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Academic literature on the topic 'Vimentin'

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Published: 4 June 2021
Last updated: 25 May 2024

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Journal articles on the topic "Vimentin"

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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 (November 15, 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 the endogenous keratin system (Klymkowsky, M. W., L. A. Maynell, and A. G. Polson. 1987. Development (Camb.). 100:543-557), which suggests that the same cellular factors are responsible for both. Before germinal vesicle breakdown, in the initial stage of oocyte maturation, large vimentin and keratin filament bundles appear in the animal hemisphere. As maturation proceeds, keratin filaments fragment into soluble oligomers (Klymkowsky, M. W., L. A. Maynell, and C. Nislow. 1991. J. Cell Biol. 114:787-797), while vimentin filaments remain intact and vimentin is hyperphosphorylated. To examine the role of MPF kinase in the M-phase reorganization of vimentin we deleted the conserved proline of vimentin's single MPF-kinase site; this mutation had no apparent effect on the prophase or M-phase behavior of vimentin. In contrast, deletion of amino acids 19-68 or 18-61 of the NH2-terminal "head" domain produced proteins that formed extended filaments in the animal hemisphere of the prophase oocyte. We suggest that the animal hemisphere cortex of the prophase oocyte contains a factor that actively suppresses the formation of extended vimentin filaments through a direct interaction with vimentin's head domain. During maturation this "suppressor of extended filaments" appears to be inactivated, leading to the formation of an extended vimentin filament system.
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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 (January 22, 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 real-time polymerase chain reaction. IMH data showed that the high vimentin expression was localized in the middle of seminiferous tubules, and low expression was in the basal membrane. ICC analysis of the colonies by isolated differentiated spermatogonia indicated the positive expression for the vimentin antibody, but vimentin’s expression level in the undifferentiated population was negative under in vitro conditions. Fluidigm real-time PCR analysis showed significant vimentin expression in differentiated spermatogonia compared to undifferentiated spermatogonia (p < 0.05). Our results showed that vimentin is upregulated in the differentiation stages of spermatogenesis, proving that vimentin is an intermediate filament with crucial roles in the differentiation stages of testicular germ cells. These results support the advanced investigations of the spermatogenic process, both in vitro and in vivo.
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Kohl, Tobias, Melanie von Brandenstein, Andreas Stog, Monika Schlosser, Timur H. Kuru, David Pfister, Jochen Fries, and Axel Heidenreich. "Vimentin 3 and endothelin in prostate cancer." Journal of Clinical Oncology 36, no. 6_suppl (February 20, 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 ET-1 with and without artificial downregulation of the ETAR, the ETBR or both receptors. A scratch assay was performed to demonstrate the influence of ET-1. Proteins were then extracted and WB for vimentin full length and vimentin 3 was performed. Additionally we analyzed ET-1 and vimentin 3 in serum from prostate cancer patients using ELISA and we did IF and IHC staining for vimentin 3 in human prostate cancer tissue. Results: Treatment with ET-1 and downregulation of the ETBR lead to a significant increased migration of DU145 cells after 3 and 6 h. The corresponding WB showed increased vimentin 3. ELISA showed increased levels of ET-1 in samples of prostate cancer patients compared to patients with no cancer history. ELISA could also demonstrate elevated levels of vimentin 3 in serum of patients with local disease and significantly elevated values in metastatic prostate cancer patients compared to patients with no cancer history. Conclusions: The data presented shows that ET-1 stimulation leads to overexpression of vimentin 3 in prostate cancer cell cultures and a concomitant aggressive biological behavior. Here we previously described the direct interaction of Vimentin 3 in prostate cancer and the activation mechanism via ET-1 and the ETAR. IHC, IF show an upregulation of the truncated variant Vimentin3 in tissue samples. In an Vimentin 3 ELISA we could show that this truncated variant is increased and therefore represents a potential biomarker. Highest values of vimentin 3 were measured using ELISA in serum of patients with recurrent and metastatic disease also suggesting that vimentin 3 correlates with aggressive tumor behavior.
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Costigliola, Nancy, Liya Ding, Christoph J. Burckhardt, Sangyoon J. Han, Edgar Gutierrez, Andressa Mota, Alex Groisman, Timothy J. Mitchison, and Gaudenz Danuser. "Vimentin fibers orient traction stress." Proceedings of the National Academy of Sciences 114, no. 20 (May 2, 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 fluorescently labeled vimentin with an mEmerald tag using TALEN genome editing. We observed vimentin architecture in migrating human foreskin fibroblasts and found that network organization varied from long, linear bundles, or “fibers,” to shorter fragments with a mesh-like organization. We developed image analysis tools employing steerable filtering and iterative graph matching to characterize the fibers embedded in the surrounding mesh. Vimentin fibers were aligned with fibroblast branching and migration direction. The presence of the vimentin network was correlated with 10-fold slower local actin retrograde flow rates, as well as spatial homogenization of actin-based forces transmitted to the substrate. Vimentin fibers coaligned with and were required for the anisotropic orientation of traction stresses. These results indicate that the vimentin network acts as a load-bearing superstructure capable of integrating and reorienting actin-based forces. We propose that vimentin's role in cell motility is to govern the alignment of traction stresses that permit single-cell migration.
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Ivaska, Johanna. "Vimentin." Small GTPases 2, no. 1 (January 2011): 51–53. http://dx.doi.org/10.4161/sgtp.2.1.15114.

