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甲状腺激素对大鼠肝脏核仁110k蛋白磷酸化及蛋白激酶NII活性的影响。

Effect of thyroid hormone on the phosphorylation of 110k proteins and the activity of protein kinase NII of rat liver nucleoli.

作者信息

Saito T, Suzuki N, Hosoya T

机构信息

Faculty of Pharmaceutical Sciences, Chiba University, Japan.

出版信息

Biochem Int. 1988 May;16(5):895-901.

PMID:3421987
Abstract

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.

摘要

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。

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