Centre of Human & Aerospace Physiological Sciences, King's College London, Room 3.3, Shepherd's House, Guy's Campus, London, SE1 1UL, UK,
J Muscle Res Cell Motil. 2013 Aug;34(3-4):171-5. doi: 10.1007/s10974-013-9345-x. Epub 2013 May 18.
Human tropomyosin mutations deregulate skeletal muscle contraction at the cellular level. One key feature is the slowing of the kinetics of force development. The aim of the present study was to characterize the potential underlying molecular mechanisms by recording and analyzing the X-ray diffraction patterns of human membrane-permeabilized muscle cells expressing a particular β-tropomyosin mutation (E41K). During resting conditions, the d1,0 lattice spacing, Δ1,0 and I1,1 to I1,0 ratio were not different from control values. These results suggest that, in presence of the E41K β-tropomyosin mutation, the myofilament lattice geometry is well maintained and therefore may not have any detrimental influence on the contraction mechanisms and thus, on the rate of force generation.
人类原肌球蛋白突变会在细胞水平上使骨骼肌收缩失调。一个关键特征是力发展动力学的减缓。本研究的目的是通过记录和分析表达特定β-原肌球蛋白突变（E41K）的人细胞膜通透肌细胞的 X 射线衍射图谱来表征潜在的分子机制。在静止状态下，d1,0 晶格间距、Δ1,0 和 I1,1 至 I1,0 的比值与对照值无差异。这些结果表明，在存在 E41Kβ-原肌球蛋白突变的情况下，肌丝晶格几何形状得到很好的维持，因此不会对收缩机制，从而对力的产生速度产生任何不利影响。
