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

2023 · Benefit · Low evidence

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BenefitLow evidencePaper 387

Study snapshot

Publicationmanual · 2023

Study typein_vitro

Reported directionBenefit

Evidence ratingLow

Abstract

Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding Huang Z, Ito M, Zhang S, Toda T, Takeda JI, Ogi T, Ohno K. Extremely low-frequency electromagnetic field induces acetylation of heat shock proteins and enhances protein folding. Ecotoxicol Environ Saf. 2023 Sep 15;264:115482. doi: 10.1016/j.ecoenv.2023.115482. Highlights • We previously showed that ELF-EMF at 10 µT induces mitochondrial hormesis. • In AML12 and HEK293 cells, ELF-EMF markedly increased acetylation of HSP70/90 at 3 h. • In both cells, ELF-EMF markedly increased binding of HSP70/90 to HOP/STIP1 at 3 h. • In both cells, ELF-EMF reduced protein aggregates and enhanced cell viability at 3 h. • In both cells, ELF-EMF reduced mitochondria mass and elevated maximal oxygen consumption at 3 h. Abstract The pervasive weak electromagnetic fields (EMF) inundate the industrialized society, but the biological effects of EMF as weak as 10 µT have been scarcely analyzed. Heat shock proteins (HSPs) are molecular chaperones that mediate a sequential stress response. HSP70 and HSP90 provide cells under undesirable situations with either assisting covalent folding of proteins or degrading improperly folded proteins in an ATP-dependent manner. Here we examined the effect of extremely low-frequency (ELF)-EMF on AML12 and HEK293 cells. Although the protein expression levels of HSP70 and HSP90 were reduced after an exposure to ELF-EMF for 3 h, acetylations of HSP70 and HSP90 were increased, which was followed by an enhanced binding affinities of HSP70 and HSP90 for HSP70/HSP90-organizing protein (HOP/STIP1). After 3 h exposure to ELF-EMF, the amount of mitochondria was reduced but the ATP level and the maximal mitochondrial oxygen consumption were increased, which was followed by the reduced protein aggregates and the increased cell viability. Thus, ELF-EMF exposure for 3 h activated acetylation of HSPs to enhance protein folding, which was returned to the basal level at 12 h. The proteostatic effects of ELF-EMF will be able to be applied to treat pathological states in humans. Open access paper: sciencedirect.com

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AI evidence extraction

Structured fields below were generated from the paper’s abstract and metadata to make the evidence easier to inspect. Automated extraction may be incomplete or incorrect; verify important details against the original paper.

Study typein_vitro

Effect directionbenefit

PopulationAML12 and HEK293 cells

Sample sizeNot supplied

ExposureELF · 3 h (effects returned to basal at 12 h)

Evidence strengthLowConfidence: 74% · Peer reviewed: yes

Main findings

In AML12 and HEK293 cells, exposure to ELF-EMF (reported as 10 µT) for 3 h reduced HSP70/90 protein expression but increased acetylation of HSP70/90 and increased their binding to HOP/STIP1. After 3 h exposure, mitochondrial mass decreased while ATP level and maximal mitochondrial oxygen consumption increased, accompanied by reduced protein aggregates and increased cell viability; effects returned to basal by 12 h.

Outcomes measured

HSP70 expression
HSP90 expression
HSP70 acetylation
HSP90 acetylation
HSP70/90 binding to HOP/STIP1
mitochondrial mass
ATP level
maximal mitochondrial oxygen consumption
protein aggregates
cell viability

Limitations

Frequency of the ELF-EMF exposure not specified in the abstract/metadata
No sample size or replication details provided in the abstract
In vitro cell models only; no in vivo or human data reported in the abstract

View raw extracted JSON

{
  "study_type": "in_vitro",
  "exposure": {
    "band": "ELF",
    "source": null,
    "frequency_mhz": null,
    "sar_wkg": null,
    "duration": "3 h (effects returned to basal at 12 h)"
  },
  "population": "AML12 and HEK293 cells",
  "sample_size": null,
  "outcomes": [
    "HSP70 expression",
    "HSP90 expression",
    "HSP70 acetylation",
    "HSP90 acetylation",
    "HSP70/90 binding to HOP/STIP1",
    "mitochondrial mass",
    "ATP level",
    "maximal mitochondrial oxygen consumption",
    "protein aggregates",
    "cell viability"
  ],
  "main_findings": "In AML12 and HEK293 cells, exposure to ELF-EMF (reported as 10 µT) for 3 h reduced HSP70/90 protein expression but increased acetylation of HSP70/90 and increased their binding to HOP/STIP1. After 3 h exposure, mitochondrial mass decreased while ATP level and maximal mitochondrial oxygen consumption increased, accompanied by reduced protein aggregates and increased cell viability; effects returned to basal by 12 h.",
  "effect_direction": "benefit",
  "limitations": [
    "Frequency of the ELF-EMF exposure not specified in the abstract/metadata",
    "No sample size or replication details provided in the abstract",
    "In vitro cell models only; no in vivo or human data reported in the abstract"
  ],
  "evidence_strength": "low",
  "confidence": 0.74,
  "peer_reviewed_likely": "yes",
  "keywords": [
    "extremely low-frequency",
    "ELF-EMF",
    "10 µT",
    "heat shock proteins",
    "HSP70",
    "HSP90",
    "acetylation",
    "HOP",
    "STIP1",
    "protein folding",
    "proteostasis",
    "mitochondria",
    "ATP",
    "oxygen consumption",
    "cell viability",
    "protein aggregates"
  ],
  "suggested_hubs": []
}

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AI-extracted fields are generated from the abstract and metadata and may be incomplete or incorrect. This material is for informational purposes and is not medical advice.

Identifiers and source

DOI: 10.1016/j.ecoenv.2023.115482
PubMed: Not supplied

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