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Luciferase activity and synthesis of Hsp70 and Hsp90 are insensitive to 50Hz electromagnetic fields.

机译:萤光素酶活性以及Hsp70和Hsp90的合成对50Hz电磁场不敏感。

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摘要

The activity of luciferase expressed in transfected 34i cells has been monitored under 50Hz EMF and heat shock. While heat shock decreased the luciferase activity, short exposure to EMFs did not, the luciferase expressed in cells exposed to EMFs at 300-3000 microT showing the same activity as that of control cells. To further analyse whether EMF and thermal stress display similar effects, the relative rate of Hsp90 and Hsp70 synthesis was investigated. Hsp90 and Hsp70 synthesis, while induced by a short thermal stress, was not increased by EMF exposure. These results, contrary to previously proposed similarities between thermal stress and EMF effects at a cellular level, indicate that protein denaturation and misfolding caused by thermal stress and responsible both for a loss of luciferase activity and for an induction of Hsp, are not necessarily induced by exposure to EMFs.
机译:已经在50Hz EMF和热激下监测了转染的34i细胞中表达的萤光素酶的活性。虽然热休克降低了荧光素酶活性,但短时间暴露于EMF却没有,荧光素酶在300-3000 microT暴露于EMFs的细胞中表达,显示出与对照细胞相同的活性。为了进一步分析EMF和热应力是否显示相似的效果,研究了Hsp90和Hsp70合成的相对速率。 Hsp90和Hsp70的合成,虽然是由短暂的热应力引起的,但并未因EMF暴露而增加。这些结果与先前提出的在细胞水平上热应激和EMF效应之间的相似性相反,表明由热应激引起并导致萤光素酶活性丧失和Hsp诱导负有责任的蛋白质变性和错折叠,并不一定是由暴露于电动势。

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