The aberrant overexpression of vimentin is linked to a more aggressive status in tumours of the gastrointestinal tract

Brzozowa, Marlena; Wyrobiec, Grzegorz; Kołodziej, Izabela; Sitarski, Mateusz; Matysiak, Natalia; Reichman-Warmusz, Edyta; Żaba, Małgorzata; Wojnicz, Romuald

doi:10.5114/pg.2014.47502

Cited by 14 publications

(14 citation statements)

References 32 publications

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“…We examined the expression levels of vimentin and USP14 in our GC sample cohorts by RT-qPCR and found higher expression levels in cancer compared with the paired adjacent normal tissues (Figures 1A and 5A ). The GC cells yielded similar results (Figure 1B and Figure S2E ), which were consistent with previous studies [ 4 , 21 , 22 , 29 – 33 ]. The correlation analysis between USP14 and vimentin in GC tissues revealed their positive correlations (Figure 5B ).…”

Section: Resultssupporting

confidence: 92%

“…Large quantities of evidence have shown that vimentin is upregulated in GC tissues [ 4 ], but the underlying mechanism of its upregulation is still unclear. The following factors were confirmed to modulate vimentin expression: (1) non-coding RNA in the regulation of transcription, such as miR-135a, miR-137, miR-200c, miR-141, miR-122 and long non-coding RNA [ 5 – 11 ]; (2) protein modification, such as phosphorylation and acetylation [ 12 – 15 ].…”

Section: Introductionmentioning

confidence: 99%

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USP14 de-ubiquitinates vimentin and miR-320a modulates USP14 and vimentin to contribute to malignancy in gastric cancer cells

et al. 2016

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Vimentin plays important roles in the epithelial-to-mesenchymal transition (EMT). In this study, we found that vimentin was highly expressed in human gastric cancer (GC) tissues and cell lines and significantly promoted cell growth, migration and invasion. Ubiquitin-specific protease 14 (USP14) interacted with the vimentin protein, which led to its de-ubiquitination. miR-320a was found to bind to the 3′UTR of both vimentin and USP14 transcripts and downregulate the expression of both proteins. The downregulation of miR-320a upregulates vimentin expression by directly binding to the 3′UTR of vimentin to derepress expression and indirectly by augmenting USP14 to increase vimentin stability in GC cells. Taken together, these results provide new insight into malignancy in gastric cancers.

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Section: Resultssupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

USP14 de-ubiquitinates vimentin and miR-320a modulates USP14 and vimentin to contribute to malignancy in gastric cancer cells

et al. 2016

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“…The contraction of myosin, the polymerization of actin, and cell adhesion could all affect cell migration (Head et al, 2014;Kevenaar and Hoogenraad, 2015). The intermediate filaments in the cytoskeletal structures play an important role in the maintenance and regulation of cell function, such as cell contraction, migration, proliferation, gene expression, and apoptosis (Eriksson et al, 2004;Xu and Yan, 2009;Brzozowa et al, 2015). Regarding cytoskeleton-associated proteins, Krause's review concludes that the VASP protein is a regulators of the actin cytoskeleton and cell migration (Krause et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

Protein phosphatase 2A inhibition and subsequent cytoskeleton reorganization contributes to cell migration caused by microcystin-LR in human laryngeal epithelial cells (Hep-2)

