Vimentin affects the mobility and invasiveness of prostate cancer cells

Zhao, Yan; Yan, Quanmei; Long, Xing; Chen, Xinmin

doi:10.1002/cbf.1478

Cited by 102 publications

(92 citation statements)

References 30 publications

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“…Vimentin is a mammalian structural cytoskeletal protein constituting type III mesenchymal filaments, and its elevated and aberrant expression correlates well with up-regulated cell invasion or migration both in the embryo and in malignancy [21] . Several studies have shown that vimentin could affect the invasion and motility of prostate cancer cells and is a promising marker for predicting aggressive and metastatic prostate cancer [22][23] . Consistent with their highly metastatic features, ARCaP M cells display higher expression of vimentin and other mesenchymal markers [14] .…”

Section: Discussionmentioning

confidence: 99%

Silibinin inhibits prostate cancer invasion, motility and migration by suppressing vimentin and MMP-2 expression

Zeng

Zhu

et al. 2009

Acta Pharmacol Sin

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Aim: Silibinin is known to exert growth inhibition and cell death together with cell cycle arrest and apoptosis in human prostate cancer cells. Whether silibinin could inhibit the invasion, motility and migration of prostate cancer cells remains largely unknown. This study was designed to evaluate this efficacy and possible mechanisms using a novel highly bone metastatic ARCaP M cell model. Methods: Four prostate cancer cell lines, LNCaP, PC-3, DU145, and ARCaP M , were used in this study. These cells were treated with increasing concentrations of silibinin (50, 100, and 200 μmol/L) for different periods of time. After treatment, cell viabilities of four prostate cancer cells were compared by MTT assay. Alterations of ARCaP M cell invasion, motility and migration were assessed by cell invasion, motility and wound healing assays. The changes of vimentin expression were observed by Western blotting and immunofluorescence staining, and the expression of MMP-2, MMP-9, and uPA was analyzed by reverse transcription-polymerase chain reaction (RT-PCR). Results: ARCaP M cells showed less sensitivity to the growth inhibition of pharmacological doses of silibinin than LNCaP, PC-3, and DU145 cells. However, silibinin exerted significant dose-and time-dependent inhibitory effects on the invasion, motility and migration of ARCaP M cells. Furthermore, the expression of vimentin and MMP-2, but not MMP-9 or uPA, was down-regulated in a dose-and timedependent manner after treatment of silibinin. Conclusion: This study shows that silibinin could inhibit the invasion, motility and migration of ARCaP M cells via down-regulation of vimentin and MMP-2 and therefore may be a promising agent against prostate cancer bone metastasis.

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Section: Discussionmentioning

confidence: 99%

Silibinin inhibits prostate cancer invasion, motility and migration by suppressing vimentin and MMP-2 expression

Zeng

Zhu

et al. 2009

Acta Pharmacol Sin

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“…This correlation has been demonstrated in migrating epithelial MCF10A cells, where vimentin is transiently and exclusively expressed in actively migrating cells at the wound edge, where it positively regulates migration (Gilles et al, 1999). Furthermore, fibroblasts of vimentin null mice exhibited defective wound healing due to reduced cell migration (Eckes et al, 1998(Eckes et al, , 2000 and in a pathological context, expression of vimentin promoted cell migration and invasion in breast, colon and prostate carcinomas (McInroy and Määttä, 2007;Zhao et al, 2008). The function of vimentin in cell migration and adhesion has also been reported in the transendothelial adhesion and extravasation of leukocytes.…”

Section: Discussionmentioning

confidence: 99%

Vimentin Regulates Scribble Activity by Protecting It from Proteasomal Degradation

