The elimination of miR-23a in heat-stressed cells promotes NOXA-induced cell death and is prevented by HSP70.

ABSTRACT: Protein-damaging stress stimulates cell destruction through apoptosis; however, non-lethal proteotoxic stress induces an adaptive response leading to the increased synthesis of heat shock proteins, which inhibit apoptosis. In this study, we sought to determine the mechanism responsible for the accumulation of the BH3-only protein NOXA in heat-stressed cells and its prevention by the heat shock protein HSP70. Analysis of transcript levels by RT-qPCR revealed that miR-23a levels decreased in heat-stressed cells and that this was correlated with an increased abundance of NOXA mRNA, which contains a miR-23a binding site in its 3' untranslated region. Cells overexpressing HSP70 had higher levels of miR-23a, maintained these levels after heat shock and accumulated lower levels of NOXA mRNA and p

SUBMITTER: Roufayel R 

PROVIDER: S-EPMC4260742 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature