Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding

Authors: Huang Z, Ito M, Zhang S, Toda T, Takeda JI, Ogi T, Ohno K

Year: 2023 Sep 15

Category: Ecotoxicology

Journal: Ecotoxicology and Environmental Safety

DOI: 10.1016/j.ecoenv.2023.115482

URL: https://www.sciencedirect.com/science/article/pii/S0147651323009867

Abstract

Overview

The study focuses on the effects of extremely low-frequency electromagnetic fields (ELF-EMF) on protein acetylation and protein folding efficiencies within cellular environments. This is particularly relevant given the pervasive nature of weak electromagnetic fields in industrialized societies.

Findings

  • Mitochondrial Hormesis: Previous studies indicated that ELF-EMF at 10 µT induces mitochondrial hormesis.
  • Increased Acetylation: In AML12 and HEK293 cells, ELF-EMF exposure for 3 hours increased acetylation levels of HSP70 and HSP90.
  • Enhanced Binding Affinities: Post-exposure, there was an increased binding of HSP70 and HSP90 to HSP70/HSP90-organizing protein (HOP/STIP1).
  • Reduced Protein Aggregates and Enhanced Cell Viability: Concurrently, these changes led to reduced protein aggregates and enhanced cell viability.
  • Mitochondrial Adjustments: ELF-EMF exposure reduced mitochondria mass while elevating maximal oxygen consumption.

Conclusion

The exposure to ELF-EMF for 3 hours activated the acetylation of heat shock proteins, which enhanced protein folding capabilities. This effect returned to the basal level at 12 hours, suggesting a temporary modulation of proteostasis. Given these results, the potential applications of ELF-EMF in treating pathological states in humans are promising, indicating a significant link between ELF-EMF exposure and cellular health dynamics.

ELF-EMF Heat Shock Proteins Protein Folding Ecotoxicology Cellular Biology
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