Changes in glial fibrillary acidic protein and karyotype during culturing of two cell lines established from human glioblastoma multiforme

Bocchini, V.; Casalone, Rosario; Collini, Paola; Rebel, G.; Curto, Francesco Lo

doi:10.1007/bf00318141

Cited by 71 publications

(57 citation statements)

References 13 publications

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“…Subcellular Distribution of S100B in GL15 Cells-GL15 glioma cells show two phenotypes, a fusiform one and a polygonal one (29) (Fig. 1A).…”

Section: Resultsmentioning

confidence: 99%

“…Silencing of S100B Results in Increased Formation of GFAP Filaments in GL15 Cells-GL15 cells show a mosaic distribution of GFAP filaments in accordance with their dedifferentiated phenotype (29). Appearance of GFAP filaments is a sign of astrocyte differentiation (56 -58).…”

Section: Silencing Of S100b In Gl15 Cells Results In Moderately Reducedmentioning

confidence: 99%

“…To obtain information about the role of intracellular S100B in astrocyte development, activation, and neoplastic transformation, we analyzed effects of S100B silencing in the astrocytoma cell line GL15 (29) and the retinal Müller cell line, MIO-M1 (30). We found that inhibition of S100B expression in GL15 cells by small interference RNA (siRNA) techniques resulted in stress fiber disassembly, acquisition of a stellate morphology, reduced migration and, to a lesser extent, proliferation, and GFAP filament formation and that these effects were dependent on reduced activity of the Src kinase/phosphatidylinositol 3-kinase (PI3K) module.…”

Section: S100b Is a Camentioning

confidence: 99%

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S100B Protein Regulates Astrocyte Shape and Migration via Interaction with Src Kinase

Brozzi¹,

Arcuri²,

Giambanco

et al. 2009

Journal of Biological Chemistry

137

109

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S100B is a Ca2؉ -binding protein of the EF-hand type that is abundantly expressed in astrocytes and has been implicated in the regulation of several intracellular activities, including proliferation and differentiation. We show here that reducing S100B levels in the astrocytoma cell line GL15 and the Müller cell line MIO-M1 by small interference RNA technique results in a rapid disassembly of stress fibers, collapse of F-actin onto the plasma membrane and reduced migration, and acquisition of a stellate shape. Also, S100B-silenced GL15 and MIO-M1 Müller cells show a higher abundance of glial fibrillary acidic protein filaments, which mark differentiated astrocytes, compared with control cells. These effects are dependent on reduced activation of the phosphatidylinositol 3-kinase (PI3K) downstream effectors, Akt and RhoA, and consequently elevated activity of GSK3␤ and Rac1 and decreased activity of the RhoAassociated kinase. Also, rat primary astrocytes transiently down-regulate S100B expression when exposed to the differentiating agent dibutyryl cyclic AMP and re-express S100B at later stages of dibutyryl cyclic AMP-induced differentiation. Moreover, reducing S100B levels results in a remarkably slow resumption of S100B expression, suggesting the S100B might regulate its own expression. Finally, we show that S100B interacts with Src kinase, thereby stimulating the PI3K/Akt and PI3K/RhoA pathways. These results suggest that S100B might contribute to reduce the differentiation potential of cells of the astrocytic lineage and participate in the astrocyte activation process in the case of brain insult and in invasive properties of glioma cells. S100B, a member of a multigenic family of Ca 2ϩ -binding protein of the EF-hand type, has been implicated in the regulation of both intracellular and extracellular activities (1-3). Within cells, S100B is found diffusely in the cytoplasm and associated with membranes and certain cytoskeleton elements. S100B has been implicated in the regulation of the state of assembly of microtubules and type III intermediate filaments, some enzyme activities, and cell proliferation. This last issue has attracted much attention because levels of S100B are high in certain cancer cells (1, 2, 4), and S100B has been proposed to contribute to tumorigenesis by inhibiting the function of the tumor suppressor protein p53 (5, 6) and to regulate cell proliferation and differentiation by stimulating the activity of the mitogenic kinases Ndr (7) and Akt (protein kinase B) (8).Astrocytes represent the brain cell type with the highest expression of S100B. Levels of S100B are augmented in astrogliosis, and several reports have associated the increased levels of S100B in astrocytes with the pathophysiology of degenerative and infectious/inflammatory brain disorders (1, 2, 9 -11). Moreover, the human S100B gene maps to chromosome 21.q22.3 (12), with consequent high S100B levels in Down syndrome. These observations led to the hypothesis that S100B might be involved in the pathogenesis and/or pathophysiology...

