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Artykuły w czasopismach na temat „Vimentin”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 25 lipca 2025

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1

Dent, J. A., R. B. Cary, J. B. Bachant, A. Domingo, and M. W. Klymkowsky. "Host cell factors controlling vimentin organization in the Xenopus oocyte." Journal of Cell Biology 119, no. 4 (1992): 855–66. http://dx.doi.org/10.1083/jcb.119.4.855.

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To study vimentin filament organization in vivo we injected Xenopus oocytes, which have no significant vimentin system of their own, with in vitro-synthesized RNAs encoding Xenopus vimentins. Exogenous vimentins were localized primarily to the cytoplasmic surface of the nucleus and to the subplasma membrane "cortex." In the cortex of the animal hemisphere, wild-type vimentin forms punctate structures and short filaments. In contrast, long anastomosing vimentin filaments are formed in the vegetal hemisphere cortex. This asymmetry in the organization of exogenous vimentin is similar to that of t

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2

Niazi Tabar, Amirreza, Hossein Azizi, Danial Hashemi Karoii, and Thomas Skutella. "Testicular Localization and Potential Function of Vimentin Positive Cells during Spermatogonial Differentiation Stages." Animals 12, no. 3 (2022): 268. http://dx.doi.org/10.3390/ani12030268.

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Vimentin is a type of intermediate filament (IF) and one of the first filaments expressed in spermatogenesis. Vimentin plays numerous roles, consisting of the determination of cell shape, differentiation, cell motility, the maintenance of cell junctions, intracellular trafficking, and assisting in keeping normal differentiating germ cell morphology. This study investigated the vimentin expression in two populations of undifferentiated and differentiated spermatogonia. We examined vimentin expression in vivo and in vitro by immunocytochemistry (ICC), immunohistochemistry (IMH), and Fluidigm rea

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Kohl, Tobias, Melanie von Brandenstein, Andreas Stog, et al. "Vimentin 3 and endothelin in prostate cancer." Journal of Clinical Oncology 36, no. 6_suppl (2018): 349. http://dx.doi.org/10.1200/jco.2018.36.6_suppl.349.

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349 Background: An upregulation of vimentin 3, a truncated version of the full length vimentin, with an unknown function, was previously described by our group, in a direct dependency of increased ET-1 levels. We analyzed now vimentin 3 in further genitourinary cancers. Here, we describe our findings how vimentin 3 is part of the signaling pathways from Endothelin-1 (ET-1) and the Endothelin-A-Receptor (ETAR) and how it correlates with aggressive tumor behavior in a PCa cell culture and in human tissue and serum samples from PCa patients. Methods: DU145 cells were cultured. We stimulated with

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4

Costigliola, Nancy, Liya Ding, Christoph J. Burckhardt, et al. "Vimentin fibers orient traction stress." Proceedings of the National Academy of Sciences 114, no. 20 (2017): 5195–200. http://dx.doi.org/10.1073/pnas.1614610114.

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The intermediate filament vimentin is required for cells to transition from the epithelial state to the mesenchymal state and migrate as single cells; however, little is known about the specific role of vimentin in the regulation of mesenchymal migration. Vimentin is known to have a significantly greater ability to resist stress without breaking in vitro compared with actin or microtubules, and also to increase cell elasticity in vivo. Therefore, we hypothesized that the presence of vimentin could support the anisotropic mechanical strain of single-cell migration. To study this, we fluorescent

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5

Wang, Ruping, Sakeeb Khan, Guoning Liao, Yidi Wu, and Dale D. Tang. "Nestin Modulates Airway Smooth Muscle Cell Migration by Affecting Spatial Rearrangement of Vimentin Network and Focal Adhesion Assembly." Cells 11, no. 19 (2022): 3047. http://dx.doi.org/10.3390/cells11193047.

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Airway smooth muscle cell migration plays a role in the progression of airway remodeling, a hallmark of allergic asthma. However, the mechanisms that regulate cell migration are not yet entirely understood. Nestin is a class VI intermediate filament protein that is involved in the proliferation/regeneration of neurons, cancer cells, and skeletal muscle. Its role in cell migration is not fully understood. Here, nestin knockdown (KD) inhibited the migration of human airway smooth muscle cells. Using confocal microscopy and the Imaris software, we found that nestin KD attenuated focal adhesion si

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6

Ivaska, Johanna. "Vimentin." Small GTPases 2, no. 1 (2011): 51–53. http://dx.doi.org/10.4161/sgtp.2.1.15114.

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7

Cary, R. B., M. W. Klymkowsky, R. M. Evans, A. Domingo, J. A. Dent, and L. E. Backhus. "Vimentin's tail interacts with actin-containing structures in vivo." Journal of Cell Science 107, no. 6 (1994): 1609–22. http://dx.doi.org/10.1242/jcs.107.6.1609.

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The tail domain of the intermediate filament (IF) protein vimentin is unnecessary for IF assembly in vitro. To study the role of vimentin's tail in vivo, we constructed a plasmid that directs the synthesis of a ‘myc-tagged’ version of the Xenopus vimentin-1 tail domain in bacteria. This polypeptide, mycVimTail, was purified to near homogeneity and injected into cultured Xenopus A6 cells. In these cells the tail polypeptide co-localized with actin even in the presence of cytochalasin. Two myc-tagged control polypeptides argue for the specificity of this interaction. First, a similarly myc-tagge

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8

Paramita, Paramita, Melva Louisa, and Nafrialdi Nafrialdi. "Increased vimentin mRNA expression in MCF-7 breast cancer cell line after repeated endoxifen-treatment." Medical Journal of Indonesia 25, no. 4 (2017): 207–13. http://dx.doi.org/10.13181/mji.v25i4.1397.

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Background: Epithelial mesenchymal transition (EMT) plays a significant role in the development of cancer cell resistance to drugs. Vimentin, a type III intermediate filament protein, is a marker of EMT. Vimentin's over-expression in cancer correlates well with increased tumor growth, change in cell shape and poor prognosis. Endoxifen is an active metabolite of tamoxifen and has become a new potent agent in the treatment of breast cancer. This is a study that aimed to investigate the effect of endoxifen exposure with or without estradiol on cell viability, cell morphology and EMT progression t

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9

Ngai, J., V. C. Bond, B. J. Wold, and E. Lazarides. "Expression of transfected vimentin genes in differentiating murine erythroleukemia cells reveals divergent cis-acting regulation of avian and mammalian vimentin sequences." Molecular and Cellular Biology 7, no. 11 (1987): 3955–70. http://dx.doi.org/10.1128/mcb.7.11.3955-3970.1987.

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We studied the expression of transfected chicken and hamster vimentin genes in murine erythroleukemia (MEL) cells. MEL cells normally repress the levels of endogenous mouse vimentin mRNA during inducermediated differentiation, resulting in a subsequent loss of vimentin filaments. Expression of vimentin in differentiating MEL cells reflects the disappearance of vimentin filaments during mammalian erythropoiesis in vivo. In contrast, chicken erythroid cells express high levels of vimentin mRNA and vimentin filaments during terminal differentiation. We demonstrate here that chicken vimentin mRNA

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10

Ngai, J., V. C. Bond, B. J. Wold, and E. Lazarides. "Expression of transfected vimentin genes in differentiating murine erythroleukemia cells reveals divergent cis-acting regulation of avian and mammalian vimentin sequences." Molecular and Cellular Biology 7, no. 11 (1987): 3955–70. http://dx.doi.org/10.1128/mcb.7.11.3955.

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We studied the expression of transfected chicken and hamster vimentin genes in murine erythroleukemia (MEL) cells. MEL cells normally repress the levels of endogenous mouse vimentin mRNA during inducermediated differentiation, resulting in a subsequent loss of vimentin filaments. Expression of vimentin in differentiating MEL cells reflects the disappearance of vimentin filaments during mammalian erythropoiesis in vivo. In contrast, chicken erythroid cells express high levels of vimentin mRNA and vimentin filaments during terminal differentiation. We demonstrate here that chicken vimentin mRNA

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11

Wang, Kai, Boxiang Du, Yan Zhang, et al. "Vimentin-Rab7a Pathway Mediates the Migration of MSCs and Lead to Therapeutic Effects on ARDS." Stem Cells International 2021 (July 29, 2021): 1–12. http://dx.doi.org/10.1155/2021/9992381.

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Acute respiratory distress syndrome (ARDS) is difficult to treat and has a high mortality rate. Mesenchymal stem cells (MSCs) have an important therapeutic effect in ARDS. While the mechanism of MSC migration to the lungs remains unclear, the role of MSCs is of great clinical significance. To this end, we constructed vimentin knockout mice, extracted bone MSCs from the mice, and used them for the treatment of LPS-induced ARDS. H&E staining and Masson staining of mouse lung tissue allowed us to assess the degree of damage and fibrosis of mouse lung tissue. By measuring serum TNF-α, TGF-β, a

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12

Scally, Stephen W., Soi-Cheng Law, Yi Tian Ting, et al. "Molecular basis for increased susceptibility of Indigenous North Americans to seropositive rheumatoid arthritis." Annals of the Rheumatic Diseases 76, no. 11 (2017): 1915–23. http://dx.doi.org/10.1136/annrheumdis-2017-211300.

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ObjectiveThe pathogenetic mechanisms by which HLA-DRB1 alleles are associated with anticitrullinated peptide antibody (ACPA)-positive rheumatoid arthritis (RA) are incompletely understood. RA high-risk HLA-DRB1 alleles are known to share a common motif, the ‘shared susceptibility epitope (SE)’. Here, the electropositive P4 pocket of HLA-DRB1 accommodates self-peptide residues containing citrulline but not arginine. HLA-DRB1 His/Phe13β stratifies with ACPA-positive RA, while His13βSer polymorphisms stratify with ACPA-negative RA and RA protection. Indigenous North American (INA) populations hav

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13

Yamaguchi, Tomoya, Hidemasa Goto, Tomoya Yokoyama, et al. "Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis." Journal of Cell Biology 171, no. 3 (2005): 431–36. http://dx.doi.org/10.1083/jcb.200504091.

