Modulation of protein oxidation by Genistein, Quercetin and Gluthathione in Hemoglobin/Myoglobin and in 3T3-L1 Cells
Abstract
Extensive literature research on various antioxidant effects on proteins suggests that antioxidants prevent the oxidation of proteins, DNA, lipids, cholesterol and carbohydrate. This antioxidant effect has been hypothesized to reduce the risk of cancer by preventing cell damage, mutations and subsequent uncontrolled cell growth. This study focuses on the antioxidant activity of flavonoids quercetin, kampferol and genistein and the tripeptide Glutathione (GSH) when administered at different dosage levels to hemoglobin, myoglobin and 3T3-L1 preadipocytes cells. Different dosages of 0-25μM, dissolved in DMSO, were administered to protein and cell samples in increasing increments of 5μM. Proteins and cells were treated with each flavonoid separately and in combination and oxidized by the Fenton's pathway, and incubated in a water bath at 37°C for 24 hours. 3T3-L1 cells treated with the same antioxidants were also incubated in an incubator at 37°C with 5% CO 2 for 24 hours. The levels of arginine and lysine residues were analyzed for the hemoglobin/myoglobin treated samples. Both flavonoids are shown to decrease lysine, arginine and thiol residue oxidation in all 24hr incubations. Similar results were observed in cells when treated with each flavonoid. Levels of GSH in cells appear to be enhanced after 24hr treatments. The addition of exogenous glutathione did not show noticeable change in intracellular GSH levels. The results indicate that both quercetin and genistein were potent in reducing protein oxidation.
Subject Area
Cellular biology|Biochemistry|Oncology
Recommended Citation
Paul K Amartey,
"Modulation of protein oxidation by Genistein, Quercetin and Gluthathione in Hemoglobin/Myoglobin and in 3T3-L1 Cells"
(2014).
ETD Collection for Tennessee State University.
Paper AAI1584207.
https://digitalscholarship.tnstate.edu/dissertations/AAI1584207