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“…Subcellular Distribution of S100B in GL15 Cells-GL15 glioma cells show two phenotypes, a fusiform one and a polygonal one (29) (Fig. 1A).…”

Section: Resultsmentioning

confidence: 99%

Section: Silencing Of S100b In Gl15 Cells Results In Moderately Reducedmentioning

confidence: 99%

Section: S100b Is a Camentioning

confidence: 99%

See 1 more Smart Citation

S100B Protein Regulates Astrocyte Shape and Migration via Interaction with Src Kinase

Brozzi¹,

Arcuri²,

Giambanco

et al. 2009

Journal of Biological Chemistry

137

109

View full text Add to dashboard Cite

show abstract

“…Two human glioblastoma cell lines were used: the GL15 cell line of clonal origin established by Bocchini et al 19,21 and the 8MG cell line recently characterised by Perzelova et al 20 GL15 and 8MG cell lines were obtained from frontal lobe tumour biopsies before any chemotherapy of 2 patients with glioblastoma multiforme, a 59-year-old man (GL15) and a 54-year-old women (8MG). These cell lines that were derived from human glioblastoma multiforme exhibited a similar morphology of flat polygonal cells.…”

Section: Human Glioblastoma Cell Linesmentioning

confidence: 99%

Molecular and functional MDR1‐Pgp and MRPs expression in human glioblastoma multiforme cell lines

Declèves

Fajac

Lehmann-Che

et al. 2002

Intl Journal of Cancer

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“…This minimum quantity of animals used in experimental protocols is according to the regulations established by the Ethical Committee for Animal Experimentation of the Federal University of Bahia. Further experiments were carried out using human glioblastoma GL-15 cell line of clonal origin, which has been previously established 15 . GL-15 cell cultures were prepared as described previously 16 .…”

Section: Glial Cell Culturesmentioning

confidence: 99%

Redox Properties of Ruthenium Complex With Catechol Are Involved in Toxicity to Glial Cells

C¹,

Vítor²,

Pereira³

et al. 2007

J. Chil. Chem. Soc.

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Since the biological activity of [Ru III (NH 3 ) 4 (catechol)] + has never been tested, its cytotoxicity to glial cells was assayed and correlated with its redox properties. Coordinated catechol oxidizes faster than catechol in the presence of oxygen, but controlled potential electrolysis showed that its oxidation involves only oneelectron. However, the oxidation of the free ligand by oxygen involves two electrons, which could generate more reactive oxygen species. Indeed, catechol was more cytotoxic than [Ru III (NH 3 ) 4 (catechol)] + complex to human glioblastoma GL-15 cells and also to rat astrocytes. [Ru III (NH 3 ) 4 (catechol)] + -induced cytotoxicity was related to the generation of reactive oxygen species and [Ru II (NH 3 ) 4 (quinone)] 2+ . However, other mechanisms should be involved since antioxidant enzymes and deferoxamine only partially protected GL-15 cells.

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Changes in glial fibrillary acidic protein and karyotype during culturing of two cell lines established from human glioblastoma multiforme

Cited by 71 publications

References 13 publications

S100B Protein Regulates Astrocyte Shape and Migration via Interaction with Src Kinase

S100B Protein Regulates Astrocyte Shape and Migration via Interaction with Src Kinase

Molecular and functional MDR1‐Pgp and MRPs expression in human glioblastoma multiforme cell lines

Redox Properties of Ruthenium Complex With Catechol Are Involved in Toxicity to Glial Cells

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