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.
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.
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.
In both cases, mutation was coincident with allelic imbalance, suggesting that HSC70 is a target of somatic mutation and deletion in a fraction of breast carcinomas.