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重水会在缠结的肌动蛋白网络中诱导形成束状结构。

Heavy water induces bundling in entangled actin networks.

作者信息

Mollenkopf Paul, Prascevic Dusan, Bayerl Thomas M, Käs Josef A, Schnauß Jörg

机构信息

Department of Physiology, University of Pennsylvania Philadelphia PA 19104 USA.

Peter-Debye Institute for Soft Matter Physics, Leipzig University 04103 Leipzig Germany

出版信息

RSC Adv. 2023 Aug 18;13(35):24795-24800. doi: 10.1039/d3ra03917j. eCollection 2023 Aug 11.

DOI:10.1039/d3ra03917j
PMID:37601592
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10437092/
Abstract

Heavy water is known to affect many different biological systems, with the most striking effects observed at the cellular level. Many dynamic processes, such as migration or invasion, but also central processes of cell proliferation are measurably inhibited by the presence of deuterium oxide (DO). Furthermore, individual cell deformabilities are significantly decreased upon DO treatment. In order to understand the origin of these effects, we studied entangled filamentous actin networks, a commonly used model system for the cytoskeleton, which is considered a central functional element for dynamic cellular processes. Using bulk shear rheology to extract rheological signatures of reconstituted actin networks at varying concentrations of DO, we found a non-monotonic behavior, which is explainable by a drastic change in the actin network architecture. Applying light scattering and fluorescence microscopy, we were able to demonstrate that the presence of deuterium oxide induces bundling in reconstituted entangled networks of filamentous actin. This constitutes an entirely novel and previously undescribed actin bundling mechanism.

摘要

众所周知,重水会影响许多不同的生物系统,在细胞水平上观察到的影响最为显著。许多动态过程,如迁移或侵袭,以及细胞增殖的核心过程,都会因氧化氘(DO)的存在而受到显著抑制。此外,经DO处理后,单个细胞的变形能力会显著下降。为了理解这些影响的起源,我们研究了缠结的丝状肌动蛋白网络,这是一种常用的细胞骨架模型系统,被认为是动态细胞过程的核心功能元件。通过使用体积剪切流变学来提取不同DO浓度下重组肌动蛋白网络的流变特征,我们发现了一种非单调行为,这可以通过肌动蛋白网络结构的剧烈变化来解释。应用光散射和荧光显微镜,我们能够证明氧化氘的存在会在重组的缠结丝状肌动蛋白网络中诱导束状形成。这构成了一种全新的、以前未描述过的肌动蛋白束状形成机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8fb5/10437092/79ebedc5704a/d3ra03917j-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8fb5/10437092/509030947498/d3ra03917j-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8fb5/10437092/f9cbb658a0c7/d3ra03917j-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8fb5/10437092/79ebedc5704a/d3ra03917j-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8fb5/10437092/509030947498/d3ra03917j-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8fb5/10437092/f9cbb658a0c7/d3ra03917j-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8fb5/10437092/79ebedc5704a/d3ra03917j-f3.jpg

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Cells in Slow Motion: Apparent Undercooling Increases Glassy Behavior at Physiological Temperatures.细胞慢动作:生理温度下明显过冷增加玻璃化行为。
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Hydrophobic-Interaction-Induced Stiffening of α-Synuclein Fibril Networks.疏水相互作用诱导的α-突触核蛋白纤维网络的僵硬化。
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