Applicability of discovery science approach to determine biological effects of mobile phone radiation
- 29 January 2004
- journal article
- research article
- Published by Wiley in Proteomics
- Vol. 4 (2) , 426-431
- https://doi.org/10.1002/pmic.200300646
Abstract
We argue that the use of high-throughput screening techniques, although expensive and laborious, is justified and necessary in studies that examine biological effects of mobile phone radiation. The “case of hsp27 protein” presented here suggests that even proteins with only modestly altered (by exposure to mobile phone radiation) expression and activity might have an impact on cell physiology. However, this short communication does not attempt to present the full scientific evidence that is far too large to be presented in a single article and that is being prepared for publication in three separate research articles. Examples of the experimental evidence presented here were designed to show the flow of experimental process demonstrating that the use of high-throughput screening techniques might help in rapid identification of the responding proteins. This, in turn, can help in speeding up of the process of determining whether these changes might affect human health.*Keywords
This publication has 10 references indexed in Scilit:
- Non-thermal activation of the hsp27/p38MAPK stress pathway by mobile phone radiation in human endothelial cells: Molecular mechanism for cancer- and blood-brain barrier-related effectsDifferentiation, 2002
- Mobile phones, precautionary principle, and future researchThe Lancet, 2001
- Hsp27 Inhibits Cytochrome c-Mediated Caspase Activation by Sequestering Both Pro-caspase-3 and Cytochrome cGene Expression, 2001
- Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3Oncogene, 2000
- Equipping scientists for the new biologyNature Biotechnology, 2000
- Induction of stress proteins in human endothelial cells by heavy metal ions and heat shockAmerican Journal of Physiology-Lung Cellular and Molecular Physiology, 1999
- Regulation of Hsp27 Oligomerization, Chaperone Function, and Protective Activity against Oxidative Stress/Tumor Necrosis Factor α by PhosphorylationJournal of Biological Chemistry, 1999
- Exposure of tumor necrosis factor‐α to luminal membrane of bovine brain capillary endothelial cells cocultured with astrocytes induces a delayed increase of permeability and cytoplasmic stress fiber formation of actinJournal of Neuroscience Research, 1995
- Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27.Journal of Biological Chemistry, 1993
- Permanent cell line expressing human factor VIII-related antigen established by hybridization.Proceedings of the National Academy of Sciences, 1983