Phua

Humbert

Hunziker

2009

MBoC

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INTRODUCTIONCell polarization is characterized by the asymmetrical distribution of cellular components such as proteins, lipids, and organelles to particular regions within a cell. The establishment of apical-basal polarity in epithelial cells is among the best-studied models of cell polarization (reviewed in Yeaman et al., 1999). The generation of cellular asymmetry, however, is also observed during cell proliferation, migration, and cell-cell or cell-matrix interactions, among others. Accordingly, cell polarity can be classified into, apical-basal (exemplified by epithelia), anterior-posterior (observed for example during migration; reviewed in , and planar or tissue polarity (found in the cochlea or the fly wing; reviewed in Zallen, 2007). Importantly, deregulation of cell polarity plays a central role in human diseases, in particular cancer (Wodarz and Nathke, 2007).Three evolutionarily conserved complexes of interacting proteins, the Par/atypical protein kinase C (aPKC) (Par6, Baz, and aPKC; reviewed in Suzuki and Ohno, 2006), the Crumbs (Crb, Sdt, and PATJ; reviewed in Assémat et al., 2007), and the Scribble (Scrib, Discs large [Dlg], and Lethal giant larvae [Lgl]; reviewed in Humbert et al., 2006; complex coordinately regulate, in conjunction with reorganization of the cytoskeleton and directed vesicle trafficking, cell polarization. In apical-basal polarity, a current model proposes that the Par and Crb complexes provide apical specification, whereas the Scrib complex confers basal identity. Par/Crb and Scrib complexes then act to repress each other's activity on the apical or basal domain, respectively .In Drosophila epithelial cells, Scrib and Dlg localize to septate junctions and Lgl to cortical junctions. Loss of these three proteins affects adherens junctions (AJs) and results in a disruption of apical-basal polarity (reviewed in Bilder, 2003Bilder, , 2004. Several lines of evidence indicate that the Scrib complex also plays a role in regulating apical-basal polarization in vertebrates. Similar to Drosophila Lgl, the two mammalian homologues bind Par6/aPKC to suppress aPKC kinase activity and inhibit apical identity (Plant et al., 2003;Yamanaka et al., 2003). Phosphorylation of Lgl by aPKC in turn inhibits its basal activity in the apical domain (Yamanaka et al., 2003).Although the importance for Scrib and Dlg in the formation of septate junctions and AJ in flies and worms is well established (Woods et al., 1996;, their role in apical-basal polarization of mammalian epithelial cells is controversial. In one study, Dlg was required for proper AJ assembly (Laprise et al., 2004), whereas in another, E-cadherin-mediated adhesion was a requisite for recruitment of Scrib to the lateral membrane . Furthermore, silencing of Lgl2 (Yamanaka et al., 2006), but not Scrib (Qin et al., 2005;, was recently reported to affect apical-basal polarity of mammalian epithelial cells. These apparently conflicting observations may be partly reconciled by the type of extracellular matrix (e.g., matrigel or collagen I) used ...

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“…9 However, vimentin can also be expressed in epithelial cells undergoing epithelial-to-mesenchimal transition (EMT), 10 a reversible critical event in the progression toward cancer metastasis 11 characterized by reduced expression of epithelial markers such as E-cadherin and upregulation of mesenchymal markers such as N-cadherin and vimentin. 12,13 Accumulating evidences demonstrated that epithelial-mesenchymal transition has also been implicated in the onset of drug resistance and tumor relapses, representing an escape mechanism from apoptosis. 11 Vimentin expression is induced in invasive epithelial carcinoma cell lines [14][15][16] and is correlated with poor prognosis.…”

Section: Introductionmentioning

confidence: 99%

HIPK2 downregulates vimentin and inhibits breast cancer cell invasion

Nodale¹,

Sheffer

Jacob‐Hirsch

et al. 2012

Cancer Biology & Therapy

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Vimentin, a mesenchymal marker, is frequently overexpressed in epithelial carcinomas undergoing epithelial to mesenchymal transition (EMT), a condition correlated with invasiveness and poor prognosis. Therefore, vimentin is a potential molecular target for anticancer therapy. Emerging studies in experimental models underscore the functions of homeodomain-interacting protein kinase 2 (HIPK2) as potential oncosuppressor by acting as transcriptional corepressor or catalytic activator of molecules involved in apoptosis and response to antitumor drugs. However, an involvement of HIPK2 in limiting tumor invasion remains to be elucidated. This study, by starting with a microarray analysis, demonstrates that HIPK2 downregulates vimentin expression in invasive, vimentin-positive, MDA-MB-231 breast cancer cells and in the noninvasive MCF7 breast cancer cells subjected to chemical hypoxia, a drive for mesenchymal shift and tumor invasion. At functional level, vimentin downregulation by HIPK2 correlates with inhibition of breast tumor cell invasion. Together, these data show that vimentin is a novel target for HIPK2 repressor function and that HIPK2-mediated vimentin downregulation can contribute to inhibition of breast cancer cells invasion that might be applied in clinical therapy.

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Vimentin affects the mobility and invasiveness of prostate cancer cells

Cited by 102 publications

References 30 publications

Silibinin inhibits prostate cancer invasion, motility and migration by suppressing vimentin and MMP-2 expression

Silibinin inhibits prostate cancer invasion, motility and migration by suppressing vimentin and MMP-2 expression

Vimentin Regulates Scribble Activity by Protecting It from Proteasomal Degradation

HIPK2 downregulates vimentin and inhibits breast cancer cell invasion

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