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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 (September 29, 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 sizes during cell spreading. Moreover, polo-like kinase 1 (Plk1) and vimentin phosphorylation at Ser-56 have been previously shown to affect focal adhesion assembly. Here, nestin KD reduced Plk1 phosphorylation at Thr-210 (an indication of Plk1 activation), vimentin phosphorylation at Ser-56, the contacts of vimentin filaments to paxillin, and the morphology of focal adhesions. Moreover, the expression of vimentin phosphorylation-mimic mutant S56D (aspartic acid substitution at Ser-56) rescued the migration, vimentin reorganization, and focal adhesion size of nestin KD cells. Together, our results suggest that nestin promotes smooth muscle cell migration. Mechanistically, nestin regulates Plk1 phosphorylation, which mediates vimenitn phosphorylation, the connection of vimentin filaments with paxillin, and focal adhesion assembly.
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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 (June 1, 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-tagged lamin tail domain localizes to the nucleus, indicating that the presence of the myc tag did not itself confer the ability to co-localize with actin (Hennekes and Nigg (1994) J. Cell Sci. 107, 1019–1029). Second, a myc-tagged polypeptide with a molecular mass and net charge at physiological pH (i.e. -4) similar to that of the mycVimTail polypeptide, failed to show any tendency to associate with actin-containing structures, indicating that the interaction between mycVimTail and actin-containing structures was not due to a simple ionic association. Franke (1987; Cell Biol. Int. Rep. 11, 831) noted a similarity in the primary sequence between the tail of the type I keratin DG81A and vimentin. To test whether the DG81A tail interacted with actin-containing structures, we constructed and purified myc-tagged DG81A tail polypeptides. Unexpectedly, these keratin tail polypeptides were largely insoluble under physiological conditions and formed aggregates at the site of injection. While this insolubility made it difficult to determine if they associated with actin-containing structures, it does provide direct evidence that the tails of vimentin and DG81A differ dramatically in their physical properties. Our data suggest that vimentin's tail domain has a highly extended structure, binds to actin-containing structures and may mediate the interaction between vimentin filaments and microfilaments involved in the control of vimentin filament organization (Hollenbeck et al. (1989) J. Cell Sci. 92, 621; Tint et al. (1991) J. Cell Sci. 98, 375).
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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 (January 25, 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 through the analysis of vimentin mRNA expression after 4-week treatment. Methods: Endoxifen, 100 nM or 1,000 nM, with or without beta-estradiol were given repeatedly to MCF-7 cells. Cells treated with dimethyl sulfoxide (DMSO) 0.001% were used as control. After 2- and 4-week exposure, the cells were counted, analyzed for mRNA vimentin expression, and observed for morphological changes. Results: Compared to control, there were significant decreases in vimentin mRNA expressions in endoxifen and endoxifen+β-estradiol treated cells after 2-weeks, which then significantly increased after 4-week compared with the 2-week exposure. We found no change in morphology of MCF-7 cells. Conclusion: Repeated exposure of endoxifen might induce EMT progression through increased expression of vimentin in MCF-7 breast cancer cell line.
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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 (November 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 levels increase significantly in differentiating transfected MEL cells, whereas similarly transfected hamster vimentin genes are negatively regulated. In conjunction with in vitro nuclear run-on transcription experiments, these results suggest that the difference in vimentin expression in avian and mammalian erythropoiesis is due to a divergence of cis-linked vimentin sequences that are responsible for transcriptional and posttranscriptional regulation of vimentin gene expression. Transfected chicken vimentin genes produce functional vimentin protein and stable vimentin filaments during MEL cell differentiation, further demonstrating that the accumulation of vimentin filaments is determined by the abundance of newly synthesized vimentin.
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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 (November 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 levels increase significantly in differentiating transfected MEL cells, whereas similarly transfected hamster vimentin genes are negatively regulated. In conjunction with in vitro nuclear run-on transcription experiments, these results suggest that the difference in vimentin expression in avian and mammalian erythropoiesis is due to a divergence of cis-linked vimentin sequences that are responsible for transcriptional and posttranscriptional regulation of vimentin gene expression. Transfected chicken vimentin genes produce functional vimentin protein and stable vimentin filaments during MEL cell differentiation, further demonstrating that the accumulation of vimentin filaments is determined by the abundance of newly synthesized vimentin.
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Dissertations / Theses on the topic "Vimentin"

