7th International Molecular Biology and Biotechnology Congress, Konya, Türkiye, 25 - 27 Nisan 2018, ss.130
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production, and synthesis of DNA, RNA and protein. Although it is essential
for all living organisms, excess iron intake induces reactive oxygen species (ROS)
the through Fenton reaction. Elevated ROS leads to damage of biomolecules and
organ function. Therefore, antioxidant system act to protect the cell against oxidative
damage. The aim of this study was to provide a better understanding of how the
long-term iron overload affects the gene expression and activity of some antioxidant
enzymes including glucose 6-phosphate dehydrogenase (G6PD), 6-phosphogluconate
dehydrogenase (6PGD), and glutathione reductase (GR) as in vivo. For
this reason, 15 male rats were classified into five groups. First group, considered
as control, was given only deionized water. Other groups were exposed daily to
the different concentrations of nontoxic (0.87, 3 ppm) and toxic (30 and 300 pmm)
iron with drinking water for 100 days. Then, the expression of G6pd, 6pgd, and
Gr were examined by real time PCR in rat spleen. Enzymatic activities of those
genes were spectroscopically examined. According to our results, iron overload reduced
the gene expression of G6pd, 6pgd, and Gr. The G6PD enzyme activity was
significantly decreased in the presence of non-toxic and toxic iron concentrations.
However, the 6PGD enzyme activity was increased in the presence of 3, 30, and
300 ppm iron. While the enzymatic activity of GR in the presence of nontoxic iron
was activated, no changes were seen in the presence of toxic iron concentrations.
Keywords: Iron overload, Oxidative stress, Gene expression, Enzyme activity,