucleolar protein kinase NII which is responsible for phosphorylation of 110k proteins was also increased by about 20-50% after injecting triiodothyronine into thyroidectomized rats. The hormone-stimulated enhancement in the phosphorylation of 110k proteins and protein kinase NII in nucleoli were abolished within 1 h after an injection of cycloheximide, without any change in the amount of the proteins.
当用[γ-32P]ATP孵育大鼠肝脏核仁时，发现110k蛋白主要被磷酸化。甲状腺切除术后，110k蛋白的磷酸化水平降至正常水平的约80%，注射三碘甲状腺原氨酸12小时后恢复。向甲状腺切除的大鼠注射三碘甲状腺原氨酸后，负责110k蛋白磷酸化的核仁蛋白激酶NII的活性也增加了约20%-50%。注射环己酰亚胺1小时内，激素刺激引起的核仁中110k蛋白和蛋白激酶NII磷酸化增强被消除，而蛋白质的量没有任何变化。
