Screening for novel cytotoxic modulators of the stress response in triple-negative breast cancer cells
HSF1 is associated with aggressive breast cancers including the triple-negative subtype which lack hormone expressions and are common among black women. HSF1 is also considered the master transcriptional protein conferring protection on cells after a cellular insult. Some of the functions involve cell development, aging and glucose metabolism.
In response to heat or oxidative stress, HSF1 dissociates itself from hsp90, trimerizes and translocates to the nucleus. HSF1 binds to the DNA at the promoter site of its target genes and enhances the transcription of heat shock proteins (hsp27, hsp40, hsp70) which participate in refolding proteins, caspase activation to promote cell survival.
This study investigates the ability of novel agents to effectively modulate the cellular stress response by targeting HSF1 for remarkable therapeutic activities in TNBCs. Furthermore, the influence of these compounds on production of cancer stem cells will be elucidated.
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Last Modified: Thu, 15 Jun 2017 09:15:11 SAST