Tskhovrebova L, Trinick J
School of Biomedical Sciences, University of Leeds, UK.
Adv Exp Med Biol. 2000;481:163-73; discussion 174-8. doi: 10.1007/978-1-4615-4267-4_10.
Studies of the origins of muscle passive tension have revealed a direct relationship between elasticity and the mechanical properties of the titin molecule. 'Molecular combing' has made it possible to visualize with high resolution changes in the configuration and structure of isolated titin caused by mechanical forces. The differential extensibility seen in individual molecules is consistent with the important role suggested for the PEVK-region in muscle elasticity. An additional factor emphasizing compliance of this part of the molecule in muscle may relate to the arrangement of the titin filament system in the sarcomere, in particular to titin interactions with thick and thin filaments. The branching of titin network near the PEVK-region suggests that, in addition to conferring extensibility, it may also be important in facilitating the transition of titin intermolecular interactions between the arrays of thick and thin filaments.
对肌肉被动张力起源的研究揭示了肌联蛋白分子的弹性与力学特性之间的直接关系。“分子梳”技术使得高分辨率可视化由机械力引起的分离肌联蛋白的构型和结构变化成为可能。在单个分子中观察到的差异延展性与PEVK区域在肌肉弹性中所起的重要作用相一致。强调该分子这一部分在肌肉中顺应性的另一个因素可能与肌节中肌联蛋白丝系统的排列有关，特别是与肌联蛋白与粗、细肌丝的相互作用有关。PEVK区域附近肌联蛋白网络的分支表明，除了赋予延展性外，它在促进肌联蛋白分子间相互作用在粗、细肌丝阵列之间的转变中可能也很重要。