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Besarani, Dler. "Anti-Vimentin Antibodies in Renal Transplantation." Thesis, Imperial College London, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.526360.

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Wong, Kai-lun, and 黃棨麟. "Nanomechanical studies of vimentin intermediate filaments." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2012. http://hub.hku.hk/bib/B49799617.

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Intermediate filaments, microtubules and microfilaments are the major components of the cytoskeleton. Though it is known that intermediate filaments play an important role in the mechanical behaviour of cells, it is surprising that their mechanical properties are far from being fully understood. The morphology and assembly process of the vimentin intermediate filaments (IFs) were studied using transmission electron microscopy (TEM) and atomic force spectroscopy (AFM). The width of the vimentin was found to change as the assembly proceeded. This finding agrees with the literature about the compaction process of vimentin IFs. The width of the IFs decreased gradually, while the range of width increased within the first few minutes after assembly initiation, and then decreased at last and became stable at 12.80±2.20nm. The average length of the IFs increased with decreasing rate. The length attained 485.60±162.23nm at 120 minutes. The range of length increased which revealed the assembly process was randomly occurring between filaments in the solution. The height of the IFs obtained with AFM did not show the periodicity in contrary to the literature. It may be due to the flattening of IFs on the functionalized mica(AP-mica) surface, or the periodicity was not prominent to be observed morphologically. In the force spectroscopy study, the nanomechanical properties of individual vimentin intermediate filaments were studied using AFM. Fresh vimentin intermediate filaments and samples fixed with glutaraldehydewere examined, and force-displacement curves with nano-scale resolutions of different vimentin intermediate filament samples were analysed. The use of glutaraldehydefixative provided cross-linking of the IF, and the structural change will result in differences in their force-displacement curves which helped to provide comparison with the non-fixed samples in order to identify the structure-mechanical property relationship. Statistical studies of these curves revealed that tearing off of protofilaments from the mature intermediate filaments (with and without glutaraldehyde) occurred inthe low force regime below 100pN, and successive tearing off events were observed readily below 25 nm separations, which were comparable with the lengths of domains of around 20 nm. Different features of sawtooth indicated the possibility of sliding mechanism in vimentin IF, and the sliding was found to occur at 30.44±13.41pN. Helical domain unfoldings were observed only in the non-fixed samples to start at 10.19±5.63pN on average witha mean increase of 42.12±26.74nm. This force agreed with the prediction of the extended Bell model described in the literature and the length increase was around double of the domain length, which indicated the uncoiling of the coiled-coils. The force-displacement curves also reveal different modes of failure of the vimentin intermediate filaments including protofilaments slippage/sliding and entropic elasticity. A new tearing off model was hence proposed based on different modes of failure and a previous model developed for desmin filaments reported in literature.
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Orthopaedics and Traumatology
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Carter, D. Vaughan. "The role of vimentin antibodies in transplantation." Thesis, University of Newcastle Upon Tyne, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.424154.

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Vechio, Aluana Maria da Costa Dal. "Expressão da vimentina em cultivo tridimensional de linhagens celulares derivadas de carcinoma epidermóide de boca." Universidade de São Paulo, 2008. http://www.teses.usp.br/teses/disponiveis/23/23141/tde-08042009-160336/.

