title: Selenoenzyme expression in thyroid and liver of second generation selenium- and iodine-deficient rats.
abstract: The stimulation of thyroid hormone synthesis in iodine deficiency may increase the requirement for the selenoproteins which are involved in thyroid hormone synthesis in the thyroid gland. Selenoenzyme activity and expression were investigated in the thyroid and liver of second generation selenium-and/or iodine-deficient rats. Selenium deficiency caused substantial decreases in hepatic selenium-containing type I iodothyronine deiodinase (ID-I) and cytosolic glutathione peroxidase (cGSHPx) activities and mRNA abundances, but phospholipid hydroperoxide glutathione peroxidase (phGSHPx) activity was only 55% of selenium-supplemented control levels, despite the absence of change in its mRNA abundance. Selenoenzyme mRNA concentrations were maintained at control levels in thyroid glands from the selenium-deficient rat pups. Despite this, a differential effect was observed in selenoenzyme activities: ID-I activity was decreased to 61%, cGSHPx activity to 45% and phGSHPx to 29% of that in selenium-adequate controls. In iodine-deficient thyroid glands, mRNA levels were increased 2.2, 5.0 and 2.8 times for ID-I, cGSHPx and phGSHPx respectively. ID-I and cGSHPx enzyme activities were also increased but the activity of phGSHPx was decreased despite the high mRNA abundance. Thyroid selenoprotein mRNA levels were also increased in combined selenium and iodine deficiency but again there were differential effects on enzyme activities, with ID-I activity increased, cGSHPx unchanged and phGSHPx decreased. Thus, iodine deficiency may produce an oxidant stress on the thyroid gland, increasing the requirement for selenium to maintain selenoenzyme activity. When dietary supplies of selenium are limiting, thyroid selenoprotein mRNA levels are increased to compensate for overall lack of the micronutrient. Furthermore, there is a preferential supply of available selenium to ID-I and cGSHPx to allow maintenance of thyroid function.
authors.affiliation: Rowett Research Institute, Bucksburn, Aberdeen, UK.
authors.forename: J H
authors.initials: JH
authors.lastname: Mitchell
authors.forename: F
authors.initials: F
authors.lastname: Nicol
authors.forename: G J
authors.initials: GJ
authors.lastname: Beckett
authors.forename: J R
authors.initials: JR
authors.lastname: Arthur
mesh_terms: D000375:Aging; D000818:Animals; D003433:Crosses, Genetic; D015342:DNA Probes; D018076:DNA, Complementary; D005260:Female; D015971:Gene Expression Regulation, Enzymologic / Q000187:drug effects; D005979:Glutathione Peroxidase / Q000096:biosynthesis*; D007453:Iodide Peroxidase / Q000096:biosynthesis*; D007455:Iodine / Q000172:deficiency* / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D008297:Male; D009929:Organ Size; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D014176:Protein Biosynthesis; D011506:Proteins; D012333:RNA, Messenger / Q000096:biosynthesis; D051381:Rats; D011919:Rats, Inbred Strains; D011995:Recombination, Genetic; D012643:Selenium / Q000172:deficiency* / Q000494:pharmacology; D051140:Selenoproteins; D013961:Thyroid Gland / Q000033:anatomy & histology / Q000201:enzymology* / Q000254:growth & development; D013972:Thyrotropin / Q000097:blood; D013974:Thyroxine / Q000097:blood; D014158:Transcription, Genetic / Q000187:drug effects; D014284:Triiodothyronine / Q000097:blood
chemical_list: D015342:DNA Probes; D018076:DNA, Complementary; D011506:Proteins; D012333:RNA, Messenger; D051140:Selenoproteins; D014284:Triiodothyronine; D013972:Thyrotropin; D007455:Iodine; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D007453:Iodide Peroxidase; D005979:Glutathione Peroxidase; D012643:Selenium; D013974:Thyroxine