In this study, we investigated the impact of Hsp70 protein expression, and its close family member, Hsc70, on breast cancer cell viability and on the activity of the Hsp90/Hsp70 chaperone complex, a complex whose activity is important for the survival of cancer cells and tumours.
HSP70-2 P1/P2, HSPA8 intronic 1541-1542delGT and HIF-1 alpha polymorphisms were not associated with breast cancer risk, as evidenced by the dose-response allele models.
CHIP/STUB1 ubiquitin ligase is a negative co-chaperone for HSP90/HSC70, and its expression is reduced or lost in several cancers, including breast cancer.