et al. 2016

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The major toxic mechanism of Microcystin-LR is inhibition of the activity of protein phosphatase 2A (PP2A), resulting in a series of cytotoxic effects. Our previous studies have demonstrated that microcystin-LR (MCLR) induced very different molecular effects in normal cells and the tumor cell line SMMC7721. To further explore the MCLR toxicity mechanism in tumor cells, human laryngeal epithelial cells (Hep-2) was examined in this study. Western blot, immunofluorescence, immunoprecipitation, and transwell migration assay were used to detect the effects of MCLR on PP2A activity, PP2A substrates, cytoskeleton, and cell migration. The results showed that the protein level of PP2A subunits and the posttranslational modification of the catalytic subunit were altered and that the binding of the AC core enzyme as well as the binding of PP2A/C and α4, was also affected. As PP2A substrates, the phosphorylation of MAPK pathway members, p38, ERK1/2, and the cytoskeleton-associated proteins, Hsp27, VASP, Tau, and Ezrin were increased. Furthermore, MCLR induced reorganization of the cytoskeleton and promoted cell migration. Taken together, direct covalent binding to PP2A/C, alteration of the protein levels and posttranslational modification, as well as the binding of subunits, are the main pattern for the effects of MCLR on PP2A in Hep-2. A dose-dependent change in p-Tau and p-Ezrin due to PP2A inhibition may contribute to the changes in the cytoskeleton and be related to the cell migration in Hep-2. Our data provide a comprehensive exposition of the MCLR mechanism on tumor cells. © 2016 Wiley Periodicals, Inc. Environ Toxicol 32: 890-903, 2017.

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“…The intermediate filament protein vimentin is the major cytoskeletal protein in mesenchymal cells and has become one of the most widely used markers of EMT 21 correlating with the relatively aggressive proliferative and migratory activity of cells during embryogenesis and cancer metastasis. [36][37][38]79,[108][109][110] In the absence of vimentin, migration is significantly reduced. 39 Thus the E-cadherin/vimentin ratio determines the switch from low to high invasion capacity.…”

Section: Vimentinmentioning

confidence: 99%

“…35 Vimentin is a microtubular component involved in the regulation of cytoskeletal function relevant to the changes in intercellular adhesion and EMT. [36][37][38][39] The expression of vimentin is increased as cells lose adherence and transition from a resting, epithelial phenotype to a migratory behaviour.…”

Section: Introductionmentioning

confidence: 99%

Serine protease modulation of Dependence Receptors and EMT protein expression

McNair

Forrest

Vincenten

et al. 2018

Cancer Biology & Therapy

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Expression of the tumour suppressor Deleted in Colorectal Cancer (DCC) and the related protein neogenin is reduced by the mammalian serine protease chymotrypsin or the bacterial serine protease subtilisin, with increased cell migration. The present work examines whether these actions are associated with changes in the expression of cadherins, β-catenin and vimentin, established markers of the Epithelial-Mesenchymal Transition (EMT) which has been linked with cell migration and tumour metastasis. The results confirm the depletion of DCC and neogenin and show that chymotrypsin and subtilisin also reduce expression of β-catenin in acutely prepared tissue sections but not in human mammary adenocarcinoma MCF-7 or MDA-MB-231 cells cultured in normal media, or primary normal human breast cells. A loss of β-catenin was also seen in low serum media but transfecting cells with a dcc-containing plasmid induced resistance. E-cadherin was not consistently affected but vimentin was induced by low serum-containing media and was increased by serine proteases in MCF-7 and MDA-MB-231 cells in parallel with increased wound closure. Vimentin might contribute to the promotion of cell migration. The results suggest that changes in EMT proteins depend on the cells or tissues concerned and do not parallel the expression of DCC and neogenin. The increased cell migration induced by serine proteases is not consistently associated with the expression of the EMT proteins implying either that the increased migration may be independent of EMT or supporting the view that EMT is not itself consistently related to migration. (241).

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The aberrant overexpression of vimentin is linked to a more aggressive status in tumours of the gastrointestinal tract

Cited by 14 publications

References 32 publications

USP14 de-ubiquitinates vimentin and miR-320a modulates USP14 and vimentin to contribute to malignancy in gastric cancer cells

USP14 de-ubiquitinates vimentin and miR-320a modulates USP14 and vimentin to contribute to malignancy in gastric cancer cells

Protein phosphatase 2A inhibition and subsequent cytoskeleton reorganization contributes to cell migration caused by microcystin-LR in human laryngeal epithelial cells (Hep-2)

Serine protease modulation of Dependence Receptors and EMT protein expression

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