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Several kinases phosphorylate vimentin, the most common intermediate filament protein, in mitosis. Aurora-B and Rho-kinase regulate vimentin filament separation through the cleavage furrow-specific vimentin phosphorylation. Cdk1 also phosphorylates vimentin from prometaphase to metaphase, but its significance has remained unknown. Here we demonstrated a direct interaction between Plk1 and vimentin-Ser55 phosphorylated by Cdk1, an event that led to Plk1 activation and further vimentin phosphorylation. Plk1 phosphorylated vimentin at ∼1 mol phosphate/mol substrate, which partly inhibited its fil

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14

Carse, Sinead, Dirk Lang, Arieh A. Katz, and Georgia Schäfer. "Exogenous Vimentin Supplementation Transiently Affects Early Steps during HPV16 Pseudovirus Infection." Viruses 13, no. 12 (2021): 2471. http://dx.doi.org/10.3390/v13122471.

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Understanding and modulating the early steps in oncogenic Human Papillomavirus (HPV) infection has great cancer-preventative potential, as this virus is the etiological agent of virtually all cervical cancer cases and is associated with many other anogenital and oropharyngeal cancers. Previous work from our laboratory has identified cell-surface-expressed vimentin as a novel HPV16 pseudovirus (HPV16-PsVs)-binding molecule modulating its infectious potential. To further explore its mode of inhibiting HPV16-PsVs internalisation, we supplemented it with exogenous recombinant human vimentin and sh

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15

Roy, Sujayita, Arun Kapoor, Fei Zhu, et al. "Artemisinins target the intermediate filament protein vimentin for human cytomegalovirus inhibition." Journal of Biological Chemistry 295, no. 44 (2020): 15013–28. http://dx.doi.org/10.1074/jbc.ra120.014116.

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The antimalarial agents artemisinins inhibit cytomegalovirus (CMV) in vitro and in vivo, but their target(s) has been elusive. Using a biotin-labeled artemisinin, we identified the intermediate filament protein vimentin as an artemisinin target, validated by detailed biochemical and biological assays. We provide insights into the dynamic and unique modulation of vimentin, depending on the stage of human CMV (HCMV) replication. In vitro, HCMV entry and viral progeny are reduced in vimentin-deficient fibroblasts, compared with control cells. Similarly, mouse CMV (MCMV) replication in vimentin kn

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16

Wang, Ruping, Qing-Fen Li, Yana Anfinogenova, and Dale D. Tang. "Dissociation of Crk-associated substrate from the vimentin network is regulated by p21-activated kinase on ACh activation of airway smooth muscle." American Journal of Physiology-Lung Cellular and Molecular Physiology 292, no. 1 (2007): L240—L248. http://dx.doi.org/10.1152/ajplung.00199.2006.

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The intermediate filament protein vimentin has been shown to be required for smooth muscle contraction. The adapter protein p130 Crk-associated substrate (CAS) participates in the signaling processes that regulate force development in smooth muscle. However, the interaction of vimentin filaments with CAS has not been well elucidated. In the present study, ACh stimulation of tracheal smooth muscle strips increased the ratio of soluble to insoluble vimentin (an index of vimentin disassembly) in association with force development. ACh activation also induced vimentin phosphorylation at Ser56 as a

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17

Wang, Ruping, Qingfen Li, and Dale D. Tang. "Role of vimentin in smooth muscle force development." American Journal of Physiology-Cell Physiology 291, no. 3 (2006): C483—C489. http://dx.doi.org/10.1152/ajpcell.00097.2006.

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Vimentin intermediate filaments undergo spatial reorganization in cultured smooth muscle cells in response to contractile activation; however, the role of vimentin in the physiological properties of smooth muscle has not been well elucidated. Tracheal smooth muscle strips were loaded with antisense oligonucleotides (ODNs) against vimentin and then cultured for 2 days to allow for protein degradation. Treatment with vimentin antisense, but not sense, ODNs suppressed vimentin protein expression; neither vimentin antisense nor sense ODNs affected protein levels of desmin and actin. Force developm

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18

Mónico, Andreia, Silvia Zorrilla, Germán Rivas, and Dolores Pérez-Sala. "Zinc Differentially Modulates the Assembly of Soluble and Polymerized Vimentin." International Journal of Molecular Sciences 21, no. 7 (2020): 2426. http://dx.doi.org/10.3390/ijms21072426.

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The intermediate filament protein vimentin constitutes a critical sensor for electrophilic and oxidative stress. We previously showed that vimentin interacts with zinc, which affects its assembly and redox sensing. Here, we used vimentin wt and C328S, an oxidation-resistant mutant showing improved NaCl-induced polymerization, to assess the impact of zinc on soluble and polymerized vimentin by light scattering and electron microscopy. Zinc acts as a switch, reversibly inducing the formation of vimentin oligomeric species. High zinc concentrations elicit optically-detectable vimentin structures

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19

Menko, A. S., B. M. Bleaken, A. A. Libowitz, L. Zhang, M. A. Stepp, and J. L. Walker. "A central role for vimentin in regulating repair function during healing of the lens epithelium." Molecular Biology of the Cell 25, no. 6 (2014): 776–90. http://dx.doi.org/10.1091/mbc.e12-12-0900.

