• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>American Journal of Physiology >Acetylcholine-induced phosphorylation and membrane translocation of CPI-17 in bronchial smooth muscle of rats.
【24h】

Acetylcholine-induced phosphorylation and membrane translocation of CPI-17 in bronchial smooth muscle of rats.

机译：乙酰胆碱诱导的大鼠支气管平滑肌中CPI-17的磷酸化和膜移位。

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

A translocation of protein kinase C (PKC) from cytosol to plasma membrane has been reported as an association with agonist-induced Ca2+ sensitization in smooth muscle contraction. Therefore, it is possible that a downstream target of PKC, CPI-17 [PKC-potentiated inhibitory protein for heterotrimeric myosin light chain (MLC) phosphatase of 17 kDa], might also be translocated to membrane when activated. To confirm this hypothesis, cytosolic and membrane CPI-17 was measured in acetylcholine (ACh)- and high-K+ depolarization-stimulated bronchial smooth muscle of rats. An active form of CPI-17, i.e., Thr38-phosphorylated CPI-17, was also measured in cytosolic and membrane fractions. Immunoblot analyses demonstrated a translocation of CPI-17 from cytosolic to membrane fraction by ACh, but not high-K+ depolarization, stimulation in time- and concentration-dependent manners. Interestingly, phosphorylated CPI-17 was detected only in membrane fractions in the ACh-stimulated tissues. However, in the high-K+ depolarization-stimulated tissues, phosphorylated CPI-17 was not detected both in membrane and cytosolic fraction. To estimate downstream of activated CPI-17, immunoblotting for phosphorylated MLC was performed in ACh- or high-K+ depolarization-stimulated tissues. ACh- and high-K+ depolarization-induced phosphorylation of MLC was observed in its contraction-dependent manner. In conclusion, we, for the first time, suggested that CPI-17 is translocated and phosphorylated by ACh, but not high-K+ depolarization, in rat bronchial smooth muscle. ACh-induced translocation and phosphorylation of CPI-17 might be caused via the activation of muscarinic receptor.
机译：据报道，蛋白激酶C（PKC）从胞浆转移到质膜与平滑肌收缩中激动剂诱导的Ca2 +致敏有关。因此，PKC的下游靶点CPI-17 [PKC增强的17 kDa异源三聚肌球蛋白轻链（MLC）磷酸酶抑制蛋白]也有可能在激活时转移到膜上。为了证实这一假设，在大鼠的乙酰胆碱（ACh）-和高K +去极化刺激的支气管平滑肌中测量了细胞质和膜CPI-17。 CPI-17的一种活性形式，即Thr38磷酸化的CPI-17，也在细胞质和膜级分中进行了测定。免疫印迹分析表明，ACh使CPI-17从胞质转移到膜部分，但没有高K +去极化，而是以时间和浓度依赖性方式刺激。有趣的是，仅在ACh刺激的组织的膜部分中检测到磷酸化的CPI-17。但是，在高K +去极化刺激的组织中，在膜和胞质中均未检测到磷酸化的CPI-17。为了估计激活的CPI-17的下游，在ACh-或高K +去极化刺激的组织中进行了磷酸化MLC的免疫印迹。观察到ACh-和高K +去极化诱导的MLC磷酸化具有收缩依赖性。总而言之，我们首次建议在大鼠支气管平滑肌中CPI-17被ACh转运并磷酸化，而不是高K +去极化。 ACh诱导的CPI-17易位和磷酸化可能是由毒蕈碱受体的激活引起的。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
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