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O carcinoma epidermóide representa mais de 90% das neoplasias malignas de cabeça e de pescoço, apresentando taxas elevadas de morbi-mortalidade. Proteínas relacionadas à invasão e proliferação celular estão em evidência devido ao seu envolvimento na carcinogênese, a exemplo da vimentina, encontrada em células de origem mesodérmica. Sua presença em células epiteliais neoplásicas contribui na transição epitélio mesenquimal e está associada à tumorigênese, à invasão celular e à metástase. O propósito deste estudo foi analisar através de métodos qualitativos (imunofluorescência e imunoistoquímica) e quantitativos (Western Blot) a expressão da vimentina em linhagens celulares de carcinoma epidermóide de cabeça e de pescoço (CECP) e em uma linhagem de queratinócitos imortalizados (HaCat) submetidas ao cultivo tridimensional em Matrigel®. O grupo controle foi representado pelas mesmas linhagens cultivadas na ausência de Matrigel®. A Vimentina apresentou marcação citoplasmática em algumas células das linhagens estudadas, exceto na HaCat, com evidente diminuição da sua expressão quando submetida ao cultivo com Matrigel®. Esses resultados foram confirmados por Western Blot. A expressão da Vimentina em diferentes linhagens de CECP pode variar dependendo da linhagem analisada, da reação de suas células aos componentes da matriz extracelular e da técnica utilizada para avaliação da expressão da proteína.
Head and neck squamous cell carcinoma (HNSCC) represents more than 90% of all head and neck malignancies, causing more deaths than any other oral disease. Proteins related to cancer growth, invasion and metastasis are in evidence due to their involvement in carcinogens, such as vimentin. This protein is observed in mesenquimal cells, however, it is considered a common finding in cervix, breast and bladder tumours. Thus its presencence in epithelial neoplasic cells contributes to epithelial-mesenchymal transition associated with tumorigenesis and tumor progression. The aim of this study was to analyse through Western Blot, Immunohistochemistry and Immunofluorescence methods, the expression of Vimentin in three different HNSCC cell lines and HaCat cell line (immortalized keratinocytes) submitted to a 3D assay into Matrigel®. The control group was represented by the same cell lines, without any treatment. Results showed that Vimentin had citoplasmatic staining in some cell of lines studied, except for HaCat cells, with evident decrease in its expression when submitted to cultive into Matrigel®. These findings were confirmed by Western Blot. Taking these results together, we conclude that in squamous cell carcinoma, the Vimentin is related to the process of tumour invasion and metastasis. This fact was showed by the reduction of its expression after treatment with Matrigel®. Therefore, the expression of Vimentin in different cell lines of HNSCC may vary according to the stimulus and, fundamentally, the localization of the tumor and the individual characteristics of neoplasic cells.
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Gianelo, Maikol Carlos Simões. "Estudo da resposta regenerativa do músculo sóleo de ratas bebês após procedimento de imobilização e reabilitação pelo alongamento." Universidade de São Paulo, 2014. http://www.teses.usp.br/teses/disponiveis/17/17152/tde-02072015-122858/.

