...
  • 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 >Skeletal muscle myosin cross-bridge cycling is necessary for myofibrillogenesis.
【24h】

Skeletal muscle myosin cross-bridge cycling is necessary for myofibrillogenesis.

机译：骨骼肌肌球蛋白跨桥循环对于肌原纤维形成是必需的。

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 major stimulus affecting myofibrillogenesis in both embryonic and mature striated muscle is contractile activity. There are two major signals associated with contractile activity: a physiological signal, the transient increase in intracellular calcium, and a physical signal, the transient increase in tension production. However, dissociating these two signals to examine their relative contributions to myofibrillogenesis has proven difficult. In this study, we have used two different myosin inhibitors to determine the importance of myosin cross-bridge cycling in sarcomere assembly. We find that the small-molecule inhibitor 2,3-butanedione monoxime (BDM), which inhibits myosin ATPase, disrupts myofibrillogenesis in amphibian myocytes, consistent with results from avian studies. However, BDM is a weak myosin inhibitor and it is non-specific; concentrations that inhibit contraction and disrupt myofibrillogenesis also disrupt calcium signaling. Therefore, we also used the recently identified skeletal muscle myosin II inhibitor, N-benzyl-p-toluenesulphonamide (BTS), which has high affinity and specificity for skeletal muscle fast myosin. BTS inhibits contraction and results in myofibrillar disruption that phenocopies our results with BDM. However, BTS does not affect either spontaneous or induced calcium transients. Furthermore, BTS is reversible and does not significantly affect the expression levels of myosin or actin. Thus, our convergent results with BDM and BTS suggest that sarcomere assembly depends on active regulation of tension in the forming myofibril. Cell Motil. Cytoskeleton 55:61-72, 2003.
机译：影响胚胎和成熟横纹肌中肌原纤维形成的主要刺激因素是收缩活动。与收缩活动有关的主要信号有两个：生理信号（细胞内钙的瞬时增加）和物理信号（张力产生的瞬时增加）。然而，已经证明分离这两种信号以检查它们对肌纤维形成的相对作用是困难的。在这项研究中，我们使用了两种不同的肌球蛋白抑制剂来确定肌球蛋白跨桥循环在肌节装配中的重要性。我们发现小分子抑制剂2，3-丁二酮单肟（BDM），抑制肌球蛋白ATPase，破坏两栖动物心肌细胞的肌原纤维形成，与禽类研究的结果一致。然而，BDM是一种弱肌球蛋白抑制剂，并且是非特异性的。抑制收缩并破坏肌原纤维形成的浓度也会破坏钙信号传导。因此，我们还使用了最近鉴定出的骨骼肌肌球蛋白II抑制剂N-苄基-对甲苯磺酰胺（BTS），它对骨骼肌快肌球蛋白具有很高的亲和力和特异性。 BTS会抑制收缩，并导致肌原纤维破坏，这明显地证明了BDM的结果。但是，BTS既不影响自发性钙瞬变也不会影响钙瞬变。此外，BTS是可逆的，不会明显影响肌球蛋白或肌动蛋白的表达水平。因此，我们与BDM和BTS的收敛结果表明，肌节组装取决于形成肌原纤维中张力的主动调节。细胞动力。 Cytoskeleton 55：61-72，2003。

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