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To study the effects of 1763 MHz irradiation emitted from mobile phones on stress response.
Expression of heat shock proteins and the phosphorylation of the mitogen-activated protein kinases (MAPK; major participants in stress responses) were monitored. Whether radiofrequency exposure exerted a synergistic effect on the status of mitogen-activated protein kinase phosphorylation induced by TPA was also determined. Positive controls were performed (43°C, 30 min).
|ばく露時間||continuous for 30 min or 1 h|
|Modulation type||cf. additional information|
|チャンバの詳細||The experimental chamber (W 115 mm x H 80 mm x L 240 mm) was made of aluminium and therefore shielded. The temperature was maintained at 37 ± 0.2°C by cooling water circulating through its bottom. Gas from an incubator was circulated through the cavity to maintain CO2 density and humidity.|
|ばく露装置の詳細||The RF signal was fed by a λ/8 monopole antenna (22 mm long) at the λ/4 position of the top plate of the cavity exciting only the fundamental TE102 mode and allowing a uniform exposure of a 100-mm culture dish. The 100-mm Petri dish having an inner diameter of 85 mm, a 1-mm wall, and a 91-mm lid was filled with 18 ml of culture medium standing 4 mm high.|
|Sham exposure||A sham exposure was conducted.|
|Additional information||For positive (heat shock) control, culture dishes were wrapped tightly with parafilm and immersed in a water bath at 43 ± 0.2°C for 30 min.|
No detectable difference was found in the expression levels of the different heat shock proteins of exposed cells as compared to the levels measured in sham-exposed cells. The phosphorylation status of mitogen-activated protein kinases, extracellular signal-regulated kinases, c-Jun N-terminal protein kinases, or p38, did not change significantly.
When TPA alone was applied, the mitogen-activated protein kinases were found to be phosphorylated in a dose-dependent manner. However, radiofrequency irradiation did not result in any enhancement of TPA-induced phosphorylation. Neither TPA nor radiofrequency irradiation exerted any detectable effect on the induction of heat shock proteins.