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Activation of endoplasmic reticulum stress in rat brain following low-intensity microwave exposure

  • Ranjeet Kumar
  • Pravin S. Deshmukh
  • Sonal Sharma
  • BasuDev BanerjeeEmail author
Research Article
  • 13 Downloads

Abstract

The present study was designed to explore the effects of low-intensity microwave radiation on endoplasmic reticulum stress and unfolded protein response. Experiments were performed on male Wistar rats exposed to microwave radiation for 30 days at 900 MHz, 1800 MHz, and 2450 MHz frequencies on four groups of animal: sham-exposed group, 900 MHz exposed (SAR 5.84 × 10−4 W/kg), 1800 MHz exposed (SAR 5.94 × 10−4 W/kg), and 2450 MHz exposed (SAR 6.7 × 10−4 W/kg) groups. Expressions of mRNA were estimated at the end of exposure in rat brain by real-time quantitative PCR. Microwave exposure at 900, 1800, and 2450 MHz with respective SAR values as mentioned above significantly (< 0.05) altered mRNA expression of transcription factors ATF4, CHOP, and XBP1 in accordance with increasing microwave frequency. The result of the present study reveals that low-intensity microwave exposure at frequencies 900, 1800, and 2450 MHz induces endoplasmic reticulum stress and unfolded protein response.

Keywords

Brain Microwave Endoplasmic reticulum stress Gene expression Unfolded protein response 

Notes

Acknowledgements

The authors would like to express their gratitude to Indian Council of Medical Research (ICMR), New Delhi, India for providing the major grant to support the microwave exposure facility. One of the authors, Ranjeet Kumar, Junior Research Fellow is grateful to University Grant Commission (UGC), Govt. of India, for providing Fellowship.

Compliance with ethical standards

The protocol and study method were approved by the Institutional Animal Ethical Committee, University College of Medical Sciences, Delhi (UCMS/IAEC/CAH/2016/093) and care of the animals was undertaken as per guidelines of the Committee for the Purpose of Control and Supervision of Experiments on Animals, India.

Conflict of interest

The authors declare that they have no conflict of interest.

