Selenoproteins of the thyroid gland: expression, localization and possible function of glutathione peroxidase 3

Cornelia Schmutzler 1 , 1 , Birgit Mentrup 2 , 2 , Lutz Schomburg 3 , 3 , Cuong Hoang-Vu 4 , 4 , Volker Herzog 5 , 5 ,  und Josef Köhrle 6 , 6
  • 1 Institut für Experimentelle Endokrinologie, Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany
  • 2 Institut für Experimentelle Endokrinologie, Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany and present address: Max-Planck-Institut für Molekulare Genetik, Fabeckstr. 60-62, D-14195 Berlin, Germany.
  • 3 Institut für Experimentelle Endokrinologie, Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany
  • 4 Experimentelle und Chirurgische Onkologie, Martin-Luther-Universität Halle/Wittenberg, Magdeburger Str. 18, D-06097 Halle/Saale, Germany
  • 5 Institut für Zellbiologie, Rheinische Friedrich-Wilhelms-Universität, Ulrich-Haberland-Str. 61a, D-53121 Bonn, Germany
  • 6 Institut für Experimentelle Endokrinologie, Charité – Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany

Abstract

The thyroid gland has an exceptionally high selenium content, even during selenium deficiency. At least 11 selenoproteins are expressed, which may be involved in the protection of the gland against the high amounts of H2O2 produced during thyroid hormone biosynthesis. As determined here by in situ hybridization and Northern blotting experiments, glutathione peroxidases (GPx) 1 and 4 and selenoprotein P were moderately expressed, occurring selectively in the follicular cells and in leukocytes of germinal follicles of thyroids affected by Hashimoto's thyroiditis. Selenoprotein 15 was only marginally expressed and distributed over all cell types. GPx3 mRNA was exclusively localized to the thyrocytes, showed the highest expression levels and was down-regulated in 5 of 6 thyroid cancer samples as compared to matched normal controls. GPx3 could be extracted from thyroidal colloid by incubation with 0.5% sodium dodecyl sulfate indicating that this enzyme is (i) secreted into the follicular lumen and (ii) loosely attached to the colloidal thyroglobulin. These findings are consistent with a role of selenoproteins in the protection of the thyroid from possible damage by H2O2. Particularly, GPx3 might use excess H2O2 and catalyze the polymerization of thyroglobulin to the highly cross-linked storage form present in the colloid.

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Biological Chemistry keeps you up-to-date with the latest advances in the molecular life sciences. The journal publishes Research Articles, Short Communications, Reviews and Minireviews. Areas include: general biochemistry/pathobiochemistry, structural biology, molecular and cellular biology, genetics and epigenetics, virology, molecular medicine, plant molecular biology/biochemistry and novel experimental methodologies.

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