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Organoids as an Emerging Tool for Nano-Pharmaceuticals
Published in Harishkumar Madhyastha, Durgesh Nandini Chauhan, Nanopharmaceuticals in Regenerative Medicine, 2022
At a cellular level, after sensing the cues, these cues may be processed as external stimuli by modulating the microenvironment and inducing specific responses through activation of genetic programme, known as the mechanotransduction process (Chan et al. 2017, Davidson 2017). These biophysical signals are interpreted by a set of specialised proteins and their dysregulation, in turn, leads to various pathologies. Vinculin is an important mechanotransducter, serving as a linker for integrins to cytoskeleton, and pathogenic variations in this protein in humans are reported in various pathologies like cancer, cardiomyopathies, and neural defects (Olson et al. 2002, Vasile et al. 2006, Liang et al. 2014, Chinthalapudi et al. 2016).
The Rous Sarcoma Virus Oncogene and its Proto-Oncogene Counterpart
Published in Pimentel Enrique, Oncogenes, 2020
In addition to 34K, two other cytoplasmic proteins, with mol wt of 50,000-dalton (50K) and 90,000-daltons (90K), also interact with pp60src but their respective functions are also not understood.112,113 Other protein substrates for pp60Art kinase activity may have higher molecular weights and about 30% of phosphotyrosine-containing protein molecules present in RSV-transformed cells have sizes greater than 100,000 daltons.114 A well identifed target, phosphorylated on tyrosine residues by the action of pp60src, is vinculin,115,116 a 130,000-daltons (130K) cytoskeletal protein which is apparently involved in the anchorage of microfilaments to the plasma membrane. However, additional phosphorylation of tyrosine residues in vinculin does not occur upon transformation by some ASV.117 The functional significance of this type of vinculin modification remains undetermined.
Dermal Fibroblast Function
Published in Brian J. Nickoloff, Dermal Immune System, 2019
Integrins are membrane proteins which link collagen, fibronectin, and laminin to actin within the cell via the interposition of talin and vinculin at adhesion plaques.79,80 The fact that fibronectin binds to collagen, proteoglycan (heparin, heparan sulfate, and hyaluronic acid), and to the surfaces of fibroblasts and other cells likely allows it to play a central role in matrix organization.41,81–84 Several growth factors (PDGF, TGF-β, and FGF) induce mobilization of vinculin and can alter focal adhesions.85–87
Serum claudin-5, claudin-11, occludin, vinculin, paxillin, and beta-catenin levels in preschool children with autism spectrum disorder
Published in Nordic Journal of Psychiatry, 2023
Ayhan Bilgiç, Hurşit Ferahkaya, Hülya Karagöz, İbrahim Kılınç, Vesile Meltem Energin
Vinculin and paxillin may be other important molecules for BBB and intestinal barrier functions. Vinculin is a cytoplasmic protein that functions in cell-matrix and cell-cell adhesions and regulation of apoptosis. This molecule also plays a role in the regulation of tight junctions in the intestinal barrier. Like occludin, the research by Vojdani and colleagues found an elevation in antibody production against vinculin in patients with celiac disease and supported its role in intestinal permeability [24]. Paxillin is first defined as a cytoplasmic scaffold/adaptor protein that plays a crucial role in focal adhesion. However, further studies demonstrate that it could also have functions in cell migration, proliferation, and as a regulator of mRNA trafficking and subsequent translation [28]. Therefore, as well as their potential effects on barrier structures, these two molecules contribute to the development of ASD by affecting many developmental and physiological processes.
In vitro stimulation with radiofrequency currents promotes proliferation and migration in human keratinocytes and fibroblasts
Published in Electromagnetic Biology and Medicine, 2021
María Luisa Hernández-Bule, Elena Toledano-Macías, Aida Naranjo, Marina de Andrés-Zamora, Alejandro Úbeda
Vinculin is a protein involved in cell-to-substrate adhesion and cell migration at the three-dimensional level. This anchorage to the substrate is the supporting point for the elongation, orientation and traction of the cytoskeleton during migration (Thievessen et al. 2015). Vinculin is mainly located in: 1) focal complexes present in the lamellipodia emitted by the cells situated on the migration front, and 2) focal adhesions present in the region of the plasma membrane that contacts with the substrate, connecting integrins with the cytoskeleton and attaching the cell to the substrate. In order to be functionally active, vinculin must be located in cytoplasm regions close to the plasma membrane, although prior to migration, unfastening and degradation of this protein are also necessary for disruption of the cell-to-substrate junction (Goldmann 2016). In keratinocytes, the CRET-induced increase in the expression and translocation of vinculin to the membrane of cells placed on the migration front (Figures 7 and Figures 8) could be expected to promote cell migration. However, the wound assay did not detect increased migration rates in electrically treated keratinocytes.
RhoA Activation Decreases Phagocytosis of Trabecular Meshwork Cells
Published in Current Eye Research, 2021
Tomokazu Fujimoto, Saori Sato-Ohira, Hidenobu Tanihara, Toshihiro Inoue
Immunostaining of F-actin and vinculin was performed at 1 h after treatment with LPA with or without C3 or Y-27632 (Figure 4a). Immunostaining of vinculin was performed to confirm focal adhesion. LPA treatment increased focal adhesion and stress fiber formation in TM cells. C3 and Y-27632 prevented stress fiber and focal adhesion formation by LPA. Moreover, the effects of LPA on F-actin and focal adhesion were evaluated in RhoA siRNA-transfected TM cells (Figure 5a). LPA increased stress fiber and focal adhesion formation in control siRNA-transfected cells. In contrast, in RhoA siRNA-transfected cells, LPA did not increase stress fiber and focal adhesion. The intracellular localization of YAP and TAZ was also examined (Figures 4b, 5b). The activity of the transcriptional coactivators YAP and TAZ is regulated by intracellular localization.32,33 In a previous report, LPA induced YAP/TAZ nuclear accumulation in TM cells,30 and we confirmed the nuclear accumulation of YAP/TAZ after LPA treatment (Figures 4b, 5b). In contrast, C3 and Y-27632 prevented the nuclear accumulation of YAP/TAZ by LPA treatment (Figure 4b). RhoA siRNA transfection did not prevent the effect of LPA on YAP/TAZ accumulation; however basal YAP nuclear accumulation was decreased in RhoA siRNA-transfected TM cells (Figure 5b).