References

  1. Ardoino L, Lopresto V, Mancini S, Marino C, Pinto R, Lovisolo GA (2005) A radio-frequency system for in vivo pilot experiments aimed at the studies on biological effects of electromagnetic fields. Phys Med Biol 15:3643–3654Google Scholar
  2. Botta A, Malena A, Loro E, Del Moro G, Suman M, Pantic B, Szabadkai G, Vergani L (2013) Altered Ca2+ homeostasis and endoplasmic reticulum stress in myotonic dystrophy type 1 muscle cells. Genes (Basel) 4(2):275–292Google Scholar
  3. Dandekar A, Mendez R, Zhang K (2015) Cross talk between ER stress, oxidative stress, and inflammation in health and disease. Methods Mol Biol 1292:205–214Google Scholar
  4. Deshmukh PS, Megha K, Banerjee BD, Abegaonkar MP, Ahmed RS, Tripathi AK, Mediratta PK (2012) Modulation of heat shock protein level and cognitive impairment in Fischer rats exposed to low level microwave radiation. Asia J Biotech Reso 03(10):1391–1399Google Scholar
  5. Deshmukh PS, Nasare N, Megha K, Banerjee BD, Ahmed RS, Singh D, Abegaonkar MP, Tripathi AK, Mediratta PK (2015) Cognitive impairment and neurogenotoxic effects in rats exposed to low intensity microwave radiation. Int J Toxicol 34(3):284–290Google Scholar
  6. Deshmukh PS, Megha K, Nasare N, Banerjee BD, Ahmed RS, Abegaonkar MP, Tripathi AK, Mediratta PK (2016) Effect of low level subchronic microwave radiation on rat brain. Biomed Environ Sci 29(12):858–867Google Scholar
  7. Esposito MD, Postle BR (2015) The cognitive neuroscience of working memory. Annu Rev Psychol 3(66):115–142Google Scholar
  8. Ferrante C, Recinella L, Locatelli M, Guglielmi P, Secci D, Leporini L, Chiavaroli A, Leone S, Martinotti S, Brunetti L, Vacca M, Menghini L, Orlando G (2017) Protective effects induced by microwave-assisted aqueous Harpagophytum extract on rat cortex synaptosomes challenged with amyloid β-peptide. Phytother Res 31(8):1257–1264Google Scholar
  9. Frade JM, Ovejero-Benito MC (2015) Neuronal cell cycle: the neuron itself and its circumstances. Cell Cycle 14(5):712–720Google Scholar
  10. Fusakio ME, Willy JA, Wang Y, Mirek ET, Al Baghdadi RJ, Adams CM, Anthony TG, Wek RC (2016) Transcription factor ATF4 directs basal and stress-induced gene expression in the unfolded protein response and cholesterol metabolism in the liver. Mol Biol Cell 27(9):1536–1551Google Scholar
  11. Gardner BM, Walter P (2011) Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science 333(6051):1891–1894Google Scholar
  12. Guidi S, Ciani E, Severi S, Contestabile A, Bartesaghi R (2015) Postnatal neurogenesis in the dentate gyrus of the guinea pig. Hippocampus 15(3):285–301Google Scholar
  13. Hermann DM, Hossmann KA (1997) Neurological effects of microwave exposure related to mobile communication. J Neurol Sci 152(1):1–14Google Scholar
  14. Hetz C (2012) The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol 13(2):89–102Google Scholar
  15. Hetz C, Martinon F, Rodriguez D, Glimcher LH (2011) The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol Rev 91(4):1219–1243Google Scholar
  16. Lee AH, Iwakoshi NN, Glimcher LH (2003) XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 23(21):7448–7459Google Scholar
  17. Li G, Mongillo M, Chin KT, Harding H, Ron D, Marks AR, Tabas I (2009) Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol 186(6):783–792Google Scholar
  18. Livak JK, Schmittgen DT (2001) Analysis of relative gene expression data using real time quantitative PCR and the 2-ΔΔCT method. Methods 25(4):402–408Google Scholar
  19. Ma Y, Hendershot LM (2003) Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress. J Biol Chem 278(37):34864–34873Google Scholar
  20. Megha K, Deshmukh PS, Banerjee BD, Tripathi AK, Abegaonkar MP (2012) Microwave radiation induced oxidative stress, cognitive impairment and inflammation in brain of Fischer rats. Indian J Exp Biol 50(12):889–896Google Scholar
  21. Megha K, Deshmukh PS, Ravi AK, Tripathi AK, Abegaonkar MP, Banerjee BD (2015) Effect of low-intensity microwave radiation on monoamine neurotransmitters and their key regulating enzymes in rat brain. Cell Biochem Biophys 73(1):93–100Google Scholar
  22. Oslowski CM, Urano F (2011) Measuring ER stress and the unfolded protein response using mammalian tissue culture system. Methods Enzymol 490:71–92Google Scholar
  23. Praticò D (2002) Alzheimer’s disease and oxygen radicals: new insights. Biochem Pharmacol 63(4):563–567Google Scholar
  24. Ron D, Harding HP (2012) Protein-folding homeostasis in the endoplasmic reticulum and nutritional regulation. Cold Spring Harb Perspect Biol 4(12)Google Scholar
  25. Ron D, Walter P (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol. 8(7):519–529Google Scholar
  26. Rubin RD, Watson PD, Duff MC, Cohen NJ (2014) The role of the hippocampus in flexible cognition and social behaviour. Front Hum Neurosci 8(742):1–15Google Scholar
  27. Salford LG, Brun AE, Eberhardt JL, Malmgren L, Persson BR (2003) Nerve cell damage in mammalian brain after exposure to microwaves from GSM mobile phones. Environ Health Perspect 111(7):881–883Google Scholar
  28. Tsang KY, Chan D, Bateman JF, Cheah KS (2010) In vivo cellular adaptation to ER stress: survival strategies with double-edged consequences. J Cell Sci 123(Pt 13):2145–2154Google Scholar
  29. Yakymenko I, Sidorik E, Kyrylenko S, Chekhun V (2011) Long-term exposure to microwave radiation provokes cancer growth: evidences from radars and mobile communication systems. Exp Oncol 33(2):62–70Google Scholar
  30. Yang M, Angel MF, Pang Y, Angel JJ, Wang Z, Neumeister MW, Wetter N, Zhang F (2012) Expression of inducible nitric oxide synthase in muscle flaps treated with ischemic postconditioning. Hand (New York, N.Y.), 7(3), 297-302.Google Scholar
  31. Zhang K, Kaufman RJ (2008) From endoplasmic-reticulum stress to the inflammatory response. Nature 454(7203):455–462Google Scholar

Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Department of BiochemistryUniversity College of Medical Sciences, University of DelhiDelhiIndia
  2. 2.Department of PathologyUniversity College of Medical Sciences, University of DelhiDelhiIndia

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