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Modelos de desusos do músculo esquelético como imobilização gessada, suspensão são frequentemente utilizados em grupos de pesquisas experimentais. Esse tempo de desuso por período prolongado pode determinar alterações significativas na citoarquitetura muscular. Este estudo teve como objetivo avaliar os aspectos morfológicos do músculo sóleo de ratas em desenvolvimento pós-natal que tiveram seus membros posteriores direitos imobilizados, e posteriormente foram submetidas ao protocolo passivo de alongamento (alongamento manual passivo intermitente), por um período de sete dias. Utilizou-se 20 ratas da raça Wistar (Rattus Norvegicus Albinus) com 21 dias de idade, dividas em cinco grupos: Grupo Controle 21 dias (GC21- Animais com 21 dias), Grupo Imobilizado (GI- Animais de 21 dias que foram imobilizados por 7 dias), Grupo Imobilizado e Alongado (GIA- Animais de 21 dias que foram imobilizados por 7 e reabilitados pelo alongamento durante 3 dias) e Grupo Alongado (GA- Animais de 21 dias não imobilizados por 7 dias e posteriormente alongamentos durante 3 dias), Grupo Controle 30 (GC30 - Animais com 30 dias). Fragmentos dos músculo sóleo foi processado sob diferentes métodos histoquímicos, coloração hematoxilina-eosina e picro-sirius. As variáveis foram avaliadas inter- e intra-grupos através de técnicas estatísticas como: Teste de Kruskall Wallis e pós teste de Dunn. Conclusão: Os resultados indicaram que o músculo sóleo de ratas bebês sofreram modificações citoarquiteturais significativas quando o alongamento manual intermitente foi usado como recurso terapêutico após 7 dias de desuso do segmento posterior direito (imobilização em flexão plantar). Nos músculos imobilizados, ambas as proteínas (desmina e vimentina) tiveram seus conteúdos reduzidos em relação aos valores controle (21 ou 30 dias), indicando balanço negativo para o tecido pós-desuso. A quantidade dessas proteínas não foi modificada nos animais submetidos somente ao procedimento de alongamento intermitente. Os animais que sofreram imobilização e que foram reabilitados, a quantidade de desmina não aumentou significativamente, não atingindo valores similares ao grupo controle 30 dias. Esses dados sugerem que os filamentos de desmina necessitam de tempo superior a 3 dias de reabilitação por alongamento intermitente para restabelecerem a arquitetura intersticial das fibras e consequentemente favorecerem a transdução mecânica de sinais entre os meios intra e extracelular. Porém, o efeito citoarquitetural do alongamento sobre os filamentos intermediários deve ser acompanhado longitudinalmente e confirmados em adicionais estudos bioquímicos e moleculares.
Disuses models of skeletal muscle as immobilization , suspension are often used in experimental research groups. This time of disuse for a prolonged period can cause significant changes in muscle cytoarchitecture .This study aimed to evaluate the morphology of the soleus muscle of rats in postnatal development that had its members later immobilized rights, and subsequently were subjected to passive stretching protocol (passive manual stretching flashes), for a period of seven days. We used 20 Wistar rats (Rattus Norvegicus Albinos) race with 21 days of age , divided into five groups: Control Group (CG21- Animal 21 days ), Immobilized Group (IG- Animal 21 days that were immobilized for 7 days ) , Immobilized and Stretched Group (ISG - Animal 21 days that were immobilized for 7 and rehabilitated by stretching for 3 days) and Stretched Group (SG -Animal 21 days not immobilized for 7 days and subsequently stretching for 3 days), Control Group (CG30 - Animals 30 days).Fragments of the soleus muscle was processed under different histochemical methods, hematoxylin - eosin staining and picro-sirius. Variables were evaluated inter - and intra - groups through statistical techniques such as Kruskall Wallis and Dunn\'s post test . Conclusion: The results indicated that the soleus muscle of rats were babies citoarquiteturais significant changes when the manual stretching intermittently been used as a therapeutic resource after 7 days of disuse of the right posterior segment ( immobilization in plantar flexion). The immobilized muscles , both proteins (desmin and vimentin ) content had decreased compared to control values (21 or 30 days), indicating negative after- tissue balance disuse. The amount of these proteins was not modified in animals subjected only to intermittent stretching procedure. The animals underwent immobilization have been rehabilitated and that the amount of desmin was not significantly increased, not reaching values similar to the control group 30 days. These data suggest that desmin filaments need to 3 days longer than the time for rehabilitation to restore the intermittent stretching interstitial fiber architecture and hence favor the mechanical transduction of signals between intra-and extracellular media. However, the effect of stretching on cytoarchitectural intermediate filaments should be followed longitudinally and confirmed in additional biochemical and molecular studies .
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Pattabiraman, Sundararaghavan [Verfasser]. "Vimentin protects differentiating stem cells from stress / Sundararaghavan Pattabiraman." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2020. http://d-nb.info/1223171582/34.

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McGinn, Mary Catherine. "Interplay Between Keratin and Vimentin Expression in Oral Cancer." VCU Scholars Compass, 2010. http://scholarscompass.vcu.edu/etd/49.