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Mock cataract surgery provides a unique ex vivo model for studying wound repair in a clinically relevant setting. Here wound healing involves a classical collective migration of the lens epithelium, directed at the leading edge by an innate mesenchymal subpopulation of vimentin-rich repair cells. We report that vimentin is essential to the function of repair cells as the directors of the wound-healing process. Vimentin and not actin filaments are the predominant cytoskeletal elements in the lamellipodial extensions of the repair cells at the wound edge. These vimentin filaments link to paxilli

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20

Kueper, Thomas, Tilman Grune, Gesa-Meike Muhr, et al. "Modification of Vimentin." Annals of the New York Academy of Sciences 1126, no. 1 (2008): 328–32. http://dx.doi.org/10.1196/annals.1433.039.

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Trevor, K. T., J. G. McGuire, and E. V. Leonova. "Association of vimentin intermediate filaments with the centrosome." Journal of Cell Science 108, no. 1 (1995): 343–56. http://dx.doi.org/10.1242/jcs.108.1.343.

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SW-13 cells that lack cytoplasmic intermediate filaments (IFs) were stably transfected with a human vimentin cDNA expression vector. Isolated subclones displayed two prevalent patterns of vimentin distribution as observed by indirect immuno-localization: (1) cytoplasmic filaments characteristic of a vimentin IF network; and (2) a distinct, juxtanuclear focus with limited filamentous extensions. Comparative analysis of two subclones that uniquely segregated these patterns of vimentin organization indicated that vimentin accumulated as a perinuclear focus in cells that expressed a 4-fold lower l

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22

Zhang, Xuefang, Guangming Cao, Xiaoli Diao, Wenyu Bai, Yang Zhang, and Shuzhen Wang. "Vimentin Protein In Situ Expression Predicts Less Tumor Metastasis and Overall Better Survival of Endometrial Carcinoma." Disease Markers 2022 (March 14, 2022): 1–12. http://dx.doi.org/10.1155/2022/5240046.

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Background. Vimentin, a cytoplasmic intermediate filament protein, has been recently identified to be a prognostic biomarker in some cancers. However, the function of vimentin in endometrial carcinoma (EC) remains unclear. Our study aimed at evaluating vimentin expression in EC and preliminarily exploring the role of vimentin in EC progression. Methods. In total, 341 EC patients who underwent surgical follow-up were enrolled in the retrospective study. Vimentin expression levels in EC tissues were analyzed using immunohistochemistry. Furthermore, the vimentin (VIM) gene expression levels in 54

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23

Chu, Shijian, Haishan Xu, Thomas J. Ferro, and Paola X. Rivera. "Poly(ADP-ribose) polymerase-1 regulates vimentin expression in lung cancer cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 293, no. 5 (2007): L1127—L1134. http://dx.doi.org/10.1152/ajplung.00197.2007.

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Vimentin is one of the mammalian intermediate filament proteins. It is expressed in cells of mesenchymal origin and is characteristic of proliferating cells at the fetal stage. During malignancy, vimentin expression is activated in certain lung epithelial cells. Examination of a group of lung cancer cells showed a marked difference in their vimentin expression. The difference in vimentin expression among lung cancer cells is due to differential regulation at the transcriptional level. Analysis of the vimentin promoter revealed a 102-bp promoter sequence that is important for promoter activity

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Sarria, A. J., S. K. Nordeen, and R. M. Evans. "Regulated expression of vimentin cDNA in cells in the presence and absence of a preexisting vimentin filament network." Journal of Cell Biology 111, no. 2 (1990): 553–65. http://dx.doi.org/10.1083/jcb.111.2.553.

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Human cells were transfected with a mouse vimentin cDNA expression vector containing the hormone response element of mouse mammary tumor virus. The distribution of mouse vimentin after induction with dexamethasone was examined by indirect immunofluorescence with antivimentin antibodies specific for either mouse or human vimentin. In stably transfected HeLa cells, which contain vimentin filaments, addition of dexamethasone resulted in the initial appearance of mouse vimentin in discrete areas, usually perinuclear, that always corresponded to areas of the human filament network with the most int

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25

Malickova, Karin, Ivana Janatkova, Petra Sandova, and Terezie Fucikova. "Relationship of Anti-vimentin antibodies to anti-endothelial antibodies." Open Medicine 1, no. 3 (2006): 228–36. http://dx.doi.org/10.2478/s11536-006-0028-5.

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AbstractThe intermediate filament protein vimentin is a potential target antigen for autoantibodies in some infectious and autoimmune diseases. Because endothelial cells contain an extensive interconnecting cytoplasmic network of vimentin, we examined the relationship between anti-vimentin and anti-endothelial cell antibodies (AECAs). We measured the level of anti-vimentin antibodies in patients with systemic autoimmune diseases (n=42), healthy blood donors (n=58), and patients with acute inflammation and showing anti-vimentin immunofluorescence (n=50). AECAs were detected by indirect immunofl

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Lavenus, Sandrine B., Sara M. Tudor, Maria F. Ullo, Karl W. Vosatka, and Jeremy S. Logue. "A flexible network of vimentin intermediate filaments promotes migration of amoeboid cancer cells through confined environments." Journal of Biological Chemistry 295, no. 19 (2020): 6700–6709. http://dx.doi.org/10.1074/jbc.ra119.011537.

