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Selenium, the Thyroid, and the Endocrine System

Institut für Experimentelle Endokrinologie (J.K.), Charité Universitätsmedizin Berlin, Humboldt Universität, D-10098 Berlin, Germany; Experimentelle und Klinische Osteologie (F.J.), Orthopädische Universitätsklinik, D-97074 Würzburg, Germany; and Institut de Recherche Interdisciplinaire en Biologie Humaine et Moléculaire (B.C., J.E.D.), Université Libre de Bruxelles, Campus Hopital Erasme, B-1070 Bruxelles, Belgium

Correspondence: Address all correspondence and requests for reprints to: Prof. Dr. Josef Köhrle, Institut für Experimentelle Endokrinologie, Charité, Humboldt Universität zu Berlin, Schumannstrasse 20/21, D-10098 Berlin, Germany. E-mail: josef.koehrle{at}charite.de

Recent identification of new selenocysteine-containing proteins has revealed relationships between the two trace elements selenium (Se) and iodine and the hormone network. Several selenoproteins participate in the protection of thyrocytes from damage by H₂O₂ produced for thyroid hormone biosynthesis. Iodothyronine deiodinases are selenoproteins contributing to systemic or local thyroid hormone homeostasis. The Se content in endocrine tissues (thyroid, adrenals, pituitary, testes, ovary) is higher than in many other organs. Nutritional Se depletion results in retention, whereas Se repletion is followed by a rapid accumulation of Se in endocrine tissues, reproductive organs, and the brain. Selenoproteins such as thioredoxin reductases constitute the link between the Se metabolism and the regulation of transcription by redox sensitive ligand-modulated nuclear hormone receptors. Hormones and growth factors regulate the expression of selenoproteins and, conversely, Se supply modulates hormone actions. Selenoproteins are involved in bone metabolism as well as functions of the endocrine pancreas and adrenal glands. Furthermore, spermatogenesis depends on adequate Se supply, whereas Se excess may impair ovarian function. Comparative analysis of the genomes of several life forms reveals that higher mammals contain a limited number of identical genes encoding newly detected selenocysteine-containing proteins.

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