Nov 9, 2018 · In the cytoplasm, HSP70 and HMGB1b synergistically enhanced ROS-induced autophagy. HSP70 also promoted HMGB1b–Beclin 1 association via direct interaction with Beclin 1. Our results highlight the antiviral role of ROS-induced autophagy in response to …

Correlation analysis revealed positive relationships between HSP70 levels and zymosan-stimulated ROS production in the elder group. This was consistent with a promoting role for HSP70 in ROS-associated neutrophils response to pathogens.

Because heat-shock proteins (HSPs) can protect cells from ROS, we investigated the effect of H (2)O (2) on HSP expression. H (2)O (2) stimulated HSP70 expression in a time-dependent manner, and AG-490 abolished H (2)O (2)-induced HSP70 expression.

Feb 28, 2022 · ROS can directly cause oxidative cysteine modifications of Hsp70 members to alter their structure and chaperone activity, resulting in changes in the interactions between Hsp70 and their clients or cochaperones, which can then transfer redox signals to Hsp70-related signaling pathways.

ROS not only directly oxidize cysteine thiols in Hsp70 proteins but also cause covalent modification by production of lipoperoxides, altering the structure and chaperone activity of Hsp70 and affecting related cellular processes.

May 28, 2024 · We found that HSP70 inhibition increased ROS levels (Supplementary Fig. 1A, B) and led to a dose-dependent increase in mROS in multiple PDAC cell lines tested (Fig. 1G, H).

Dec 15, 2014 · Correlation analysis revealed positive relationships between HSP70 levels and zymosan-stimulated ROS production in the elder group. This was consistent with a promoting role for HSP70 in ROS-associated neutrophils response to pathogens.

Feb 26, 2018 · Inhibition of HSP90 and HSP70 activity leads to ROS imbalance and autophagy in developing fibers. The HSPs are involved in cellular homeostasis during stress and rapid growth.

Jun 12, 2018 · The mechanisms by which PLY disrupts the pulmonary endothelial barrier are not fully understood. Previously, we found that reactive oxygen species (ROS) contribute to the barrier destructive effects of PLY and identified an unexpected but potent role of Hsp70 in suppressing ROS production.

We clarified a novel mechanism for autophagy regulation: ROS induces HSP70 to translocate to the nucleus, where it interacts with HMGB1b, which results in HMGB1b cytoplasmic translocation and subsequent HMGB1b–Beclin 1 autophagic pathway activation.