Growth and migration markers of rat C6 glioma cells identified by serial analysis of gene expression

Gunnersen, Jenny M.; Spirkoska, Violeta; Smith, Paul E.; Danks, Rachel; Tan, Seong‐Seng

doi:10.1002/1098-1136(200011)32:2<146::aid-glia40>3.0.co;2-3

Cited by 83 publications

(33 citation statements)

References 55 publications

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“…The presented data are in agreement with previously published results, which have shown over-expression of cofilin in the highly invasive C6 rat glioblastoma cell line and in cells derived from human breast cancer. 41–44 Furthermore, the decreased level of phosphorylated, inactive cofilin was reported for T-cell lymphoma, cervix carcinoma (HeLa), colon cancer (KM12), liver (HepG2), and kidney (COS1) cells. 44–46 Our results also show a similar correlation of cofilin expression and activation, i.e.…”

Section: Discussionmentioning

confidence: 90%

Subcellular distribution and expression of cofilin and ezrin in human colon adenocarcinoma cell lines with different metastatic potential

Nowak

Mazur²,

Popow-Woźniak³

et al. 2010

Eur J Histochem

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The dynamic reorganization of the actin cytoskeleton is regulated by a number of actin binding proteins (ABPs). Four human colon adenocarcinoma cell lines – parental and three selected sublines, which differ in motility and metastatic potential, were used to investigate the expression level and subcellular localization of selected ABPs. Our interest was focused on cofilin and ezrin. These proteins are essential for cell migration and adhesion. The data received for the three more motile adenocarcinoma sublines (EB3, 3LNLN, 5W) were compared with those obtained for the parental LS180 adenocarcinoma cells and fibroblastic NRK cells. Quantitative densitometric analysis and confocal fluorescence microscopy were used to examine the expression levels and subcellular distribution of the selected ABPs. Our data show distinct increase in the level of cofilin in adenocarcinoma cells accompanied by the reduction of inactive phosphorylated form of cofilin. In more motile cells, cofilin was accumulated at cellular periphery in co-localization with actin filaments. Furthemore, we indicated translocation of ezrin towards the cell periphery within more motile cells in comparison with NRK and parental adenocarcinoma cells.In summary, our data indicate the correlation between migration ability of selected human colon adenocarcinoma sublines and subcellular distribution as well as the level of cofilin and ezrin. Therefore these proteins might be essential for the higher migratory activity of invasive tumor cells.

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Section: Discussionmentioning

confidence: 90%

Subcellular distribution and expression of cofilin and ezrin in human colon adenocarcinoma cell lines with different metastatic potential

Nowak

Mazur²,

Popow-Woźniak³

et al. 2010

Eur J Histochem

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“…The spontaneous overexpression of cofilin has been detected in the invasive subpopulation of tumor cells in mammary tumors (Wang et al, 2004). Cofilin is overexpressed in the highly invasive C6 rat glioblastoma cell line (Gunnersen et al, 2000), and the amount of phosphorylated, inactive cofilin is decreased in cell lines derived from T lymphoma (Jurkat) and carcinomas from the cervix (HeLa), colon (KM12), liver (HepG2), and kidney (COS1; Nebl et al, 1996). These results suggest that cofilin activity enhances, but LIMK activity inhibits, cell motility and metastasis.…”

Section: Introductionmentioning

confidence: 99%

The activity status of cofilin is directly related to invasion, intravasation, and metastasis of mammary tumors

Wang¹,

Mouneimne²,

Sidani³

et al. 2006

The Journal of Cell Biology

239

143

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Understanding the mechanisms controlling cancer cell invasion and metastasis constitutes a fundamental step in setting new strategies for diagnosis, prognosis, and therapy of metastatic cancers. LIM kinase1 (LIMK1) is a member of a novel class of serine–threonine protein kinases. Cofilin, a LIMK1 substrate, is essential for the regulation of actin polymerization and depolymerization during cell migration. Previous studies have made opposite conclusions as to the role of LIMK1 in tumor cell motility and metastasis, claiming either an increase or decrease in cell motility and metastasis as a result of LIMK1 over expression (Zebda, N., O. Bernard, M. Bailly, S. Welti, D.S. Lawrence, and J.S. Condeelis. 2000. J. Cell Biol. 151:1119–1128; Davila, M., A.R. Frost, W.E. Grizzle, and R. Chakrabarti. 2003. J. Biol. Chem. 278:36868–36875; Yoshioka, K., V. Foletta, O. Bernard, and K. Itoh. 2003. Proc. Natl. Acad. Sci. USA. 100:7247–7252; Nishita, M., C. Tomizawa, M. Yamamoto, Y. Horita, K. Ohashi, and K. Mizuno. 2005. J. Cell Biol. 171:349–359). We resolve this paradox by showing that the effects of LIMK1 expression on migration, intravasation, and metastasis of cancer cells can be most simply explained by its regulation of the output of the cofilin pathway. LIMK1-mediated decreases or increases in the activity of the cofilin pathway are shown to cause proportional decreases or increases in motility, intravasation, and metastasis of tumor cells.

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“…32 In vitro , cell motility has been shown to be an key part of the invasive potential of glioma tumors; moreover, the locomotory habits of particular glioma cell lines derived from tumors has been shown to be stable, and unaffected by passage number 33. Cofilin is known to be overexpressed in glioma tumor cells, 34 and in several other tumor cell types 35,36. We found a decrease in the expression of cofilin in the A172r cells as shown in Table I.…”

Section: Resultsmentioning

confidence: 99%

Chemo-Resistant Protein Expression Pattern of Glioblastoma Cells (A172) to Perillyl Alcohol

Fischer

Carvalho²,

Fonseca³

et al. 2011

J. Proteome Res.

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Glioblastoma multiform (GBM) is by far the most malignant glioma. We have introduced a new treatment for GBMs that comprises the inhalation of a naturally occurring terpene with chemotherapeutic properties known as perillyl alcohol (POH). Clinical trial results on recurrent GBM patients showed that POH extends the average life by more than eight months, temporarily slows tumor growth, and in some cases even decreases tumor size. After approximately seven months the tumor continues to grow and leads to a dismal prognosis. To investigate how these tumors become resistant to POH we generated an A172 human glioblastoma cell culture tolerant to 0.06 mM of POH (A172r). We used Multidimensional Protein Identification Technology (MudPIT) to compare the protein expression profile of A172r cells to the established glioblastoma A172 cell line. Our results include a list of identified proteins unique to either the resistant or the non-resistant cell line. These proteins are related to cellular growth, negative apoptosis regulation, Ras pathway, and other key cellular functions that could be connected to the underlying mechanisms of resistance.

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Growth and migration markers of rat C6 glioma cells identified by serial analysis of gene expression

Cited by 83 publications

References 55 publications

Subcellular distribution and expression of cofilin and ezrin in human colon adenocarcinoma cell lines with different metastatic potential

Subcellular distribution and expression of cofilin and ezrin in human colon adenocarcinoma cell lines with different metastatic potential

The activity status of cofilin is directly related to invasion, intravasation, and metastasis of mammary tumors

Chemo-Resistant Protein Expression Pattern of Glioblastoma Cells (A172) to Perillyl Alcohol

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