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Single-Molecule Manipulation by Magnetic Tweezers
Published in Shuo Huang, Single-Molecule Tools for Bioanalysis, 2022
In vivo, biomolecules bind to other molecules, cell membranes or subcellular organelles to perform their functions, in which their mechanical properties play important roles [1, 2]. In the process of gene expression, transcription factors bind to the regulation sites on a strand of DNA, which results in bending or twisting of the DNA template [3]. In more complicated circumstances, some crosslinker proteins could join two or more molecules together to form higher ordered structures, such as cytoskeletons, focal adhesions, or cell–cell junctions [4–6]. The cytoskeleton network supports the morphological shape of the cell and the tension within the network regulates cell migration, proliferation, and differentiation via force-dependent interactions between the cell’s components [7–9]. Though force is crucial in the regulation of cellular activities, it is challenging to directly study the mechanical properties of such biomolecules in the absence of a suitable technique to perform single molecule manipulations [10].
Fundamentals of biology and thermodynamics
Published in Mohammad E. Khosroshahi, Applications of Biophotonics and Nanobiomaterials in Biomedical Engineering, 2017
The cytoskeleton structure, located just under the membrane, is a network of fibers composed of proteins, called protein filaments. This structure is connected to other organelles. In animal cells, it is often organized from an area near the nucleus. These arrays of protein filament perform a variety of functions:Establish the cell shapeProvide mechanical strength to the cellPerform muscle contractionControl changes in cell shape and thus produce locomotionFacilitate intracellular transport of organelles
General Introductory Topics
Published in Vadim Backman, Adam Wax, Hao F. Zhang, A Laboratory Manual in Biophotonics, 2018
Vadim Backman, Adam Wax, Hao F. Zhang
From a biomedical optics perspective, cytoskeleton filaments are just too small to give rise to substantial elastic scattering. However, multiple absorbing and fluorescent contrast agents and stains are available that have affinities for different elements of the cytoskeleton. Thus, the cytoskeleton can be readily visualized by bright-field fluorescence and confocal microscopy. Furthermore, as the cytoskeleton plays a key role in maintaining and regulating cell size, shape, surface profile, and internal structure, cytoskeletal events can be detected by observing changes in light scattering or by means of microscopy modalities that use the phase of light interacting with live cells as a source of contrast.
A novel thermoresponsive membrane as potential material for tissue engineering
Published in Liquid Crystals, 2021
Na Li, Zexiang Zheng, Xiang Cai, Qiao Liu, Yifan Zhang, Changren Zhou, Lihua Li, Yaowu Zhao
The cytoskeleton organisation was characterised by laser confocal microscopy. MC3T3-E1 cells adhered to all membranes and showed healthy, spindle-like or polygonal shapes, as shown in Figure 9(b). However, blend membranes with TCLC were able to support more cells than the PU membranes, and these cells were mostly stretched with a polygon shape, suggesting that they spread easily on the TCLC/PU membranes. Some of the cells exhibited rudimentary filopodia after 1 day of cultivation, indicating a slight interaction with the blend TCLC/PU matrix. A significant increase in the cell spreading area and an elongated cell cytoskeleton as well as many cells joined together and/or overlapped with one another was observed after culturing for 2 days. This indicated that MC3T3-E1 cells were better integrated into the TCLC/PU than the PU membranes.
Proteomic analysis of whole-body responses in medaka (Oryzias latipes) exposed to benzalkonium chloride
Published in Journal of Environmental Science and Health, Part A, 2020
Young Sang Kwon, Jae-Woong Jung, Yeong Jin Kim, Chang-Beom Park, Jong Cheol Shon, Jong-Hwan Kim, June-Woo Park, Sang Gon Kim, Jong-Su Seo
The cytoskeleton is a skeletal network structure built by structural proteins, is involved in many important cellular functions,[26] and plays an important role in neuronal function and development of the nervous system.[27,28] An ecotoxicology study by Karim et al. (2011) reported that increased cytoskeletal proteins are a major indicator of oxidative stress, which can be induced by specific xenobiotics or toxins.[29] Previous studies used proteomic analyses to demonstrate that cytoskeletal proteins are regulated by hypoxic stress in zebrafish embryos and grass carp gills.[30] In our study, nine cytoskeletal proteins were upregulated by BAC exposure, including myosin light chain (spot 2), tropomyosin 1 (spot 7), and actin (spots 10, 13, 14, 15, 16, 17, and 18).
Involvement of MAPK/ERK1/2 pathway in microcystin-induced microfilament reorganization in HL7702 hepatocytes
Published in Journal of Toxicology and Environmental Health, Part A, 2018
Fei Yang, Cong Wen, Shuilin Zheng, Shu Yang, Jihua Chen, Xiangling Feng
Previously investigators demonstrated that MC produce their effects by inhibition of serine/threonine protein phosphatases1 (PP1) and 2A (PP2A) resulting in disruption of the dynamic equilibrium of protein phosphorylation as well as expression and activation of their downstream proteins, which leads to cytoskeletal reorganization (Ding, Shen, and Ong 2001; MacKintosh et al. 1990; Sun et al. 2001; Zeng et al. 2015). The cytoskeleton is a cellular network system containing different protein fibers intertwined with various regulatory proteins which play an important role in maintaining the morphology, intracellular transport, resist deformation, and change shape during movement of eukaryotic cells (Fletcher and Mullins 2010; Wickstead and Gull 2011). The cytoskeleton is predominantly composed of microfilaments (MF), microtubules (MT) and intermediate fibers (IF) (Sun et al. 2001; Zeng et al. 2015). Microfilaments, polymerized from actin molecules, exhibit various key functions involved in migration, secretion, and apoptosis (Papakonstanti and Stournaras 2008). Zeng et al. (2015) found that F-actin was depolymerized and that actin fibers aggregated around the cell periphery in the human liver HL7702 cells following exposure to 10 µM MC-LR. Further, Wang et al. (2014) reported that in the SMMC-7721 human liver cancer cell line, 10 µM MC-LR treatment induced actin to become concentrated and form bundles. Data thus suggest that MC-LR affects the cytoskeleton via interaction with actin fibers.