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Generation and propagation of yeast prion [URE3] are elevated under electromagnetic field.

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Lian HY, Lin KW, Yang C, Cai P. · 2017

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EMF exposure promotes protein misfolding linked to neurodegenerative diseases, with effects increasing over time and exposure intensity.

Plain English Summary

Summary written for general audiences

Researchers exposed yeast cells to radiofrequency radiation (2.0 GHz) and extremely low frequency fields (50 Hz) to study effects on protein misfolding. They found that both types of electromagnetic fields increased the formation and spread of prions (misfolded proteins linked to neurodegenerative diseases) in a dose-dependent manner. This suggests EMF exposure may contribute to protein misfolding disorders through oxidative stress mechanisms.

Why This Matters

This study breaks new ground by demonstrating that electromagnetic fields can directly promote protein misfolding, a process central to neurodegenerative diseases like Alzheimer's and Parkinson's. The researchers used yeast as a model organism because prion formation follows similar mechanisms across species. What makes this particularly concerning is that the 2.0 GHz frequency is close to what cell phones use, while 50 Hz matches the electrical grid frequency in many countries. The dose-dependent response they observed with ELF fields suggests that higher exposures create more protein damage. The finding that oxidative stress increased during short-term exposure provides a biological mechanism for how EMF might contribute to neurodegeneration over time.

Exposure Information

A logarithmic frequency spectrum from 10 Hz to 100 GHz showing where this study's 50 Hz - 2 GHz exposure sits relative to common EMF sources.Where This Frequency Sits on the EMF SpectrumELFVLFLF / MFHF / VHFUHFSHFmm10 Hz100 GHzThis study: 50 Hz - 2 GHzCell phones~1 GHzWiFi2.4 GHz5G mm28 GHzLogarithmic scale

Specific exposure levels were not quantified in this study. The study examined exposure from: 2.0 GHz and 50 Hz

Study Details

In this study, we studied the effect of 2.0 GHz radio frequency electromagnetic field (RF-EMF) and 50 Hz extremely low frequency electromagnetic field (ELF-EMF) exposure on prion generation and propagation using two budding yeast strains, NT64C and SB34, as model organisms.

Under exposure to RF-EMF or ELF-EMF, the de novo generation and propagation of yeast prions [URE3] w...

This work demonstrated for the first time that EMF exposure could elevate the de novo generation and propagation of yeast prions and supports the hypothesis that ROS may play a role in the effects of EMF on protein misfolding. The effects of EMF on protein folding and ROS levels may mediate the broad effects of EMF on cell function.

Cite This Study
Lian HY, Lin KW, Yang C, Cai P. (2017). Generation and propagation of yeast prion [URE3] are elevated under electromagnetic field. Cell Stress Chaperones. 2017 Dec 6. doi: 10.1007/s12192-017-0867-9.
Show BibTeX
@article{hy_2017_generation_and_propagation_of_2362,
  author = {Lian HY and Lin KW and Yang C and Cai P.},
  title = {Generation and propagation of yeast prion [URE3] are elevated under electromagnetic field.},
  year = {2017},
  
  url = {https://pubmed.ncbi.nlm.nih.gov/29214607/},
}
PubMed: 29214607

Cited By (11 papers)

Quick Questions About This Study

Yes, a 2017 study found that both 2.0 GHz radiofrequency and 50 Hz extremely low frequency electromagnetic fields increased prion formation and spread in yeast cells. This protein misfolding occurred in a dose-dependent manner, suggesting EMF exposure may contribute to neurodegenerative disease processes.
Research demonstrates that both 2.0 GHz radiofrequency radiation and 50 Hz extremely low frequency fields elevate prion generation and propagation in yeast cells. The effects increased over time, with 50 Hz fields showing dose-dependent responses, indicating frequency-specific biological impacts.
EMF exposure significantly elevated reactive oxygen species (ROS) levels and increased superoxide dismutase and catalase enzyme activities during short-term exposure in yeast cells. This oxidative stress response may explain how electromagnetic fields contribute to protein misfolding and cellular dysfunction.
No, electromagnetic field exposure did not significantly change the expression levels of key molecular chaperones Hsp104, Hsp70-Ssa1/2, and Hsp40-Ydj1 in yeast cells. This suggests EMF-induced protein misfolding occurs through mechanisms independent of chaperone protein regulation.
EMF exposure increased prion formation in yeast cells, which are misfolded proteins linked to neurodegenerative diseases. This 2017 research was the first to demonstrate that electromagnetic fields can promote protein misfolding, potentially contributing to conditions like Alzheimer's and Parkinson's disease.