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The selenoprotein synthesis pathway is a specialized translation process responsible for the incorporation of the 21st amino acid, selenocysteine (Sec), into proteins (Labunskyy et al., 2014). Unlike standard amino acids, Sec is encoded by the UGA stop codon, requiring a unique recoding mechanism involving a cis-acting SECIS element in the mRNA 3' UTR and trans-acting factors such as SECIS-binding protein 2 (SBP2) and a specialized tRNA (Papp et al., 2007). This pathway is critical for the production of approximately 25 human selenoproteins, including glutathione peroxidases and thioredoxin reductases, which are essential for maintaining cellular redox balance and protecting against oxidative damage (Roman et al., 2014). Dysregulation of this pathway is linked to various pathologies, including cancer progression, where tumor cells often overexpress selenoproteins to survive high oxidative stress. Pharmacological modulation involves either selenium supplementation to support antioxidant capacity or the use of inhibitors like auranofin to disrupt selenoprotein function in malignant cells (Rigobello et al., 2010).
Modulation of selenium availability for selenocysteine synthesis or direct inhibition of downstream selenoprotein enzymes like thioredoxin reductase (Labunskyy et al., 2014; Rigobello et al., 2010).
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