αII-血影蛋白调节核机械弹性而非硬度。
Nuclear mechanical resilience but not stiffness is modulated by αII-spectrin.
作者信息
Armiger Travis J, Spagnol Stephen T, Dahl Kris Noel
机构信息
Department of Chemical Engineering, Carnegie Mellon University, Pittsburgh, PA, USA.
Department of Chemical Engineering, Carnegie Mellon University, Pittsburgh, PA, USA; Department of Biomedical Engineering, Carnegie Mellon University, Pittsburgh, PA, USA.
出版信息
J Biomech. 2016 Dec 8;49(16):3983-3989. doi: 10.1016/j.jbiomech.2016.10.034. Epub 2016 Oct 27.
Spectrins are multi-domain, elastic proteins that provide elasticity to the plasma membrane of erythrocytes and select nucleated cells. Spectrins have also been found in the nucleus of non-erythrocytes, but their function remains to be uncovered. It has been hypothesized that a spring-like spectrin network exists within the lamina nucleoskeleton, however, experiments testing a spectrin network׳s mechanical impact on the nucleus are lacking. Here, we knock-down levels of nuclear αII-spectrin with the goal of disrupting this nucleoskeletal spectrin network. We mechanically test live cells with intranuclear particle tracking and compression assays to probe changes in nuclear mechanics with decreases in αII-spectrin. We show no changes in chromatin mechanics or in the stiffness of nuclei under compression. However, we do observe a reduction in the ability of nuclei with decreased αII-spectrin to recover after compression. These results establish spectrin as a nucleoskeletal component that specifically contributes to elastic recovery after compression.
血影蛋白是多结构域弹性蛋白，为红细胞质膜和某些有核细胞提供弹性。血影蛋白也存在于非红细胞的细胞核中，但其功能仍有待揭示。据推测，核纤层核骨架中存在类似弹簧的血影蛋白网络，然而，缺乏测试血影蛋白网络对细胞核机械影响的实验。在此，我们通过敲低核αII-血影蛋白水平来破坏这种核骨架血影蛋白网络。我们使用核内粒子追踪和压缩试验对活细胞进行力学测试，以探究随着αII-血影蛋白减少细胞核力学的变化。我们发现染色质力学或压缩状态下细胞核的硬度没有变化。然而，我们确实观察到αII-血影蛋白减少的细胞核在压缩后恢复能力降低。这些结果表明血影蛋白是一种核骨架成分，特别有助于压缩后的弹性恢复。
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