Cellular progesterone receptor phosphorylation in response to ligands activating protein kinases.
Cellular progesterone receptor phosphorylation in response to ligands activating protein kinases.
复制标题
细胞黄体酮受体磷酸化响应配体激活蛋白激酶。
DOI：
10.1016/0006-291x(87)90799-6
复制
发表时间：
1987
影响因子：
3.1
通讯作者：
Fox,CF
中科院分区：
文献类型：
--
作者：
Rao,KV;Peralta,WD;Greene,GL;Fox,CF
用来自人乳腺癌T47D细胞裂解物的单克隆抗体KD68对孕酮受体进行免疫沉淀，该细胞用32 Pi标记为稳态比活性。通过聚丙烯酰胺凝胶电泳解析 120 kDa32P 标记的孕酮受体条带，并通过放射自显影进行鉴定。磷酸氨基酸分析显示丝氨酸磷酸化，但没有苏氨酸或酪氨酸磷酸化。用EGF、TPA或二丁酰cAMP处理32Pi标记的细胞对孕酮受体磷酸化没有显着的定量影响，尽管已报道EGF受体和cAMP依赖性蛋白激酶在无细胞系统中催化纯化的禽类孕酮受体制剂的磷酸化。在用 10 nM 孕酮处理的细胞中，孕酮受体丝氨酸残基磷酸化增加了 2 倍； EGF 对孕酮介导的孕酮受体磷酸化没有影响。
Progesterone receptors were immunoprecipitated with monoclonal antibodies KD68 from lysates of human breast carcinoma T47D cells labelled to steady state specific activity with32Pi. The 120 kDa32P-labelled progesterone receptor band was resolved by polyacrylamide gel electrophoresis and identified by autoradiography. Phosphoamino acid analysis revealed serine phosphorylation, but no threonine or tyrosine phosphorylation. Treatment of the32Pi-labelled cells with EGF, TPA or dibutyryl cAMP had no significant quantitative effect on progesterone receptor phosphorylation, though the EGF receptor and the cAMP-dependent protein kinases have been reported to catalyze phosphorylation of purified avian progesterone receptor preparations in cell free systems. Progesterone receptor phosphorylation on serine residues was increased by 2-fold in cells treated with 10 nM progesterone; EGF had no effect on progesterone-mediated progesterone receptor phosphorylation.