To study the effects of free radicals on proteins by means of detecting protein carbonyl content, advanced oxidation protein products and 3-nitrotyrosine in guinea pigs under the effect of 50 Hz electric fields.
Concurrent with the application of the electric field, the administration of N-acetyl-cysteine was also investigated in order to explain if it acts as antioxidant, reduce oxidative damage or as pro-oxidant in tissue medium. Hepatic hydroxyproline level was also examined to study protein synthesis.
A total of 40 male guinea pigs were randomly divided into four groups composed of 10 animals: 1) control group (injection of saline solution), 2) electric field exposure group (+ injection of saline solution 30 min before the daily exposure), 3) N-acetyl-cysteine administration + sham exposure group, 4) N-acetyl-cysteine administration (30 minutes before exposure) + electric field exposure group.
Exposure | Parameters |
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Exposure 1:
50 Hz
Exposure duration:
continuous for 8 hr/day on 7 days
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animals were treated in four groups: i) control group - sham exposure ii) E-field exposure iii) daily injection of 300 mg/kg NAC + sham exposure iv) daily injection of 300 mg/kg NAC + E-field exposure
Frequency | 50 Hz |
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Type | |
Exposure duration | continuous for 8 hr/day on 7 days |
Exposure source |
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Setup | 80 cm x 80 cm x 18 cm wooden cages with the copper plates mounted on the top and bottom of the cage |
Sham exposure | A sham exposure was conducted. |
Measurand | Value | Type | Method | Mass | Remarks |
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electric field strength | 12 kV/m | - | measured and calculated | - | - |
No statistically significant changes occurred in protein carbonyl content, advanced oxidation protein products and 3-nitrotyrosine levels of the guinea pigs that were exposed to the electric field compared to the control group. However, liver hydroxyproline level was significantly diminished in the electric field exposure group compared to the control group.
These results may be caused by the fact that electric field exposure may affect the early formation of stable oxidized proteins, changing the direction of the reaction of oxidized proteins or Ieading to structural damage in protein synthesis although no statistically significant change was found in the levels of protein carbonyl content and advanced oxidation protein products.
Protein carbonyl content, advanced oxidation protein products and 3-nitrotyrosine levels changed significantly in the N-acetyl-cysteine-administrated groups (group 3 and 4).
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