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Tumor cells can spread to distant sites through their ability to switch between mesenchymal and amoeboid (bleb-based) migration. Because of this difference, inhibitors of metastasis must account for each migration mode. However, the role of vimentin in amoeboid migration has not been determined. Because amoeboid leader bleb–based migration (LBBM) occurs in confined spaces and vimentin is known to strongly influence cell-mechanical properties, we hypothesized that a flexible vimentin network is required for fast amoeboid migration. To this end, here we determined the precise role of the vimenti

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Vohnoutka, Rishel B., Anushree C. Gulvady, Gregory Goreczny, et al. "The focal adhesion scaffold protein Hic-5 regulates vimentin organization in fibroblasts." Molecular Biology of the Cell 30, no. 25 (2019): 3037–56. http://dx.doi.org/10.1091/mbc.e19-08-0442.

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Focal adhesion (FA)-stimulated reorganization of the F-actin cytoskeleton regulates cellular size, shape, and mechanical properties. However, FA cross-talk with the intermediate filament cytoskeleton is poorly understood. Genetic ablation of the FA-associated scaffold protein Hic-5 in mouse cancer-associated fibroblasts (CAFs) promoted a dramatic collapse of the vimentin network, which was rescued following EGFP-Hic-5 expression. Vimentin collapse correlated with a loss of detergent-soluble vimentin filament precursors and decreased vimentin S72/S82 phosphorylation. Additionally, fluorescence

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Li, Zhenlin, Denise Paulin, Patrick Lacolley, Dario Coletti, and Onnik Agbulut. "Vimentin as a target for the treatment of COVID-19." BMJ Open Respiratory Research 7, no. 1 (2020): e000623. http://dx.doi.org/10.1136/bmjresp-2020-000623.

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We and others propose vimentin as a possible cellular target for the treatment of COVID-19. This innovative idea is so recent that it requires further attention and debate. The significant role played by vimentin in virus-induced infection however is well established: (1) vimentin has been reported as a co-receptor and/or attachment site for SARS-CoV; (2) vimentin is involved in viral replication in cells; (3) vimentin plays a fundamental role in both the viral infection and the consequent explosive immune-inflammatory response and (4) a lower vimentin expression is associated with the inhibit

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Tang, P., C. R. Sharpe, T. J. Mohun, and C. C. Wylie. "Vimentin expression in oocytes, eggs and early embryos of Xenopus laevis." Development 103, no. 2 (1988): 279–87. http://dx.doi.org/10.1242/dev.103.2.279.

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Immunocytochemical studies using a monoclonal anti-porcine vimentin antibody reveal a well-organized pattern of staining in Xenopus laevis oocytes, eggs and early embryos. The positions of Xenopus vimentin and desmin in two-dimensional (2D) polyacrylamide gels were first established by immunoblotting of muscle Triton extracts with anti-intermediate filament antibodies (anti-IFA), which cross-react with all intermediate filament proteins (IFPs). The anti-porcine vimentin reacts with vimentin and desmin in muscle 2D immunoblots, but only reacts with one polypeptide in oocyte blots in the positio

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Kanaji, Nobuhiro, Kyuichi Kadota, Akira Tadokoro, et al. "Serum CYFRA 21-1 but not Vimentin is Associated with Poor Prognosis in Advanced Lung Cancer Patients." Open Respiratory Medicine Journal 13, no. 1 (2019): 31–38. http://dx.doi.org/10.2174/1874306401913010031.

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Background: Cytokeratins and Vimentin are intermediate filament proteins. Vimentin expression in tissue samples has been reported to be associated with a poor prognosis in non-small cell lung cancer patients who underwent surgery. CYFRA 21-1 (Cytokeratin 19 Fragment) is a well known tumor marker. Objective: This study aimed to investigate the usefulness of serum vimentin as a tumor marker and significance of CYFRA 21-1 and vimentin expression on prognosis of advanced lung cancer patients. Methods: One hundred and four advanced lung cancer patients and 19 non-lung cancer patients were included.

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Evans, R. M. "Phosphorylation of vimentin in mitotically selected cells. In vitro cyclic AMP-independent kinase and calcium-stimulated phosphatase activities." Journal of Cell Biology 108, no. 1 (1989): 67–78. http://dx.doi.org/10.1083/jcb.108.1.67.

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The phosphorylation of the intermediate filament protein vimentin was examined under in vitro conditions. Cell cytosol and Triton-insoluble cytoskeleton preparations from nonmitotic and mitotically selected mouse L-929 cells exhibited vimentin kinase activity that is apparently cAMP and Ca2+ independent. The level of vimentin kinase activity was greater in preparations from mitotically selected cells than nonmitotic cells. Addition of Ca2+ to mitotic cytosol decreased net vimentin phosphorylation. Dephosphorylation experiments indicated that there is phosphatase activity in these preparations

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32

Tsuru, A., N. Nakamura, E. Takayama, Y. Suzuki, K. Hirayoshi, and K. Nagata. "Regulation of the expression of vimentin gene during the differentiation of mouse myeloid leukemia cells." Journal of Cell Biology 110, no. 5 (1990): 1655–64. http://dx.doi.org/10.1083/jcb.110.5.1655.

