Department of Physiology and Aging, University of Florida, Gainesville, Florida, United States of America.
Department of Pharmacology and Therapeutics, University of Florida, Gainesville, Florida, United States of America.
PLoS One. 2024 Apr 30;19(4):e0300348. doi: 10.1371/journal.pone.0300348. eCollection 2024.
The sarcomere is the fundamental contractile unit in skeletal muscle, and the regularity of its structure is critical for function. Emerging data demonstrates that nanoscale changes to the regularity of sarcomere structure can affect the overall function of the protein dense ~2μm sarcomere. Further, sarcomere structure is implicated in many clinical conditions of muscle weakness. However, our understanding of how sarcomere structure changes in disease, especially at the nanoscale, has been limited in part due to the inability to robustly detect and measure at sub-sarcomere resolution. We optimized several methodological steps and developed a robust pipeline to analyze sarcomere structure using structured illumination super-resolution microscopy in conjunction with commercially-available and fluorescently-conjugated Variable Heavy-Chain only fragment secondary antibodies (nanobodies), and achieved a significant increase in resolution of z-disc width (353nm vs. 62nm) compared to confocal microscopy. The combination of these methods provides a unique approach to probe sarcomere protein localization at the nanoscale and may prove advantageous for analysis of other cellular structures.
肌节是骨骼肌的基本收缩单位,其结构的规律性对于功能至关重要。新出现的数据表明,肌节结构规律性的纳米级变化会影响蛋白质密集的~2μm肌节的整体功能。此外,肌节结构与许多肌肉无力的临床状况有关。然而,我们对肌节结构在疾病中如何变化的理解,特别是在纳米级水平上,受到了一定的限制,部分原因是无法在亚肌节分辨率下进行稳健的检测和测量。我们优化了几个方法步骤,并开发了一个稳健的管道,使用结构照明超分辨率显微镜结合商业上可用的和荧光标记的可变重链仅片段二抗(纳米体)来分析肌节结构,与共聚焦显微镜相比,Z 盘宽度的分辨率显著提高(353nm 对 62nm)。这些方法的结合为在纳米尺度上探测肌节蛋白定位提供了一种独特的方法,并且可能对其他细胞结构的分析具有优势。