caa a22 4500 606234756 CHVBK 20210128101239.0 cr unu---uuuuu 210128e20151101xx s 000 0 eng 10.1007/s11010-015-2508-x doi (NATIONALLICENCE)springer-10.1007/s11010-015-2508-x Immuno-spin trapping detection of antioxidant/pro-oxidant properties of zinc or selenium on DNA and protein radical formation via hydrogen peroxide [Elektronische Daten] [Vedia Deletioglu, Erkan Tuncay, Aysegul Toy, Mustafa Atalay, Belma Turan] Trace elementscan participate in the catalysis of group-transfer reactions and can serve as their structural components.However, most of them including zinc and selenium have multifunctional roles in biological environments such as antioxidant and/or pro-oxidant effects, as concentration-dependent manner. Although it has been demonstrated the antioxidant actions of either selenium or zinc compounds, there are several documents pointing out their pro-oxidant/oxidant roles in biological systems. Here we have used ELISA-based immuno-spin trapping, a method for detection of free radical formation, to detect whether or not a zinc compound, Zn3(PO4)2, or a selenium compound, Na2SeO3, has antioxidant and/or pro-oxidant effect on 5,5-Dimethyl-1-Pyrroline-N-Oxide (DMPO)-DNA nitrone adducts induced with Cu(II)-H2O2-oxidizing system in in vitro preparations. Second, we examined whether this technique is capable to demonstrate the different DMPO-protein nitrone adduct productions in isolated protein crude of hearts from normal rats (CON) or rats with metabolic syndrome (MetS). Our data demonstrated that either Zn2+ (100 µM) or $${\text{SeO}}_{3}^{ - 2}$$ SeO 3 - 2 (50 nM) has very strong antioxidant action against 200 µM H2O2-induced DMPO-DNA nitrone adduct production, whereas their higher concentrations have apparent pro-oxidant actions. We also used verification by Western blotting analysis whether immuno-spin trapping can be used to assess H2O2-induced DMPO-protein nitrone adducts in heart protein crudes. Our Western blot data further confirmed the ELISA-data from proteins and demonstrated how Zn2+ or $${\text{SeO}}_{3}^{ - 2}$$ SeO 3 - 2 are dual-functioning ions such as antioxidant at lower concentrations while pro-oxidant at higher concentrations. Particularly, our present data with $${\text{SeO}}_{3}^{ - 2}$$ SeO 3 - 2 in DMPO-protein nitrone adducts, being in line with our previous observation on its dual-actions in ischemia/reperfusion-induced damaged heart, have shown that this ion has higher pro-oxidant actions over 50 nM in MetS-group compared to that of CON group. Springer Science+Business Media New York, 2015 Reactive oxygen species nationallicence Hydrogen peroxide nationallicence Heart nationallicence Metabolic syndrome nationallicence Lipid peroxidation nationallicence Glutathione nationallicence Deletioglu Vedia Department of Biophysics, Ankara University Faculty of Medicine, 06100, Ankara, Turkey aut Tuncay Erkan Department of Biophysics, Ankara University Faculty of Medicine, 06100, Ankara, Turkey aut Toy Aysegul Department of Biophysics, Ankara University Faculty of Medicine, 06100, Ankara, Turkey aut Atalay Mustafa Institute of Biomedicine, Physiology, University of Eastern Finland, Kuopio, Finland aut Turan Belma Department of Biophysics, Ankara University Faculty of Medicine, 06100, Ankara, Turkey aut Molecular and Cellular Biochemistry Springer US; http://www.springer-ny.com 409/1-2(2015-11-01), 23-31 0300-8177 409:1-2<23 2015 409 11010 https://doi.org/10.1007/s11010-015-2508-x text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s11010-015-2508-x text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Deletioglu Vedia Department of Biophysics, Ankara University Faculty of Medicine, 06100, Ankara, Turkey aut NATIONALLICENCE 700 1- Tuncay Erkan Department of Biophysics, Ankara University Faculty of Medicine, 06100, Ankara, Turkey aut NATIONALLICENCE 700 1- Toy Aysegul Department of Biophysics, Ankara University Faculty of Medicine, 06100, Ankara, Turkey aut NATIONALLICENCE 700 1- Atalay Mustafa Institute of Biomedicine, Physiology, University of Eastern Finland, Kuopio, Finland aut NATIONALLICENCE 700 1- Turan Belma Department of Biophysics, Ankara University Faculty of Medicine, 06100, Ankara, Turkey aut NATIONALLICENCE 773 0- Molecular and Cellular Biochemistry Springer US; http://www.springer-ny.com 409/1-2(2015-11-01), 23-31 0300-8177 409:1-2<23 2015 409 11010