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We have examined the expression of vimentin during the differentiation of mouse myeloid leukemia cells (M1), which were induced to differentiate into macrophages by exposure to conditioned medium (CM) obtained from rat embryo fibroblasts. The synthesis of vimentin, which was examined by two-dimensional gel electrophoresis, increased after 12-24 h of incubation of M1 cells in CM and the elevated level of synthesis continued up to 96 h. A macrophage cell line (Mm1) that was derived from spontaneously differentiated M1 cells constantly synthesized much higher levels of vimentin. The amount of vim

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Gao, Ya-sheng, and Elizabeth Sztul. "A Novel Interaction of the Golgi Complex with the Vimentin Intermediate Filament Cytoskeleton." Journal of Cell Biology 152, no. 5 (2001): 877–94. http://dx.doi.org/10.1083/jcb.152.5.877.

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The integration of the vimentin intermediate filament (IF) cytoskeleton and cellular organelles in vivo is an incompletely understood process, and the identities of proteins participating in such events are largely unknown. Here, we show that the Golgi complex interacts with the vimentin IF cytoskeleton, and that the Golgi protein formiminotransferase cyclodeaminase (FTCD) participates in this interaction. We show that the peripherally associated Golgi protein FTCD binds directly to vimentin subunits and to polymerized vimentin filaments in vivo and in vitro. Expression of FTCD in cultured cel

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Tang, Ho Lam, Hong Lok Lung, Ka Chun Wu, Anh-Huy Phan Le, Ho Man Tang, and Ming Chiu Fung. "Vimentin supports mitochondrial morphology and organization." Biochemical Journal 410, no. 1 (2008): 141–46. http://dx.doi.org/10.1042/bj20071072.

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Vimentin is one of the intermediate filaments that functions in structural support, signal transduction and organelle positioning of a cell. In the present study, we report the contribution of vimentin in mitochondrial morphology and organization. Using subcellular fractionation, immunoprecipitation and fluorescence microscopy analyses, we found that vimentin was associated with mitochondria. Knockdown of vimentin resulted in mitochondrial fragmentation, swelling and disorganization. We further demonstrated that the vimentin cytoskeleton co-localized and interacted with mitochondria to a great

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Coleman, T. R., and E. Lazarides. "Continuous growth of vimentin filaments in mouse fibroblasts." Journal of Cell Science 103, no. 3 (1992): 689–98. http://dx.doi.org/10.1242/jcs.103.3.689.

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We have investigated the dynamics of intermediate filament assembly in vivo by following the fate of heterologous chicken vimentin subunits expressed under the control of an inducible promoter in transfected mouse fibroblasts. Using RNase protection, metabolic protein pulse-chase and immunofluorescence microscopy, we have examined the fate of newly assembled subunits under physiological conditions in situ. Following induction and subsequent removal of inducer, chicken vimentin mRNA had a half-life of approximately 6 h while both chicken and mouse vimentin protein polymer had long half-lives--r

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Correia, Ivan, Donald Chu, Ying-Hao Chou, Robert D. Goldman, and Paul Matsudaira. "Integrating the Actin and Vimentin Cytoskeletons." Journal of Cell Biology 146, no. 4 (1999): 831–42. http://dx.doi.org/10.1083/jcb.146.4.831.

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Cells adhere to the substratum through specialized structures that are linked to the actin cytoskeleton. Recent studies report that adhesion also involves the intermediate filament (IF) and microtubule cytoskeletons, although their mechanisms of interaction are unknown. Here we report evidence for a novel adhesion-dependent interaction between components of the actin and IF cytoskeletons. In biochemical fractionation experiments, fimbrin and vimentin coprecipitate from detergent extracts of macrophages using vimentin- or fimbrin-specific antisera. Fluorescence microscopy confirms the biochemic

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Zhang, Xi, Xiaogang Wang, Taixiu Liu, et al. "Smad2/3 Upregulates the Expression of Vimentin and Affects Its Distribution in DBP-Exposed Sertoli Cells." PPAR Research 2015 (2015): 1–11. http://dx.doi.org/10.1155/2015/489314.

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Sertoli cells (SCs) in the testes provide physical and nutritional support to germ cells. The vimentin cytoskeleton in SCs is disrupted by dibutyl phthalate (DBP), which leads to SCs dysfunction. In a previous study, we found that peroxisome proliferator-activated receptor alpha (PPARα) influenced the distribution of vimentin by affecting its phosphorylation in DBP-exposed SCs. In the present study, we investigated the role of Smad2/3 in regulating the expression of vimentin in DBP-exposed SCs. We hypothesized that Smad2/3 affects the distribution of vimentin by regulating its expression and t

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Valgeirsdottir, S., L. Claesson-Welsh, E. Bongcam-Rudloff, U. Hellman, B. Westermark, and C. H. Heldin. "PDGF induces reorganization of vimentin filaments." Journal of Cell Science 111, no. 14 (1998): 1973–80. http://dx.doi.org/10.1242/jcs.111.14.1973.

