Figure 5From: Targeted inhibition of heat shock protein 90 disrupts multiple oncogenic signaling pathways, thus inducing cell cycle arrest and programmed cell death in human urinary bladder cancer cell linesHsp90 harm after exposure of bladder cancer cells to geldanamycin. Western blottings (upper left panel) of critical members of the eukaryotic chaperosome (Hsp90 and Hsp70) after 24-hour geldanamycin administration in RT4 and T24 bladder cancer cells. A cell line-specific Hsp90 proteolytic processing is observed, as documented by the production of a ~65 kDa Hsp90-like protein fragment. Detection of Hsp90α and Hsp90β mRNA levels via sqRT-PCR (lower left panel), proving the absence of Hsp90 transcriptional regulation in response to the drug. Right panel: protein (top and middle) and RNA transcript (bottom) densitometric quantification bars, denoting the drug-induced alterations of Hsp90/Hsp70/α-Tubulin and Hsp90α/Hsp90β expression levels compared to control conditions, using Actin (upper left panel) and GAPDH (lower left panel) as protein and gene of reference, respectively. Western blotting and sqRT-PCR experiments were executed three times, with a respective characteristic image collection presented here. Standard deviation values are depicted as error bars on top of each value.Back to article page