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Previous research in our laboratory found that inhibiting expression of vimentin, a marker of epithelial-to mesenchymal transition, inhibited cell growth and motility in vitro and in vivo. Tumors derived from vimentin knockdown cells showed features of epithelial redifferentiation and increased expression of differentiation-specific keratins. It is unknown what causes re-expression of keratins when vimentin is inhibited. Although, canonical Wnt signaling may activate NF-κB and repress of keratin and/or induce vimentin expression through β-catenin. We hypothesize that downregulation of differentiation-specific keratins contributes to tumor progression, mediated directly or indirectly by expression of vimentin. Vimentin-negative HN4 cells were transfected with plasmids encoding wild-type, PKCε-phosphomimetic, or unphosphorylatable versions of vimentin. Expression of vimentin was confirmed by western blot and immunofluorescence. Effects on cell growth and motility were determined using MTT, cell proliferation, and wound-closure assays. These results indicate that mutation of vimentin PKCε-phosphorylation sites cause changes in proliferation and filament assembly. Treatment of cells with an NF-κB inhibitor or 5-Aza-C, which allows re-expression of the Wnt inhibitor DKK3, led to a decrease in proliferation. These results suggest that inhibiting Wnt signaling removes the inhibition on GSK-3β and prevents activation of NF-κB, which decreases proliferation.
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Kirmse, Robert. "Studium der Wachstumskinetik von Intermediärfilamenten mit Hilfe von Vimentin." [S.l. : s.n.], 2007. http://nbn-resolving.de/urn:nbn:de:bsz:16-opus-83413.

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Fay, Nikta. "Parvoviral interactions with the cytoskeleton : exposing vimentin – the forgotten player." Thesis, University of British Columbia, 2014. http://hdl.handle.net/2429/50672.

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There are three structurally and functionally distinct cytoskeleton components: actin filaments, microtubules, and intermediate filaments (IFs). Among the three cytoskeleton networks IFs are understudied; consequently, there is a lack of information about the role of IFs during early viral infection. IFs have long been known to serve structural functions within the cell, and recently, additional functions have been elucidated, including novel roles during infection by many viruses. During early infection with the parvovirus minute virus of mice (MVM), prior to viral replication, I have found that the virus induces dramatic morphological changes in mouse fibroblast cells. This observed change in the shape of infected cells may be a result of the virus using the host cytoskeleton to aid in the mechanism of intracellular trafficking. Thus, this thesis focuses on MVM and its effects on the cytoskeleton components, especially IFs, during infection. Using fluorescence microscopy techniques, I found that during early infection with MVM, after endosomal escape, the vimentin IF network was considerably altered, yielding collapsed immunofluorescence staining near the nuclear periphery. Furthermore, I found that vimentin plays an important role in the infection cycle of MVM. The number of cells successfully replicating MVM was reduced in infected cells in which the vimentin network was pharmacologically modified or in cells lacking a vimentin network; viral endocytosis, however, remained unaltered. Perinuclear accumulation of MVM-containing vesicles and progression of MVM through the endocytic pathway was reduced in cells lacking vimentin. Cells lacking vimentin, accumulated virions in early endosomes up to 2 h post-infection compared to wild type cells. Thus, my data supports a model where vimentin facilitates a productive MVM infection, presenting possibly a dual role: (1) during progression of MVM through the endocytic pathway and (2) following MVM escape from endosomes.
Science, Faculty of
Zoology, Department of
Graduate
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Rato, Leila Sofia Coelho. "Vimentin interacts with the Akt/mTOR pathway mediating cell growth." Master's thesis, Universidade de Aveiro, 2017. http://hdl.handle.net/10773/22372.

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Mestrado em Bioquímica - Bioquímica Clínica
A vimentina é uma proteína da classe III dos filamentos intermédios que promove processos tais como proliferação, migração e invasão celular através da interação com diferentes vias de sinalização. No entanto, o papel da vimentina no crescimento celular é ainda pouco conhecido. Neste estudo, observamos que fibroblastos isolados de embriões de ratinhos sem vimentina (Vim -/- MEFs) eram mais pequenos que o tipo normal (WT). Assim, o objetivo deste estudo era entender de que forma a vimentina regula o crescimento celular. Com recurso a modelos in vitro, técnicas de microscopia e técnicas bioquímicas descobrimos que Vim -/- MEFs tinham menor volume e concentração de proteínas quando comparadas com WT MEFs. Adicionalmente, a síntese proteica e ativação de mTORC1 estavam significativamente reduzidas em Vim -/- MEFs. Através de co-imunoprecipitação, descobrimos que a vimentina interage com os complexos mTORC2 e TSC. Assim, postulamos que a vimentina regula o crescimento celular por interação com proteínas da via de sinalização AKT/mTO
Vimentin is a type III intermediate filament protein that takes part in cell proliferation, migration and invasion, by acting as a signalling scaffold. The role of vimentin in cell growth, however, is poorly understood. We observed that vimentin knockout mouse embryonic fibroblasts (Vim -/- MEFs) were smaller than the wild type (WT). Therefore, this work aimed to understanding how vimentin regulates cell growth. Using in vitro models, imaging techniques and biochemical approaches, we have found that the volume and protein concentration of Vim -/- MEFs is lower when compared to WT MEFs. Further, protein synthesis and mammalian target of rapamycin complex 1 (mTORC1) activation was attenuated in Vim -/- MEFs. By co-immunoprecipitation we found that vimentin interacts with mammalian target of rapamycin complex 2 (mTORC2) and tuberous sclerosis protein complex (TSC) after insulin stimulation. Consequently, we postulate that vimentin regulates cell growth by interacting with proteins of the AKT/mTOR pathway
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Books on the topic "Vimentin"

