Abstract

<p>The serum sodium iodide is transported into the thyrocyte and then iodine is incorporated into the thyroglobulin molecule (Tg) in a reaction catalyzed by the hemoprotein thyroid peroxidase (TPO). In this reaction, H<sub>2</sub>O<sub>2</sub> generated by the NADPH-dependent thyroxidase (ThOx) is required as substrate by TPO for the iodination and coupling of tyrosyl residues in Tg. Then, thyroid hormones triiodothyronine (T3) and tetraiodothyronine (T4) are released into the bloodstream. H<sub>2</sub>O<sub>2</sub> used in this reaction decreases the amount of H<sub>2</sub>O<sub>2</sub> that would otherwise be available for damaging oxidation reactions. Selenium-dependent glutathione peroxidase 1 (<i>GPX 1</i>) and other GPX s remove H<sub>2</sub>O<sub>2</sub> from the tissues, also decreasing oxidative damage. (Modified from: J. Köhrle <i>et al</i>. Selenium, the thyroid, and the endocrine system. Endocrine Reviews, December 2005, 26(7):944–984; Lyn Patrick, ND. Iodine: deficiency and therapeutic considerations. Alternative Medicine Review, 2008, 13(2):116–127).</p

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