• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Cell motility and the cytoskeleton >Actin-based centripetal flow: Phosphatase inhibition by calyculin-A alters flow pattern, actin organization, and actomyosin distribution.
【24h】

Actin-based centripetal flow: Phosphatase inhibition by calyculin-A alters flow pattern, actin organization, and actomyosin distribution.

机译：基于肌动蛋白的向心流：钙调蛋白A抑制磷酸酶可改变流型，肌动蛋白组织和肌动球蛋白分布。

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

Previous studies have suggested that the actin-based centripetal flow process in sea urchin coelomocytes is the result of a two-part mechanism, actin polymerization at the cell edge coupled with actomyosin contraction at the cell center. In the present study, we have extended the testing of this two-part model by attempting to stimulate actomyosin contraction via treatment of coelomocytes with the phosphatase inhibitor Calyculin A (CalyA). The effects of this drug were studied using digitally-enhanced video microscopy of living cells combined with immunofluorescent localization and scanning electron microscopy. Under the influence of CalyA, the coelomocyte actin cytoskeleton undergoes a radical reorganization from a dense network to one displaying an array of tangential arcs and radial rivulets in which actin and the Arp2/3 complex concentrate. In addition, the structure and dynamics of the cell center are transformed due to the accumulation of actin and membrane in this region and the constriction of the central actomyosin ring. Physiological evidence of an increase in actomyosin-based contractility following CalyA treatment was demonstrated in experiments in which cells generated tears in their cell centers in response to the drug. Western blotting and immunofluorescent localization with antibodies against the phosphorylated form of the myosin regulatory light chain (MRLC) suggested that the demonstrated constriction of actomyosin distribution was the result of CalyA-induced phosphorylation of MRLC. Overall, the results suggest that there is significant cross talk between the two underlying mechanisms of actin polymerization and actomyosin contraction, and indicate that changes in actomyosin tension may be translated into alterations in the structural organization of the actin cytoskeleton. Cell Motil. Cytoskeleton 56:252-266, 2003.
机译：先前的研究表明，海胆腔内皮细胞中基于肌动蛋白的向心流动过程是两部分机制的结果，即细胞边缘的肌动蛋白聚合与细胞中心的肌动球蛋白收缩。在本研究中，我们通过尝试通过用磷酸酶抑制剂Calyculin A（CalyA）处理结肠细胞刺激肌动球蛋白收缩，扩展了该两部分模型的测试。使用活细胞的数字增强视频显微镜与免疫荧光定位和扫描电子显微镜相结合，研究了该药物的作用。在CalyA的影响下，结肠细胞肌动蛋白细胞骨架从一个密集的网络经历了一次自由基重组，呈现出一系列切向弧和放射状小核，其中肌动蛋白和Arp2 / 3复合物集中。此外，由于肌动蛋白和膜在该区域的积累以及中央肌动球蛋白环的收缩，因此改变了细胞中心的结构和动力学。 CalyA处理后基于肌动球蛋白的收缩力增加的生理证据已在实验中证实，其中细胞响应药物而在其细胞中心产生了眼泪。蛋白质印迹和针对肌球蛋白调节性轻链（MRLC）磷酸化形式的抗体的免疫荧光定位表明，证明的肌动球蛋白分布收缩是CalyA诱导的MRLC磷酸化的结果。总体而言，结果表明肌动蛋白聚合和肌动球蛋白收缩的两个基本机制之间存在显着的相互干扰，并表明肌动球蛋白张力的变化可能转化为肌动蛋白细胞骨架的结构改变。细胞动力。细胞骨架56：252-266，2003。

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