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In this study we demonstrate that stimulation with platelet-derived growth factor (PDGF) leads to a marked reorganization of the vimentin filaments in porcine aortic endothelial (PAE) cells ectopically expressing the PDGF beta-receptor. Within 20 minutes after stimulation, the well-spread fine fibrillar vimentin was reorganized as the filaments aggregated into a dense coil around the nucleus. The solubility of vimentin upon Nonidet-P40-extraction of cells decreased considerably after PDGF stimulation, indicating that PDGF caused a redistribution of vimentin to a less soluble compartment. In ad

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Cary, R. B., and M. W. Klymkowsky. "Differential organization of desmin and vimentin in muscle is due to differences in their head domains." Journal of Cell Biology 126, no. 2 (1994): 445–56. http://dx.doi.org/10.1083/jcb.126.2.445.

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In most myogenic systems, synthesis of the intermediate filament (IF) protein vimentin precedes the synthesis of the muscle-specific IF protein desmin. In the dorsal myotome of the Xenopus embryo, however, there is no preexisting vimentin filament system and desmin's initial organization is quite different from that seen in vimentin-containing myocytes (Cary and Klymkowsky, 1994. Differentiation. In press.). To determine whether the organization of IFs in the Xenopus myotome reflects features unique to Xenopus or is due to specific properties of desmin, we used the injection of plasmid DNA to

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Kim, Hugh, Fumihiko Nakamura, Wilson Lee, Yulia Shifrin, Pamela Arora, and Christopher A. McCulloch. "Filamin A is required for vimentin-mediated cell adhesion and spreading." American Journal of Physiology-Cell Physiology 298, no. 2 (2010): C221—C236. http://dx.doi.org/10.1152/ajpcell.00323.2009.

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Cell adhesion and spreading are regulated by complex interactions involving the cytoskeleton and extracellular matrix proteins. We examined the interaction of the intermediate filament protein vimentin with the actin cross-linking protein filamin A in regulation of spreading in HEK-293 and 3T3 cells. Filamin A and vimentin-expressing cells were well spread on collagen and exhibited numerous cell extensions enriched with filamin A and vimentin. By contrast, cells treated with small interfering RNA (siRNA) to knock down filamin A or vimentin were poorly spread; both of these cell populations exh

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Takai, Y., M. Ogawara, Y. Tomono, et al. "Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes." Journal of Cell Biology 133, no. 1 (1996): 141–49. http://dx.doi.org/10.1083/jcb.133.1.141.

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Using two types of anti-phosphopeptide antibodies which specifically recognize vimentin phosphorylated by protein kinase C (PKC) at two distinct PKC sites, we found that PKC acted as a mitotic vimentin kinase. Temporal change of vimentin phosphorylation by PKC differed form changes by cdc2 kinase. The mitosis-specific vimentin phosphorylation by PKC was dramatically enhanced by treatment with a PKC activator, 12-O-tetradecanoylphorbol-13-acetate (TPA), while no phosphorylation of vimentin by PKC was observed in interphase cells treated with TPA. By contrast, the disruption of subcellular compa

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Holwell, T. A., S. C. Schweitzer, and R. M. Evans. "Tetracycline regulated expression of vimentin in fibroblasts derived from vimentin null mice." Journal of Cell Science 110, no. 16 (1997): 1947–56. http://dx.doi.org/10.1242/jcs.110.16.1947.

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Fibroblast cell lines were derived from vim-/- mice that express a mouse vimentin transgene in a tetracycline regulatable manner. Vimentin null mouse primary embryo fibroblasts were transformed with SV-40 early genes and vim- cell lines were isolated. A vim- cell line was then serially transfected with an expression plasmid encoding the tetracycline regulatable transactivator (tTA) and a mouse vimentin cDNA expression plasmid under the regulation of Escherichia coli tet operator and minimal CMV promoter sequences. Two stable cell lines were obtained that contained little or no vimentin in the

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Hes, Ondrej, Michal Michal, Naoto Kuroda, et al. "Vimentin Reactivity in Renal Oncocytoma: Immunohistochemical Study of 234 Cases." Archives of Pathology & Laboratory Medicine 131, no. 12 (2007): 1782–88. http://dx.doi.org/10.5858/2007-131-1782-vriroi.

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Abstract Context.—The expression of vimentin in benign renal oncocytomas has been controversal. However, this is of clinical significance because immunostains may be used in differential diagnosis of renal tumors on limited biopsy specimens. Using different staining and analysis methods, we studied vimentin immunoreactivity in a large series of renal oncocytomas with a special emphasis on the immunoreactivity patterns. Objective.—Immunohistochemical expression of vimentin has been used in the differential diagnosis of renal epithelial neoplasms. Although typically expressed in most renal cell

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Vilalta, P. M., L. Zhang, and S. F. Hamm-Alvarez. "A novel taxol-induced vimentin phosphorylation and stabilization revealed by studies on stable microtubules and vimentin intermediate filaments." Journal of Cell Science 111, no. 13 (1998): 1841–52. http://dx.doi.org/10.1242/jcs.111.13.1841.

