ver-155008 and Urinary-Bladder-Neoplasms
ver-155008 has been researched along with Urinary-Bladder-Neoplasms* in 2 studies
Other Studies
2 other study(ies) available for ver-155008 and Urinary-Bladder-Neoplasms
Article | Year |
---|---|
Drug-induced keratin 9 interaction with Hsp70 in bladder cancer cells.
A pull-down experiment (co-immunoprecipitation) was performed on a T24 human bladder cancer cell lysate treated with the Hsp inhibitor VER155008 using an Hsp70 antibody attached to Dynabeads. Keratin 9, a cytoskeleton intermediate filament protein, was identified by LC MS/MS analysis. This novel finding was confirmed by Western blotting, RT-PCR, and immunocytochemistry. Other members of the keratin family of proteins have been shown to be involved in cancer progression, most recently identified to be associated with cell invasion and metastasis. The specific role of keratin 9 expression in these cells is yet to be determined. Topics: Cell Line, Tumor; Chromatography, Liquid; HSP70 Heat-Shock Proteins; Humans; Immunoprecipitation; Keratin-9; Purine Nucleosides; Tandem Mass Spectrometry; Urinary Bladder Neoplasms | 2018 |
Combined inhibition of heat shock proteins 90 and 70 leads to simultaneous degradation of the oncogenic signaling proteins involved in muscle invasive bladder cancer.
Heat shock protein 90 (HSP90) plays a critical role in the survival of cancer cells including muscle invasive bladder cancer (MIBC). The addiction of tumor cells to HSP90 has promoted the development of numerous HSP90 inhibitors and their use in clinical trials. This study evaluated the role of inhibiting HSP90 using STA9090 (STA) alone or in combination with the HSP70 inhibitor VER155008 (VER) in several human MIBC cell lines. While both STA and VER inhibited MIBC cell growth and migration and promoted apoptosis, combination therapy was more effective. Therefore, the signaling pathways involved in MIBC were systematically interrogated following STA and/or VER treatments. STA and not VER reduced the expression of proteins in the p53/Rb, PI3K and SWI/SWF pathways. Interestingly, STA was not as effective as VER or combination therapy in degrading proteins involved in the histone modification pathway such as KDM6A (demethylase) and EP300 (acetyltransferase) as predicted by The Cancer Genome Atlas (TCGA) data. This data suggests that dual HSP90 and HSP70 inhibition can simultaneously disrupt the key signaling pathways in MIBC. Topics: Apoptosis; Blotting, Western; Cell Line, Tumor; Cell Movement; Cell Proliferation; Cell Survival; Drug Synergism; HSP70 Heat-Shock Proteins; HSP90 Heat-Shock Proteins; Humans; Muscles; Neoplasm Invasiveness; Phosphatidylinositol 3-Kinases; Proto-Oncogene Proteins; Purine Nucleosides; Retinoblastoma Protein; Signal Transduction; Triazoles; Tumor Suppressor Protein p53; Urinary Bladder Neoplasms | 2015 |