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Biochim Biophys Acta. 2013 Apr;1830(4):3112-20. doi: 10.1016/j.bbagen.2013.01.007. Epub 2013 Jan 15.

Selenoprotein W serves as an antioxidant in chicken myoblasts.

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  • 1Department of Veterinary Medicine, Northeast Agricultural University, Harbin 150030, P. R. China.

Abstract

BACKGROUND:

Selenoprotein W (SelW) was thought to play an antioxidant role in mammals. Because chicken SelW has no cysteine (Cys) at the residue 37 (Cys37) that is required for the presumed antioxidant function in mammals, this study was conducted to determine whether chicken SelW possessed the same function.

METHODS:

Small interfering RNAs (siRNAs) technology was applied to suppress the SelW expression in chicken embryonic myoblasts. Thereafter, these myoblasts were treated with different concentrations of H2O2 and assayed for cell viability, apoptosis rate, reactive oxygen species (ROS) status, and expression levels of apoptosis-related genes and proteins (Bax, Bcl-2, and caspase-3).

RESULTS:

Silencing of the myoblast SelW gene decreased their cell viability, and increased their apoptosis rate and susceptibility to H2O2. While the knockout down of SelW up-regulated Bax and caspase-3 and down-regulated Bcl-2, the induced oxidative injuries were alleviated by treatment with a ROS scavenger, N-acetyl-l-cysteine (NAC).

CONCLUSION:

Chicken SelW protected embryonic myoblasts against cell apoptosis mediated by endogenous and exogenous H2O2.

GENERAL SIGNIFICANCE:

Chicken SelW possesses antioxidant function similar to the mammalian homologues despite the lack of Cys37 in the peptide.

PMID:
23333634
DOI:
10.1016/j.bbagen.2013.01.007
[PubMed - indexed for MEDLINE]
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