...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Cellular Physiology >Nuclear translocation of prolactin: collaboration of tyrosine kinase and protein kinase C activation in rat Nb2 node lymphoma cells.
【24h】

Nuclear translocation of prolactin: collaboration of tyrosine kinase and protein kinase C activation in rat Nb2 node lymphoma cells.

机译：催乳素核易位:协作酪氨酸激酶和蛋白激酶C淋巴瘤细胞激活大鼠Nb2节点。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Recent evidence has suggested that prolactin (PRL), internalized by lactogen-dependent Nb2 lymphoma cells, is actively translocated to the nucleus where it binds to PRL receptors. Moreover, the mitogenic action of PRL in these cells has been separately linked to protein tyrosyl phosphorylation and activation of protein kinase C (PKC). Therefore, the coupling of PRL internalization and nuclear translocation to the activation of these signal transduction pathways was investigated. Results from control experiments indicated that 30% of internalized and 5% total cell-associated 125I-rat PRL could be recovered within nuclei obtained from Nb2 cells previously incubated with the radiolabel for 3 h at 37 degrees C. Furthermore, internalized PRL was found to be intact and not associated with any carrier proteins. Addition of tyrosine kinase (TK) antagonists, genistein or tyrphostin, significantly reduced cell surface binding, internalization, and nuclear translocation of 125I-rat PRL. In contrast, neither the level of cell-associated nor internalized hormone differed between cells treated with the PKC antagonists, staurosporine or calphostin C, and control cultures. Instead, PKC inhibition significantly reduced nuclear PRL translocation. The inhibitory effects of the TK and PKC antagonists on PRL internalization and nuclear translocation in intact Nb2 cells were verified by immunofluorescence microscopy in parallel experiments. In other experiments, each of the kinase inhibitors blocked PRL-stimulated Nb2 cell proliferation in a concentration-dependent manner. It is concluded that activated TK and PKC collaborate in the process of PRL internalization and translocation to the nucleus. TK activation may participate in PRL receptor binding or hormone internalization while activation of PKC appears to be required for its nuclear targeting. Since TK and PKC activation are required for lactogen-stimulated Nb2 cell proliferation, we suggest that a component of the mitogenic pathway in these cells is a direct nuclear interaction of PRL.
机译：最近的证据表明,泌乳素(PRL),内化lactogen-dependent Nb2淋巴瘤细胞,是积极转移到核和PRL受体结合。此外,在这些PRL的促有丝分裂的作用细胞已经分别与蛋白质有关酪氨酰磷酸化和激活的蛋白质激酶C (PKC)。内化和核易位这些信号转导途径的激活被调查。实验表明,30%的内化和5% 125 i-rat PRL细胞相关在原子核从Nb2获得恢复细胞之前与radiolabel孵化3 h在37度c。此外,内化PRL完好无损,没有被发现与任何载体蛋白质有关。酪氨酸激酶(TK)拮抗剂,染料木黄酮或tyrphostin,显著降低细胞表面绑定、内化和核125 i-rat PRL的易位。无论是细胞相关的水平内化激素细胞之间的不同与PKC拮抗剂治疗,staurosporine或calphostin C和控制文化。PKC抑制核光杆载荷显著降低易位。和PRL内化和PKC拮抗剂完整Nb2细胞的核易位验证了免疫荧光显微镜平行实验。PRL-stimulated激酶抑制剂的阻塞Nb2细胞增殖浓度的方式。激活TK和PKC的协作PRL内化的过程和易位细胞核。PRL受体结合或激素内化而激活PKC似乎是必需的核目标。激活lactogen-stimulated所需Nb2细胞增殖,我们建议组成部分,这些细胞的促有丝分裂的途径是一个光杆载荷的直接核相互作用。

著录项

相似文献

  • 外文文献
  • 中文文献
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号