Journal
RSC ADVANCES
Volume 4, Issue 109, Pages 64032-64042Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c4ra11502c
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Funding
- National Natural Science Foundation of China [31272626]
- International (Regional) Cooperation and Exchange Projects of the National Natural Science Foundation of China [31320103920]
- Doctoral Fund of the Ministry of Education of China [20122325110018]
- Key Laboratory of Myocardial Ischemia, Harbin Medical University
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The aim of the present study was to examine the role of Selenoprotein W (Sepw1) in modulating the expression of other selenoproteins. In the present study, we silenced and overexpressed the expression of Sepw1 in chicken myoblasts and subsequently treated the myoblasts with a reactive oxygen species (ROS) scavenger, N-acetyl-L-cysteine (NAC), and H2O2. Thereafter, the levels of expression of 25 selenoproteins and the activities of certain antioxidative enzymes, glutathione peroxidase (Gpx), superoxide dismutase (SOD), and catalase (CAT) were analyzed. In addition, principal component analysis (PCA) was used to define the most important parameters that could be used as key factors. The results indicated that as a highly expressed selenoprotein (only lower than Gpx1, Selk, Sels and Sep15), Sepw1 could interact with H2O2 (P < 0.05) and influence the expression of some selenoproteins (Gpx3, Gpx4, Txnrd1, Selt, Selh, Sepp1, Sels and Sep15, P < 0.05) and the sensitivity of the cells to H2O2. Both the overexpression and silencing of Sepw1 influenced the mRNA levels of selenoproteins. However, the responses of selenoproteins to altered Sepw1 expression were different. The results indicated that Sepw1 played a special role in H2O2 metabolism and may modulate the expression of certain selenoproteins through the redox pathway. Therefore, these results indicate that Sepw1 is an essential antioxidative selenoprotein in chicken myoblasts.
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