Biomechanical Properties of the Sarcolemma and Costameres of Skeletal Muscle Lacking Desmin.
Biomechanical Properties of the Sarcolemma and Costameres of Skeletal Muscle Lacking Desmin.
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DOI：
10.3389/fphys.2021.706806
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发表时间：
2021
影响因子：
4
通讯作者：
Bloch RJ
中科院分区：
文献类型：
--
作者：
Garcia-Pelagio KP;Bloch RJ
中间丝(IF)主要由结蛋白和角蛋白组成，将肌原纤维相互连接，连接到细胞内细胞器和肌膜。在那里，它们可能在将紧邻的肌原纤维的Z盘和M线的收缩力量传递到膜上的尾部，跨膜传递到细胞外基质，最终传递到肌腱上发挥重要作用(“侧向力传递”)。我们测量了结蛋白缺失小鼠的肌膜弹性以及它与单个快速抽动肌纤维的基本收缩机构之间的联系。通过将吸管放置在肌膜表面并施加增加的压力，我们确定了肌膜与附近肌节分离的压力P分离，以及分离的肌膜破裂的压力P。我们还检查了完整的肌膜-胞浆-肌节复合体在较低压力下达到平衡所需的时间。所有测量结果显示，结蛋白缺失的纤维的平衡时间比对照组慢，P分离和P爆裂也比对照组低，这表明在没有结蛋白的情况下，肌膜及其与附近收缩结构的胞间连接较弱。与早期测定的肌营养不良蛋白或同步素缺失值的比较表明，结蛋白缺失的表型比前者更稳定，比后者更不稳定。我们的结果与在结蛋白缺失肌肉中看到的中度肌病是一致的，并支持结蛋白对肌膜稳定性和侧向力传递有显著贡献的观点。
Intermediate filaments (IFs), composed primarily by desmin and keratins, link the myofibrils to each other, to intracellular organelles, and to the sarcolemma. There they may play an important role in transfer of contractile force from the Z-disks and M-lines of neighboring myofibrils to costameres at the membrane, across the membrane to the extracellular matrix, and ultimately to the tendon (“lateral force transmission”). We measured the elasticity of the sarcolemma and the connections it makes at costameres with the underlying contractile apparatus of individual fast twitch muscle fibers of desmin-null mice. By positioning a suction pipet to the surface of the sarcolemma and applying increasing pressure, we determined the pressure at which the sarcolemma separated from nearby sarcomeres, Pseparation, and the pressure at which the isolated sarcolemma burst, Pbursting. We also examined the time required for the intact sarcolemma-costamere-sarcomere complex to reach equilibrium at lower pressures. All measurements showed the desmin-null fibers to have slower equilibrium times and lower Pseparation and Pbursting than controls, suggesting that the sarcolemma and its costameric links to nearby contractile structures were weaker in the absence of desmin. Comparisons to earlier values determined for muscles lacking dystrophin or synemin suggest that the desmin-null phenotype is more stable than the former and less stable than the latter. Our results are consistent with the moderate myopathy seen in desmin-null muscles and support the idea that desmin contributes significantly to sarcolemmal stability and lateral force transmission.
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DOI：
10.1083/jcb.134.4.971
发表时间：
1996-08
期刊：
The Journal of cell biology
影响因子：
--
作者：
Goldman RD;Khuon S;Chou YH;Opal P;Steinert PM
通讯作者：
Steinert PM
影响因子：
3.3
作者：
Dowling P;Gargan S;Murphy S;Zweyer M;Sabir H;Swandulla D;Ohlendieck K
通讯作者：
Ohlendieck K
影响因子：
7.2
作者：
Herrmann, Harald;Aebi, Ueli
通讯作者：
Aebi, Ueli
影响因子：
6
作者：
Delacroix, Clement;Hyzewicz, Janek;Ferry, Arnaud
通讯作者：
Ferry, Arnaud
影响因子：
4.8
作者：
Bellin, RM;Sernett, SW;Robson, RM
通讯作者：
Robson, RM