Effect of Exposure to 1,800 MHz Electromagnetic Fields on Heat Shock Proteins and Glial Cells in the Brain of Developing Rats.

Summary of "Effect of Exposure to 1,800 MHz Electromagnetic Fields on Heat Shock Proteins and Glial Cells in the Brain of Developing Rats."

The increasing use of mobile phones by children raise issues about the effects of electromagnetic fields (EMF) on the immature Central Nervous System (CNS). In the present study, we quantified cell stress and glial responses in the brain of developing rats one day after a single exposure of 2 h to a GSM 1,800 MHz signal at a brain average Specific Absorption Rate (SAR) in the range of 1.7 to 2.5 W/kg. Young rats, exposed to EMF on postnatal days (P) 5 (n = 6), 15 (n = 5) or 35 (n = 6), were compared to pseudo-exposed littermate rats (n = 6 at all ages). We used western blotting to detect heat shock proteins (HSPs) and cytoskeleton- or neurotransmission-related proteins in the developing astroglia. The GSM signal had no significant effect on the abundance of HSP60, HSC70 or HSP90, of serine racemase, glutamate transporters including GLT1 and GLAST, or of glial fibrillary acid protein (GFAP) in either total or soluble tissue extracts. Imunohistochemical detection of CD68 antigen in brain sections from pseudo-exposed and exposed animals did not reveal any differences in the morphology or distribution of microglial cells. These results provide no evidence for acute cell stress or glial reactions indicative of early neural cell damage, in developing brains exposed to 1,800 MHz signals in the range of SAR used in our study.


Inserm, UMR 894, Physiopathologie des Maladies Psychiatriques, Centre de Psychiatrie et Neurosciences, Paris, France.

Journal Details

This article was published in the following journal.

Name: Neurotoxicity research
ISSN: 1476-3524


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A group of eukaryotic high-molecular mass heat-shock proteins that represent a subfamily of HSP70 HEAT-SHOCK PROTEINS. Hsp110 proteins prevent protein aggregation and can maintain denatured proteins in folding-competent states.

Stress-inducible members of the heat-shock proteins 70 family. HSP72 heat shock proteins function with other MOLECULAR CHAPERONES to mediate PROTEIN FOLDING and to stabilize pre-existent proteins against aggregation.

A subfamily of small heat-shock proteins that are closely related to ALPHA B-CRYSTALLIN. Hsp20 heat-shock proteins can undergo PHOSPHORYLATION by CYCLIC GMP-DEPENDENT PROTEIN KINASES.

A subfamily of small heat-shock proteins that function as molecular chaperones that aid in refolding of non-native proteins. They play a protective role that increases cellular survival during times of stress.

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