Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding
Abstract
Overview
The study investigates the effects of extremely low-frequency electromagnetic fields (ELF-EMF) on heat shock proteins (HSPs) and cellular functions.
Findings
- ELF-EMF at 10 µT induces mitochondrial hormesis, revealed through various experiments in AML12 and HEK293 cells.
- Significant acetylation of HSP70 and HSP90 at 3 hours and their enhanced binding to HOP/STIP1.
- Reduction in mitochondria mass and simultaneous increase in maximal oxygen consumption and ATP levels.
- Overall, ELF-EMF exposure reduced protein aggregates and enhanced cell viability.
Conclusion
The application of ELF-EMF can activate acetylation of HSPs, improve protein folding, and potentially treat pathological states, though the effect returned to basal level after 12 hours.