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Mello, Ramon Andrade de. Vimentin Concepts and Molecular Mechanisms. Nova Science Publishers, Incorporated, 2013.

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Book chapters on the topic "Vimentin"

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Koch, Clarissa M., and Karen M. Ridge. "Vimentin." In Encyclopedia of Signaling Molecules, 5921–27. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101951.

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Holdenrieder, S., and P. Stieber. "Vimentin." In Springer Reference Medizin, 2450. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_3253.

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Holdenrieder, S., and P. Stieber. "Vimentin." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-49054-9_3253-1.

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Koch, Clarissa M., and Karen M. Ridge. "Vimentin." In Encyclopedia of Signaling Molecules, 1–7. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101951-1.

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Wang, Ning, and Dimitrijie Stamenovic. "Mechanics of vimentin intermediate filaments." In Mechanics of Elastic Biomolecules, 535–40. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-010-0147-2_13.

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Gierten, B. "Autoantikörper gegen mutiertes citrulliniertes Vimentin." In Springer Reference Medizin, 319. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_3698.

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Gierten, B. "Autoantikörper gegen mutiertes citrulliniertes Vimentin." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_3698-1.

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Leong, Anthony S.-Y. "The Expression of Vimentin in Epithelial Neoplasms." In Progress in Surgical Pathology, 31–48. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-662-09515-7_2.

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Schepers, Anna V., Julia Kraxner, Charlotta Lorenz, and Sarah Köster. "Mechanics of Single Vimentin Intermediate Filaments Under Load." In Optical Tweezers, 677–700. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2229-2_24.

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Quax, Wim, and Hans Bloemendal. "Organization and Expression of the Vimentin and Desmin Genes." In Cell and Molecular Biology of the Cytoskeleton, 109–30. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2151-4_5.

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Conference papers on the topic "Vimentin"

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Muszbek, L., R. Adåny, M. A. Glukhova, M. G. Frid, A. E. Kabakov, and V. E. Kot-e-liansky. "THE IDENTIFICATION OF VIMENTIN, AN INTERMEDIATE,FILAMENT SUBUNIT PROTEIN IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643900.

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In platelets the presence of basic subunit proteins of microtubules as well as microfilaments has been verified a long time ago and it was also shown that both of these cytoskeletal systems go through a tremendous reorganization during the activation process. Surprisingly, none of the components of intermediate filaments has so far been identified in these cells, perhaps because platelets were considered too motile to have intermediate filaments, the most static structures among the three major cytoskeletal systems. By using two different monoclonal antibodies (II C4 and II D8) here we attempted to establish if vimen-tin, an intermediate filament subunit protein present in most differentiating cells, in cells grown in tissue culture and in certain fully differentiated cells also exists in human platelets The IgM type antibodies were characterized by various immuno-morphological and immunobiochemical techniques. They labelled selectively colcemid-sensitive filamentous structures in fibroblasts, in endothelial cells and in vascular but not myometrium smooth muscle and were shown to be monospecific against epitopes on vimentin in fibroblast homogenate. When whole platelet homogenate was submitted to high resolution gradient SDS PAGE and then electroblotted to nitrocellulose sheet, both antibodies reacted with a single protein band of 55 kD that comigrated with fibroblast vimentin. By immunofluorescence microscopy an annular ring-like structure was stained for vimentin that suggests a membran skeletal role for this protein. During pseu-dopode formation a redistribution of vimentin could be observed. Parallel with the disappearance of ring-like structures vimentin appears in pseudopodia suggesting that like in the case of other filamentous systems platelet activation induces a structural reorganization of the intermediate filaments, as well.
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Schmidt, G., M. Kasoha, EF Solomayer, and R. Bohle. "Vimentin als Prognosefaktor beim triple negativen Mammakarzinom." In 38. Jahrestagung der Deutschen Gesellschaft für Senologie. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1651796.