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To understand how protein phosphorylation modulates cytoskeletal organization, we used immunofluorescence microscopy to examine the effects of okadaic acid, a serine/threonine protein phosphatase inhibitor, and taxol, a microtubule-stabilizing agent, on stable (acetylated and detyrosinated) microtubules, vimentin intermediate filaments and other cytoskeletal elements in CV-1 cells. Okadaic acid caused major changes in both stable microtubules and vimentin intermediate filaments, but through independent mechanisms. At 300 nM, okadaic acid caused apparent fragmentation and loss of stable microtu

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Turowski, Patric, Timothy Myles, Brian A. Hemmings, Anne Fernandez, and Ned J. C. Lamb. "Vimentin Dephosphorylation by Protein Phosphatase 2A Is Modulated by the Targeting Subunit B55." Molecular Biology of the Cell 10, no. 6 (1999): 1997–2015. http://dx.doi.org/10.1091/mbc.10.6.1997.

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The intermediate filament protein vimentin is a major phosphoprotein in mammalian fibroblasts, and reversible phosphorylation plays a key role in its dynamic rearrangement. Selective inhibition of type 2A but not type 1 protein phosphatases led to hyperphosphorylation and concomitant disassembly of vimentin, characterized by a collapse into bundles around the nucleus. We have analyzed the potential role of one of the major protein phosphatase 2A (PP2A) regulatory subunits, B55, in vimentin dephosphorylation. In mammalian fibroblasts, B55 protein was distributed ubiquitously throughout the cyto

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TANG, Dale D., Ying BAI, and Susan J. GUNST. "Silencing of p21-activated kinase attenuates vimentin phosphorylation on Ser-56 and reorientation of the vimentin network during stimulation of smooth muscle cells by 5-hydroxytryptamine." Biochemical Journal 388, no. 3 (2005): 773–83. http://dx.doi.org/10.1042/bj20050065.

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Vimentin intermediate filaments undergo spatial reorganization in endothelial cells and fibroblasts in response to stimulation with platelet-derived growth factor and epidermal growth factor. In the present study, the vimentin network exhibited a curved filamentous structure in unstimulated smooth muscle cells. Vimentin filaments became straight and were arranged along the long axis of cells upon stimulation with 5-hydroxytryptamine (5-HT; serotonin). Stimulation of smooth muscle cells with 5-HT also induced phosphorylation of vimentin on Ser-56. Treatment of cells with small interfering RNA s

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Wang, Pei-Wen, Tung-Ho Wu, Tung-Yi Lin, Mu-Hong Chen, Chau-Ting Yeh, and Tai-Long Pan. "Characterization of the Roles of Vimentin in Regulating the Proliferation and Migration of HSCs during Hepatic Fibrogenesis." Cells 8, no. 10 (2019): 1184. http://dx.doi.org/10.3390/cells8101184.

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The activation of hepatic stellate cells (HSCs) manifested as proliferation and migration is the pivotal event involved in liver fibrogenesis. The vimentin network, an intermediate filament (IF) system, is one of the critical cascades by which the cell morphology, growth, and motility are modulated. However, the vimentin-mediated cytoskeletal cross talk, as well as the signaling transduction, which further coordinates the cellular responses during hepatic fibrogenesis, is poorly understood. In the current study, both messenger RNA (mRNA) and the vimentin protein were significantly increased in

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Battaglia, Rachel A., Samed Delic, Harald Herrmann, and Natasha T. Snider. "Vimentin on the move: new developments in cell migration." F1000Research 7 (November 15, 2018): 1796. http://dx.doi.org/10.12688/f1000research.15967.1.

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The vimentin gene (VIM) encodes one of the 71 human intermediate filament (IF) proteins, which are the building blocks of highly ordered, dynamic, and cell type-specific fiber networks. Vimentin is a multi-functional 466 amino acid protein with a high degree of evolutionary conservation among vertebrates. Vim−/− mice, though viable, exhibit systemic defects related to development and wound repair, which may have implications for understanding human disease pathogenesis. Vimentin IFs are required for the plasticity of mesenchymal cells under normal physiological conditions and for the migration

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Ramos, Irene, Konstantinos Stamatakis, Clara L. Oeste, and Dolores Pérez-Sala. "Vimentin as a Multifaceted Player and Potential Therapeutic Target in Viral Infections." International Journal of Molecular Sciences 21, no. 13 (2020): 4675. http://dx.doi.org/10.3390/ijms21134675.

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Vimentin is an intermediate filament protein that plays key roles in integration of cytoskeletal functions, and therefore in basic cellular processes such as cell division and migration. Consequently, vimentin has complex implications in pathophysiology. Vimentin is required for a proper immune response, but it can also act as an autoantigen in autoimmune diseases or as a damage signal. Although vimentin is a predominantly cytoplasmic protein, it can also appear at extracellular locations, either in a secreted form or at the surface of numerous cell types, often in relation to cell activation,

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Gilles, C., M. Polette, J. M. Zahm, et al. "Vimentin contributes to human mammary epithelial cell migration." Journal of Cell Science 112, no. 24 (1999): 4615–25. http://dx.doi.org/10.1242/jcs.112.24.4615.

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Vimentin expression in human mammary epithelial MCF10A cells was examined as a function of their migratory status using an in vitro wound-healing model. Analysis of the trajectories of the cells and their migratory speeds by time lapse-video microscopy revealed that vimentin mRNA and protein expression were exclusively induced in cells at the wound's edge which were actively migrating towards the center of the lesion. Actin labeling showed the reorganization of actin filaments in cells at the wound's edge which confirmed the migratory phenotype of this cell subpopulation. Moreover, the vimenti

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