Proteomic analysis of human glioblastoma cell lines differently resistant to a nitric oxide releasing agent

NO exposure of two human high grade glioma cell lines (CCF-STTG1 and T98G) characterized by a different proteomic profile shows differential ceramide distribution and proliferation.

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Comparison of 99mTc-Tetrofosmin and 99mTc-Sestamibi Uptake in Glioma Cell Lines: The Role of P-Glycoprotein Expression

International Journal of Molecular Imaging ◽

10.1155/2014/471032 ◽

2014 ◽

Vol 2014 ◽

pp. 1-5 ◽

Cited By ~ 4

Author(s):

George A. Alexiou ◽

Xanthi Xourgia ◽

Evrysthenis Vartholomatos ◽

Spyridon Tsiouris ◽

John A. Kalef-Ezra ◽

...

Keyword(s):

Multidrug Resistance ◽

Cell Line ◽

Cell Lines ◽

Glioma Cell ◽

Tumor Imaging ◽

High Grade Glioma ◽

High Grade ◽

P Glycoprotein ◽

99Mtc Tetrofosmin ◽

Glioma Cell Lines

Tc-Tetrofosmin (Tc-TF) and Tc-Sestamibi (Tc-MIBI) are SPECT tracers that have been used for brain tumor imaging. Tumor’s multidrug resistance phenotype, namely, P-glycoprotein (p-gp), and the multidrug resistance related proteins (MRPs) expression have been suggested to influence both tracers’ uptake. In the present study we set out to compare Tc-MIBI uptake in high-grade glioma cell lines and to investigate the influence of gliomas p-gp expression on both tracers’ uptake. We used four glioma cell lines (U251MG, A172, U87MG, and T98G). The expression of p-gp protein was evaluated by flow cytometry. Twenty μCi (7.4·105 Bq) of Tc-TF and Tc-MIBI were used. The radioactivity in the cellular lysate was measured with a dose calibrator. P-gp was significantly expressed only in the U251MG cell line (). In all gliomas cell lines (U251MG, U87MG, A172, and T98G) the Tc-TF uptake was significantly higher than Tc-sestamibi. The U251MG cell line, in which significant p-gp expression was documented, exhibited the strongest uptake difference. Tc-TF uptake was higher than Tc-MIBI in all studied high-grade glioma cell lines. Thus, Tc-TF may be superior to Tc-MIBI for glioma imaging in vivo.

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Dianthin-30 or gelonin versus monomethyl auristatin E, each configured with an anti-calcitonin receptor antibody, are differentially potent in vitro in high-grade glioma cell lines derived from glioblastoma

Cancer Immunology Immunotherapy ◽

10.1007/s00262-017-2013-z ◽

2017 ◽

Vol 66 (9) ◽

pp. 1217-1228 ◽

Cited By ~ 8

Author(s):

Roger Gilabert-Oriol ◽

Sebastian G. B. Furness ◽

Brett W. Stringer ◽

Alexander Weng ◽

Hendrik Fuchs ◽

...

Keyword(s):

Cell Lines ◽

Glioma Cell ◽

High Grade Glioma ◽

High Grade ◽

Calcitonin Receptor ◽

Receptor Antibody ◽

Glioma Cell Lines

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Correction: EGFRvIII Deletion Mutations in Pediatric High-Grade Glioma and Response to Targeted Therapy in Pediatric Glioma Cell Lines

Clinical Cancer Research ◽

10.1158/1078-0432.ccr-09-2835 ◽

2009 ◽

Vol 15 (22) ◽

pp. 7110.1-7110

Keyword(s):

Targeted Therapy ◽

Cell Lines ◽

Glioma Cell ◽

High Grade Glioma ◽

High Grade ◽

Pediatric Glioma ◽

Deletion Mutations ◽

Glioma Cell Lines ◽

Pediatric High Grade Glioma

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EGFRvIII Deletion Mutations in Pediatric High-Grade Glioma and Response to Targeted Therapy in Pediatric Glioma Cell Lines

Clinical Cancer Research ◽

10.1158/1078-0432.ccr-08-3210 ◽

2009 ◽

Vol 15 (18) ◽

pp. 5753-5761 ◽

Cited By ~ 59

Author(s):

Dorine A. Bax ◽

Nathalie Gaspar ◽

Suzanne E. Little ◽

Lynley Marshall ◽

Lara Perryman ◽

...

Keyword(s):

Targeted Therapy ◽

Cell Lines ◽

Glioma Cell ◽

High Grade Glioma ◽

High Grade ◽

Pediatric Glioma ◽

Deletion Mutations ◽

Glioma Cell Lines ◽

Pediatric High Grade Glioma

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Development of barcode and proteome profiling of glioblastoma

Biomeditsinskaya Khimiya ◽

10.18097/pbmc20146003308 ◽

2014 ◽

Vol 60 (3) ◽

pp. 308-321 ◽

Cited By ~ 4

Author(s):

S.N. Naryzhny ◽

N.L. Ronzhina ◽

M.A. Mainskova ◽

N.V. Belyakova ◽

R.A. Pantina ◽

...

Keyword(s):

Mass Spectrometry ◽

Brain Tumor ◽

Cell Lines ◽

High Grade Glioma ◽

Initial Step ◽

High Grade ◽

Glioblastoma Cell ◽

Cancer Death ◽

Annexin 1 ◽

Glioblastoma Cell Lines

High grade glioma (glioblastoma) is the most common brain tumor. Its malignancy makes it the fourth biggest cause of cancer death. In our experiments we used several glioblastoma cell lines generated in our laboratory to obtain proteomics information specific for this disease. This study starts our developing the complete 2DE map of glioblastoma proteins. 2DE separation with following imaging, immunochemistry, spot picking, and mass-spectrometry allowed us detecting and identifying more than 100 proteins. Several of them have prominent differences in their level between norm and cancer. Among them are alpha-enolase (ENOA_HUMAN), pyruvate kinase isozymes M1/M2 (KPYM_HUMAN), cofilin 1 (COF1_HUMAN), translationally-controlled tumor protein TCTP_HUMAN, annexin 1 (ANXA1_HUMAN), PCNA (PCNA_HUMAN), p53 (TP53_HUMAN) and others. Most interesting results were obtained with protein p53. In all glioblastoma cell lines, its level was dramatically up regulated and enriched by multiple additional isoforms. This distribution is well correlated with presence of these proteins inside of cells themselves. At this initial step we suggest the panel of specific brain tumor markers (signature) to help creating noninvasive techniques to diagnose disease. These preliminary data point to these proteins as promising markers of glioblastoma.

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