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Raveendran, V. V., S. AlQattan, A. Alaiya, R. Abdulqawi, R. A. Saleh, S. F. Mohammed, F. A. Al-Mohanna, and E. A. Almutairy. "Interaction of S100A13 With Vimentin in Pulmonary Fibrosis." In American Thoracic Society 2023 International Conference, May 19-24, 2023 - Washington, DC. American Thoracic Society, 2023. http://dx.doi.org/10.1164/ajrccm-conference.2023.207.1_meetingabstracts.a2232.

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Buehler, Markus J., and Je´re´mie Bertaud. "Hierarchical Structure Controls Nanomechanical Properties of Vimentin Intermediate Filaments." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13103.

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Intermediate filaments (often abbreviated as IFs), in addition to microtubules and microfilaments, are one of the three major components of the cytoskeleton in eukaryotic cells (Figure 1). It has been suggested that intermediate filaments are crucial in defining key mechanical functions of cells such as cell migration, cell division and mechanotransduction, and have also been referred to as the “safety belts of cells” reflecting their role in preventing exceedingly large cell stretch [1, 2]. Vimentin is a specific type of this protein filament found in fibroblasts, leukocytes, and blood vessel endothelial cells, representing the most widely distributed type of intermediate filaments. Several diseases have been linked to the structure and density of intermediate filaments. Here we report a systematic study of the effects of intermediate filaments on cell mechanics, specifically focused on changes in the density of filaments. We compare the results with experimental studies in vimentin deficient cells, showing good qualitative agreement.
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Ackbarow, Theodor, and Markus J. Buehler. "Superelasticity of Vimentin Coiled-Coil Intermediate Filaments: Atomistic and Continuum Studies." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176471.

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Vimentin coiled-coil alpha-helical dimers are elementary protein building blocks of intermediate filaments (IFs), an important component of the cell’s cytoskeleton that has been shown to control the large-deformation behavior of eukaryotic cell [1].
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Thaiparambil, J., L. Bender, E. Kline, T. Ganesh, J. Snyder, D. Liotta, and A. Marcus. "Vimentin: A Novel Chemopreventive Target for Breast Cancer Metastasis." In Abstracts: Thirty-Second Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 10‐13, 2009; San Antonio, TX. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-09-5063.

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Buehler, Markus J., and Zhao Qin. "Hierarchical Structure Controls Nanomechanical Properties of Vimentin Intermediate Filaments." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13102.

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Intermediate filaments (IFs), in addition to microtubules and microfilaments, are one of the three major components of the cytoskeleton in eukaryotic cells, playing a vital role in mechanotransduction and in providing mechanical stability to cells (Figure 1) [1]. Despite the importance of IF mechanics for cell biology and cell mechanics, the structural basis for their mechanical properties remains unknown. Specifically, our understanding of fundamental filament properties, such as the basis for their great extensibility, stiffening properties, and their exceptional mechanical resilience remains limited. This has prevented us from answering fundamental structure-function relationship questions related to the biomechanical role of intermediate filaments, which is crucial to link structure and function in the protein material’s biological context.
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Zhu, Quansheng, Guy Lahat, Svetlana Bolshakov, Jeffery Liu, Keila Torres, Robert R. Langley, Alexander J. Lazar, Mien Chie Hung, and Dina Lev. "Abstract 642: Vimentin is a novel anticancer therapeutic target." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-642.

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Wang Xiao-Wu, Ding Gui-Rong, Zhao Tao, Zhang Ji, Xie Xue-Jun, Zeng Li-Hua, and Guo Gno-Zhen. "Effects of electromagnetic pulse on the vimentin of mice testes." In 4th International Symposium on Electromagnetic Compatibility 2007. IEEE, 2007. http://dx.doi.org/10.1109/elmagc.2007.4413530.

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Kayyali, Usamah S., Tiegang Liu, Oscar Guevara, and Nicholas S. Hill. "Role Of Vimentin Intermediate Filaments In Endothelial Permeability Barrier Regulation." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a4182.

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