Iynedjian P B, Arslan Y
FEBS Lett. 1984 Dec 3;178(1):143-8. doi: 10.1016/0014-5793(84)81258-2.
Phosphorylation of a characteristic subset of nuclear proteins is increased in rat liver cells stimulated with glucagon. Regulated proteins include histones H1 and H3, an HMG 14-like protein and a previously unidentified 23-kDa basic protein. The effect of glucagon is mimicked by forskolin and exogenous cAMP. Insulin and dexamethasone have no effect. In a cell-free system containing purified hepatocyte nuclei, addition of cAMP-dependent protein kinase results in phosphorylation of histone H3, an HMG 14-like protein and a 23-kDa basic protein similar or identical to the protein phosphorylated in vivo.
用胰高血糖素刺激大鼠肝细胞后，核蛋白特征性子集的磷酸化作用增强。受调控的蛋白质包括组蛋白H1和H3、一种HMG 14样蛋白以及一种以前未鉴定的23 kDa碱性蛋白。福斯可林和外源性环磷酸腺苷（cAMP）可模拟胰高血糖素的作用。胰岛素和地塞米松则无作用。在含有纯化肝细胞核的无细胞体系中，添加cAMP依赖性蛋白激酶会导致组蛋白H3、一种HMG 14样蛋白以及一种与体内磷酸化蛋白相似或相同的23 kDa碱性蛋白发生磷酸化。
