The Aurora Kinases Inhibitor VE-465 is a Novel Treatment for Glioblastoma Multiforme
Resource
Oncology, 84(6), 326-335
Journal
Oncology
Pages
326-335
Date Issued
2013
Date
2013
Author(s)
Abstract
Glioblastoma multiforme (GBM) is one of the most common and aggressive types of primary brain tumor. After complete surgical resection combined with radiation and chemotherapy, approximately 10% of patients survive for more than 5 years. Therefore, a novel therapy for GBM is needed. Aurora-A (AURKA) plays important roles in cell cycle regulation, such as centrosome maturation, chromatic separation, bipolar spindle assembly, and mitotic entry. To investigate the effects of AURKA inhibition, three GBM cell lines, including GBM 8401, GBM 8901, and U87-MG cells, were treated with the AURKA inhibitor VE-465. Sensitivities to VE-465, as indicated by 50% inhibitory concentration values for GBM 8401, GBM 8901, and U87-MG cells, were 6, 25, and 19 nM, respectively. Additionally, colony formation of GBM 8401 and GBM 8901 cells was decreased after treatment with the VE-465. VE-465 treatment increased polyploidy and p53 protein expression, and inhibited cell growth in a caspase-independent manner. Taken together, these results suggest that the inhibition of AURKA by a small-molecule inhibitor may have potential to serve as a novel therapeutic approach for GBM. Copyright (c) 2013 S. Karger AG, Basel
Subjects
Glioblastoma multiforme
VE-465
Brain tumor
SDGs
Other Subjects
antineoplastic agent; aurora kinase; aurora kinase inhibitor; caspase 3; caspase 8; caspase 9; protein p53; unclassified drug; ve 465; antineoplastic activity; Article; breast carcinoma; cancer inhibition; cell cycle progression; cell division; cell fractionation; cell growth; cell shape; cell survival; cell viability; colony formation; concentration (parameters); controlled study; cytotoxicity; down regulation; drug exposure; drug sensitivity; endoreduplication; enzyme activation; enzyme activity; enzyme inhibition; glioblastoma; growth inhibition; human; human cell; IC50; in vitro study; priority journal; protein expression; protein phosphorylation; protein protein interaction; signal transduction; upregulation
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