Proteomic response of human neuroblastoma cells to azaspiracid-1
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Wall shear stress and statin drugs have both been shown to influence endothelial cell function. We investigated the effect of statins on the morphology and F-actin cytoskeleton arrangement of endothelial cells with and without wall shear stress. Under static conditions, statins caused cells to become rounded and disorganized the F-actin cytoskeleton. Wall shear stress abrogated the morphological effects, but did not reverse the cytoskeleton disorganization.
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The cytoskeleton coordinates all aspects of growth in plant cells, including exocytosis of membrane and wall components during cell expansion. This review seeks to integrate current information about cytoskeletal components in plants and the role they play in generating cell form. Advances in genome analysis have fundamentally changed the nature of research strategies and generated an explosion of new information on the cytoskeleton-associated proteins, their regulation, and their role in signaling to the cytoskeleton. Some of these proteins appear novel to plants, but many have close homologues in other eukaryotic systems. It is becoming clear that the mechanisms behind cell growth are essentially similar across the growth continuum, which ranges from tip growth to diffuse expansion. Remodeling of the actin cytoskeleton at sites of exocytosis is an especially critical feature of polarized and may also contribute to axial growth. We evaluate the most recent work on the signaling mechanisms that continually remodel the actin cytoskeleton via the activation of actin-binding proteins (ABPs) and consider the role the microtubule cytoskeleton plays in this process.
Actin remodeling
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Actin remodeling
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In the present study we analysed the changes in cytoskeleton actin in lymphoid cells following IL-2 activation and during cell interactions by means of light and electron microscopy, immunofluorescence and molecular analysis. By morphological analysis we observed a higher fluorescence in the activated cells than in the quiescent ones with no modifications in the cytoskeleton pattern comparing activated to resting cells. The results of molecular analysis indicate that, after IL-2 activation, there is a reorganisation of the actin component of the cell cytoskeleton accompanied by the differential expression of the corresponding genes. A future study will be extended to the analysis of others components of the cytoskeleton network.
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Podocalyxin
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Living cells respond to external stimuli through the reorganization of the actin cytoskeleton, and the actin cytoskeleton significantly affects the cellular mechanical behavior. However, due to the lack of approaches to actin cytoskeleton quantification, the dynamics of mechanotransduction is still poorly understood. In this study, we propose an image recognition-based quantification (IRQ) approach to actin cytoskeleton quantification. IRQ quantifies the actin cytoskeleton through three parameters: the partial actin-cytoskeletal deviation (PAD), the total actin-cytoskeletal deviation (TAD) and the average actin-cytoskeletal intensity (AAI). First, Canny and Sobel edge detectors are applied to skeletonize the actin cytoskeleton images, then PAD and TAD are quantified using the direction of lines detected by Hough transform, and AAI is calculated through the summational brightness over the detected cell area. For validation, six different actin cytoskeleton meshwork models were generated to verify the quantification accuracy of IRQ. The average error for both the quantified PAD and TAD was less than 1.22°. Then IRQ was implemented to quantify the actin cytoskeleton of NIH/3T3 cells treated with an F-actin inhibitor. The quantification results suggest that the local and total actin-cytoskeletal organization of treated cells were more disordered than untreated cells, and the quantity of the actin cytoskeleton decreased significantly after the F-actin treatment.
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Quantification of the actin cytoskeleton is of prime importance to unveil the cellular force sensing and transduction mechanism. Although fluorescence imaging provides a convenient tool for observing the morphology of the actin cytoskeleton, due to the lack of approaches to accurate actin cytoskeleton quantification, the dynamics of mechanotransduction is still poorly understood. Currently, the existing image-based actin cytoskeleton analysis tools are either incapable of quantifying both the orientation and the quantity of the actin cytoskeleton simultaneously or the quantified results are subject to analysis artifacts. In this study, we propose an image recognition-based actin cytoskeleton quantification (IRAQ) approach, which quantifies both the actin cytoskeleton orientation and quantity by using edge, line, and brightness detection algorithms. The actin cytoskeleton is quantified through three parameters: the partial actin-cytoskeletal deviation (PAD), the total actin-cytoskeletal deviation (TAD), and the average actin-cytoskeletal intensity (AAI). First, Canny and Sobel edge detectors are applied to skeletonize the actin cytoskeleton images, then PAD and TAD are quantified using the line directions detected by Hough transform, and AAI is calculated through the summational brightness over the detected cell area. To verify the quantification accuracy, the proposed IRAQ was applied to six artificially-generated actin cytoskeleton mesh work models. The average error for both the quantified PAD and TAD was less than 1.22 ∘ . Then, IRAQ was implemented to quantify the actin cytoskeleton of NIH/3T3 cells treated with an F-actin inhibitor (latrunculin B). The quantification results suggest that the local and total actin-cytoskeletal organization became more disordered with the increase of latrunculin B dosage, and the quantity of the actin cytoskeleton showed a monotonically decreasing relation with latrunculin B dosage.
