Microwave radiation can alter protein conformation without bulk heating.

FEBS letters · 2003 · Harm · Low evidence

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HarmLow evidencePaper 6398

Study snapshot

PublicationFEBS letters · 2003

Study typein_vitro

Reported directionHarm

Evidence ratingLow

Abstract

Exposure to microwave radiation enhances the aggregation of bovine serum albumin in vitro in a time- and temperature-dependent manner. Microwave radiation also promotes amyloid fibril formation by bovine insulin at 60 degrees C. These alterations in protein conformation are not accompanied by measurable temperature changes, consistent with estimates from field modelling of the specific absorbed radiation (15-20 mW kg(-1)). Limited denaturation of cellular proteins could explain our previous observation that modest heat-shock responses are induced by microwave exposure in Caenorhabditis elegans. We also show that heat-shock responses both to heat and microwaves are suppressed after RNA interference ablating heat-shock factor function.

Machine Enhanced Logic

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 directionharm

PopulationNot supplied

Sample sizeNot supplied

Exposuremicrowave

Evidence strengthLowConfidence: 74% · Peer reviewed: yes

Main findings

Microwave exposure enhanced aggregation of bovine serum albumin in vitro in a time- and temperature-dependent manner and promoted amyloid fibril formation by bovine insulin at 60C. The reported conformational alterations were not accompanied by measurable temperature changes and were described as consistent with field-modelling estimates of specific absorbed radiation (150 mW kg(-1)). Heat-shock responses to both heat and microwaves were reported to be suppressed after RNA interference ablating heat-shock factor function.

Outcomes measured

Protein aggregation (bovine serum albumin)
Amyloid fibril formation (bovine insulin)
Measurable temperature change / bulk heating
Heat-shock response (Caenorhabditis elegans)
Effect of RNA interference ablating heat-shock factor on heat- and microwave-induced heat-shock responses

Limitations

Microwave frequency and exposure duration not specified in the abstract
In vitro protein systems; generalizability to living organisms not established from the abstract
Temperature measurements described as showing no measurable change, but methods/sensitivity not provided in the abstract
Specific absorbed radiation reported as an estimate from field modelling; details not provided in the abstract

View raw extracted JSON

{
  "study_type": "in_vitro",
  "exposure": {
    "band": "microwave",
    "source": null,
    "frequency_mhz": null,
    "sar_wkg": null,
    "duration": null
  },
  "population": null,
  "sample_size": null,
  "outcomes": [
    "Protein aggregation (bovine serum albumin)",
    "Amyloid fibril formation (bovine insulin)",
    "Measurable temperature change / bulk heating",
    "Heat-shock response (Caenorhabditis elegans)",
    "Effect of RNA interference ablating heat-shock factor on heat- and microwave-induced heat-shock responses"
  ],
  "main_findings": "Microwave exposure enhanced aggregation of bovine serum albumin in vitro in a time- and temperature-dependent manner and promoted amyloid fibril formation by bovine insulin at 60\u0000C. The reported conformational alterations were not accompanied by measurable temperature changes and were described as consistent with field-modelling estimates of specific absorbed radiation (15\u0013\u00020 mW kg(-1)). Heat-shock responses to both heat and microwaves were reported to be suppressed after RNA interference ablating heat-shock factor function.",
  "effect_direction": "harm",
  "limitations": [
    "Microwave frequency and exposure duration not specified in the abstract",
    "In vitro protein systems; generalizability to living organisms not established from the abstract",
    "Temperature measurements described as showing no measurable change, but methods/sensitivity not provided in the abstract",
    "Specific absorbed radiation reported as an estimate from field modelling; details not provided in the abstract"
  ],
  "evidence_strength": "low",
  "confidence": 0.74,
  "peer_reviewed_likely": "yes",
  "keywords": [
    "microwave radiation",
    "protein conformation",
    "protein aggregation",
    "bovine serum albumin",
    "amyloid fibrils",
    "bovine insulin",
    "non-thermal effects",
    "specific absorbed radiation",
    "heat-shock response",
    "Caenorhabditis elegans",
    "RNA interference",
    "heat-shock factor"
  ],
  "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/s0014-5793(03)00413-7
PubMed: 12753912

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