title: Exposure to ELF magnetic fields modulate redox related protein expression in mouse macrophages.
abstract: The interaction of extremely low frequency (ELF) magnetic fields (MF) with cells can induce alterations in various cell physiological processes. Here, we present evidence that exposure of mouse macrophages to 50 Hz, 1.0 mT MF lead to immune cell activation seen as increased production of reactive oxygen species (ROS), and also to modulation on the expression level of important proteins acting in redox regulatory processes and thus explaining the noted changes in ROS levels seen after exposure. The MF exposure caused slight and transient decreases after short term exposures (2h or less) of clathrin, adaptin, PI3-kinase, protein kinase B (PKB) and PP2A, whereas longer exposures had no effect. The levels of the NAD(P)H oxidase subunit gp91phox oscillated between increased and normal levels compared to controls. The stress proteins Hsp70 and Hsp110 exhibited increased levels at certain time points, but not generally. The effects of MF on protein levels are different from the effects exerted by 12-O-tetradecanolyphobol-13-acetate (TPA) or LPS, although all three factors cause increases in ROS release. This suggests that ELF MF interacts with other cellular constituents than these chemicals, although induced pathways at least partially converge.
authors.affiliation: Division of Environmental Physiology, Department of Cell Biology and Biosystems Technology, University of Rostock, Rostock, Germany.
authors.forename: Jana
authors.initials: J
authors.lastname: Frahm
authors.forename: Mats-Olof
authors.initials: MO
authors.lastname: Mattsson
authors.forename: Myrtill
authors.initials: M
authors.lastname: Simkó
mesh_terms: D033965:Adaptor Protein Complex alpha Subunits / Q000096:biosynthesis; D000818:Animals; D015153:Blotting, Western; D002460:Cell Line; D002966:Clathrin / Q000096:biosynthesis; D004574:Electromagnetic Fields; D005434:Flow Cytometry; D050957:HSP110 Heat-Shock Proteins / Q000096:biosynthesis; D018840:HSP70 Heat-Shock Proteins / Q000096:biosynthesis; D008264:Macrophages / Q000378:metabolism / Q000502:physiology / Q000528:radiation effects*; D051379:Mice; D010084:Oxidation-Reduction / Q000528:radiation effects*; D018384:Oxidative Stress / Q000528:radiation effects; D019869:Phosphatidylinositol 3-Kinases / Q000096:biosynthesis; D014176:Protein Biosynthesis / Q000528:radiation effects*; D051057:Proto-Oncogene Proteins c-akt / Q000096:biosynthesis; D017382:Reactive Oxygen Species / Q000378:metabolism / Q000528:radiation effects; D015398:Signal Transduction / Q000528:radiation effects
chemical_list: D033965:Adaptor Protein Complex alpha Subunits; D002966:Clathrin; D050957:HSP110 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D017382:Reactive Oxygen Species; D019869:Phosphatidylinositol 3-Kinases; D051057:Proto-Oncogene Proteins c-akt