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Nox generated ROS, particularly those derived from Nox1, Nox2 and Nox4, have emerged as important regulators of the actin cytoskeleton and cytoskeleton-supported cell functions, such as migration and adhesion. The effects of Nox-derived ROS on cytoskeletal remodeling may be largely attributed to the ability of ROS to directly modify proteins that constitute or are associated with the cytoskeleton. Additionally, Nox-derived ROS may participate in signaling pathways governing cytoskeletal remodeling. In addition to these more extensively studied signaling pathways involving Nox-derived ROS, there also exist redox sensitive pathways for which the source of ROS is unclear. ROS from as of yet undetermined sources play a role in modifying, and thus regulating, the activity of several proteins critical for remodeling of the actin cytoskeleton. In this review we discuss ROS sensitive targets that are likely to affect cytoskeletal dynamics, as well as the potential involvement of Nox proteins. Keywords: Cytoskeleton, NADPH oxidase, ROS, oxidation, signaling.
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Actin cytoskeleton plays crucial roles in various cellular functions. Extracellular matrix (ECM) can modulate cell morphology by remodeling the internal cytoskeleton. To define how geometry of ECM regulates the organization of actin cytoskeleton, we plated individual NIH 3T3 cells on micropatterned substrates with distinct shapes and sizes. It was found that the stress fibers could form along the nonadhesive edges of T-shaped pattern, but were absent from the opening edge of V-shaped pattern, indicating that the organization of actin cytoskeleton was dependent on the mechanical environment. Furthermore, a secondary actin ring was observed on 50[Formula: see text][Formula: see text]m circular pattern while did not appear on 30[Formula: see text][Formula: see text]m and 40[Formula: see text][Formula: see text]m pattern, showing a size-dependent organization of actin cytoskeleton. Finally, osteoblasts, MDCK and A549 cells exhibited distinct organization of actin cytoskeleton on T-shaped pattern, suggesting a cell-type specificity in arrangement of actin cytoskeleton. Together, our findings brought novel insight into the organization of actin cytoskeleton on micropatterned environments.
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The plant cytoskeleton, consisting of actin filaments and microtubules, is a highly dynamic filamentous framework involved in plant growth, development, and stress responses. Recently, research has demonstrated that the plant cytoskeleton undergoes rapid remodeling upon sensing pathogen attacks, coordinating the formation of microdomain immune complexes, the dynamic and turnover of pattern-recognizing receptors (PRRs), the movement and aggregation of organelles, and the transportation of defense compounds, thus serving as an important platform for responding to pathogen infections. Meanwhile, pathogens produce effectors targeting the cytoskeleton to achieve pathogenicity. Recent findings have uncovered several cytoskeleton-associated proteins mediating cytoskeletal remodeling and defense signaling. Furthermore, the reorganization of the actin cytoskeleton is revealed to further feedback-regulate reactive oxygen species (ROS) production and trigger salicylic acid (SA) signaling, suggesting an extremely complex role of the cytoskeleton in plant immunity. Here, we describe recent advances in understanding the host cytoskeleton dynamics upon sensing pathogens and summarize the effectors that target the cytoskeleton. We highlight advances in the regulation of cytoskeletal remodeling associated with the defense response and assess the important function of the rearrangement of the cytoskeleton in the immune response. Finally, we propose suggestions for future research in this area.
Actin remodeling
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