Browse

Radiofrequency radiation does not induce stress response in human T-lymphocytes and rat primary astrocytes

Cited 28 time in Web of Science Cited 34 time in Scopus
Authors
Lee, Jae-Seon; Huang, Tai-Qin; Kim, Tae-Hyung; Kim, Jin Young; Kim, Hyun Jeong; Pack, Jeong-Ki; Seo, Jeong-Sun
Issue Date
2006-07-14
Publisher
Wiley-Blackwell
Citation
Bioelectromagnetics. 2006 Oct;27(7):578-88.
Keywords
AnimalsAstrocytes/*radiation effectsCells, Cultured*Cellular PhoneExtracellular Signal-Regulated MAP Kinases/metabolismHSP27 Heat-Shock ProteinsHSP72 Heat-Shock Proteins/biosynthesisHeat-Shock Proteins/*biosynthesisHumansHot Temperature/adverse effectsJNK Mitogen-Activated Protein Kinases/metabolismJurkat CellsMitogen-Activated Protein Kinases/*biosynthesisNeoplasm Proteins/biosynthesisPhosphorylation/radiation effects*Radio WavesRatsT-Lymphocytes/*radiation effectsTetradecanoylphorbol Acetate/pharmacologyp38 Mitogen-Activated Protein Kinases/metabolism
Abstract
Heat shock proteins (HSPs) are rapidly induced by a variety of stressors, including heat shock, ethanol, heavy metals, UV, and gamma-radiation. Mitogen-activated protein kinases (MAPKs) are also involved in the stress transduction pathways in all eukaryotes. In this study, we attempted to determine whether radiofrequency (RF) radiation is able to induce a non-thermal stress response. Human T-lymphocyte Jurkat cells and rat primary astrocytes were exposed to 1763 MHz of RF radiation at an average specific absorption rate (SAR) of either 2 W/kg or 20 W/kg, for 30 min or 1 h. Temperature was completely controlled at 37 +/- 0.2 degrees C throughout the exposure period. The sham exposures were performed under exactly identical experimental conditions without exposure to RF radiation. We assessed alterations in the expression of HSPs and the activation of MAPKs in the RF-exposed cells. No detectable difference was observed in the expression levels of HSP90, HSP70, and HSP27. The phosphorylation status of MAPKs, extracellular signal-regulated kinases (ERK1/2), c-Jun N-terminal protein kinases (JNK1/2), or p38, did not change significantly. In order to determine whether RF radiation can promote the effects of 12-O-tetradecanoylphorbol 13-acetate (TPA) on stress response, cells were exposed to RF radiation coupled with TPA treatment. When TPA alone was applied, the MAPKs were found to be phosphorylated in a dose-dependent manner. However, RF radiation did not result in any enhancement of TPA-induced MAPK phosphorylation. Neither TPA nor RF radiation exerted any detectable effect on the induction of HSPs. These results indicate that 1763 MHz RF radiation alone did not elicit any stress response, nor did it have any effect on TPA-induced MAPK phosphorylation, under our experimental conditions.
ISSN
0197-8462 (Print)
Language
English
URI
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16838270

http://hdl.handle.net/10371/23859
DOI
https://doi.org/10.1002/bem.20235
Files in This Item:
There are no files associated with this item.
Appears in Collections:
College of Medicine/School of Medicine (의과대학/대학원)Dept. of Biochemistry & Molecular Biology (생화학교실)Journal Papers (저널논문_생화학교실)
  • mendeley

Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse