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- W2076071322 abstract "Plasma glutathione peroxidase (GPx-3) is a selenocysteine-containing extracellular antioxidant protein that catalyzes the reduction of hydrogen peroxide and lipid hydroperoxides. Selenoprotein expression involves the alternate recognition of a UGA codon as a selenocysteine codon and requires signals in the 3′-untranslated region (UTR), including a selenocysteine insertion sequence (SECIS), as well as specific translational cofactors. To ascertain regulatory determinants of GPx-3 expression and function, we generated recombinant GPx-3 (rGPX-3) constructs with various 3′-UTR, as well as a Sec73Cys mutant. In transfected Cos7 cells, the Sec73Cys mutant was expressed at higher levels than the wild type rGPx-3, although the wild type rGPx-3 had higher specific activity, similar to plasma purified GPx-3. A 3′-UTR with only the SECIS was insufficient for wild type rGPx-3 protein expression. Selenocompound supplementation and co-transfection with SECIS binding protein 2 increased wild type rGPx-3 expression. These results demonstrate the importance of translational mechanisms in GPx-3 expression." @default.
- W2076071322 created "2016-06-24" @default.
- W2076071322 creator A5021018955 @default.
- W2076071322 creator A5028396638 @default.
- W2076071322 creator A5041785566 @default.
- W2076071322 creator A5056138634 @default.
- W2076071322 date "2009-02-15" @default.
- W2076071322 modified "2023-10-16" @default.
- W2076071322 title "Regulation of the extracellular antioxidant selenoprotein plasma glutathione peroxidase (GPx-3) in mammalian cells" @default.
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- W2076071322 doi "https://doi.org/10.1007/s11010-009-0049-x" @default.
- W2076071322 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2693281" @default.
- W2076071322 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19219623" @default.
- W2076071322 hasPublicationYear "2009" @default.
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