Quantitative observations on cytoskeleton changes of osteocytes at different cell parts using digital holographic microscopy

Quantitative observations on cytoskeleton changes of osteocytes at different cell parts using digital holographic microscopy
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数字全息显微镜定量观察骨细胞不同细胞部位的细胞骨架变化

DOI:
10.1364/boe.9.000072
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发表时间:
2018-01-01
影响因子:
3.4
通讯作者:
Pan, Feng
Pan, Feng
中科院分区:
医学2区
文献类型:
--
作者:
Cao, Runyu;Xiao, Wen;Pan, Feng

文献摘要

被引文献

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细胞骨架如F-肌动蛋白在细胞的不同部位有不同的分布,当F-肌动蛋白被破坏时,它们是导致细胞不同程度塌陷的原因。传统的荧光显微镜和原子力显微镜等方法由于测量速度慢、需要活细胞染色等原因,难以对细胞不同部位的动态过程进行实时三维观察。在这项研究中,不同的形态变化,骨细胞部分所造成的F-肌动蛋白中断动态测量使用数字全息显微镜(DHM)。我们分别分析细胞的局部参数(细胞高度和细胞宽度)和全局参数(细胞投影面积和细胞体积),以解决特定细胞面积的变化,并量化整个细胞的变化过程。我们发现细胞体和细胞突起的局部和整体细胞参数的时间变化存在显著差异,这与荧光染色的定性遮蔽一致。我们的研究不仅验证了DHM同时研究细胞不同部位的动态过程的独特能力,而且为探索F-actin断裂机制提供了充分的实验基础。(c)2017美国光学学会
Cytoskeletons such as F-actin have different distributions in different cell parts and they are the cause of different degrees of cell collapse when the F-actin is disrupted. It is challenging to use conventional methods such as fluorescence microscopy and atomic force microscopy to conduct real-time and three-dimensional observations on the dynamic processes at different cell parts due to the slow measuring speed and the need for live-cell staining. In this study, the morphological variations of different, bone cell parts caused by F-actin disruption are dynamically measured by using digital holographic microscopy (DHM). We separately analyze local parameters (cell height, and cell width) and global parameters (cell projected area, and cell volume) of cells to address variations of specific cell areas and quantify the changing process of the whole cell. We found significant differences in temporal variations of both local and global cell parameters between the cell body and cell process, which is consistent with the qualitative obscn-ation by fluorescence staining. Our study not only validates the unique ability of DHM to simultaneously investigate the dynamic process at different, cell parts, but also provides sufficient experimental bases for exploring the mechanism for F-actin disruption. (c) 2017 Optical Society of America