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Selenomethionine is a naturally occurring organic selenium compound where selenium replaces the sulfur atom in the amino acid methionine. It is the primary dietary form of selenium found in plants and is highly bioavailable. In the body, selenomethionine is non-specifically incorporated into proteins in place of methionine or converted into selenocysteine for the synthesis of functional selenoproteins. These selenoproteins, including glutathione peroxidase (GPx), thioredoxin reductase, and iodothyronine deiodinases, are essential for antioxidant defense, redox signaling, and thyroid hormone metabolism. Clinically, selenomethionine has been investigated for its ability to reduce thyroid peroxidase antibody (TPOAb) titers in patients with autoimmune thyroiditis (Hashimoto's) and for its potential role in cancer chemoprevention, particularly in prostate cancer and follicular lymphoma, by mitigating oxidative DNA damage and supporting immune function.
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