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The human selenoprotein family consists of 25 proteins that incorporate the trace element selenium in the form of the amino acid selenocysteine (UniProt: P49908, Q9BQE3). These proteins are essential for various physiological processes, primarily acting as enzymes (oxidoreductases) that manage cellular redox balance and protect against oxidative damage (Labunskyy et al., 2014). Selenoprotein P (SELENOP) serves as the major selenium transport protein in the plasma and is a key biomarker for selenium status, with links to insulin resistance and metabolic syndrome (PubMed: 30107219). Selenoprotein N (SELENON) is localized in the endoplasmic reticulum and is critical for calcium regulation and muscle function; its deficiency leads to Selenoprotein N-related myopathy (NCBI: GeneID 57190). Selenoprotein K (SELENOK) plays a role in immune cell activation and the endoplasmic reticulum-associated degradation (ERAD) pathway (Reeves & Hoffmann, 2009). Therapeutically, these proteins are targeted through selenium supplementation to boost antioxidant defenses in cancer and cardiovascular disease, or through mimetics like ebselen (PubChem: CID 3194). However, the narrow therapeutic index of selenium requires careful monitoring to avoid toxicity or unintended metabolic consequences like selenosis.
Enhancement of selenoprotein biosynthesis through selenium supplementation or direct redox modulation by selenium mimetics (PubMed: 24510460).
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