Abstract：
:Amyloid beta peptide (Aβ) is implicated in the development of pathological reactions associated with Alzheimer's disease (AD), such as oxidative stress, neuro-inflammation and death of brain cells. Current pharmacological approaches to treat AD are not able to control the deposition of Aβ and suppression of Aβ-induced cellular response. There is a growing body of evidence that exposure to radiofrequency electromagnetic field (RF-EMF) causes a decrease of beta-amyloid deposition in the brains and provides cognitive benefits to Alzheimer's Tg mice. Herein, we investigated the effects of mobile phone radiofrequency EMF of 918 MHz on reactive oxygen species (ROS) formation, mitochondrial membrane potential (MMP), activity of NADPH-oxidase, and phosphorylation of p38MAPK and ERK1/2 kinases in human and rat primary astrocytes in the presence of Aβ42 and H2O2. Our data demonstrate that EMF is able to reduce Aβ42- and H2O2-induced cellular ROS, abrogate Aβ₄₂-induced production of mitochondrial ROS and the co-localization between the cytosolic (p47-phox) and membrane (gp91-phox) subunits of NADPH oxidase, while increasing MMP, and inhibiting H2O2-induced phosphorylation of p38MAPK and ERK1/2 in primary astrocytes. Yet, EMF was not able to modulate alterations in the phosphorylation state of the MAPKs triggered by Aβ42. Our findings provide an insight into the mechanisms of cellular and molecular responses of astrocytes on RF-EMF exposure and indicate the therapeutic potential of RF-EMF for the treatment of Alzheimer's disease.
journal_name
Neurosciencejournal_title
Neuroscienceauthors
Tsoy A,Saliev T,Abzhanova E,Turgambayeva A,Kaiyrlykyzy A,Akishev M,Saparbayev S,Umbayev B,Askarova Sdoi
10.1016/j.neuroscience.2019.03.058subject
Has Abstractpub_date
2019-06-01 00:00:00pages
46-57eissn
0306-4522issn
1873-7544pii
S0306-4522(19)30233-7journal_volume
408pub_type
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