Identification of type I iodothyronine 5′-deiodinase as a selenoenzyme

Behne, D.; Kyriakopoulos, Antonios; Meinhold, H.; Köhrle, Josef

doi:10.1016/s0006-291x(05)80905-2

Cited by 372 publications

(129 citation statements)

References 17 publications

Supporting

Mentioning

115

Contrasting

Unclassified

Order By: Relevance

“…Selenium status also plays a role in thyroid function because the three iodothyronine deiodinases that catalyze conversions of thyroxine to triiodo-and diiodothyronines have been identi®ed as selenoproteins (Arthur et al, 1990;Behne et al, 1990;Salvatore et al, 1996). Pronounced changes in thyroid hormone metabolism occur in experimental selenium de®ciency, but the functional effects of Figure 5 The correlation between selenium and TSH in plasma (r 7 0.30, P 0.01).…”

Section: Discussionmentioning

confidence: 99%

Plasma levels of selenium, selenoprotein P and glutathione peroxidase and their correlations to fish intake and serum levels of thyrotropin and thyroid hormones: A study on Latvian fish consumers

et al. 1998

View full text Add to dashboard Cite

Objective: To study the relationships between ®sh intake and different markers of selenium status and thyroid hormone function. Design: Cross-sectional study. Setting and subjects: Sixty-eight men (age 24±79 years) were recruited among coastal ®shermen and inland subjects from Latvia. None of the subjects was on selenium medication or had any known endocrine disease. Main outcome measures: Correlations between ®sh intake, plasma levels of selenium, selenoprotein P, glutathione peroxidase, organic mercury in erythrocytes and TSH in serum. Results: Selenium in plasma ranged from 0.30 to 1.56 mmola1, selenoprotein P from 0.54 to 2.21 arbitrary units relative to pooled plasma, and glutathione peroxidase from 1.20 to 5.73 mga1. The number of ®sh meals per month was correlated with plasma selenium, selenoprotein P and glutathione peroxidase (r 0.63, r 0.62 and r 0.50, respectively; P`0.001). Plasma selenium was correlated with selenoprotein P and glutathione peroxidase (r 0.88 and r 0.67, respectively; P`0.001), and also selenoprotein P and glutathione peroxidase were correlated (r 0.63, P`0.001). The mean plasma selenium level in those with a high ®sh intake (21±50 ®sh mealsamonth), was 81% higher than in those with lowest ®sh intake. TSH in serum was inversely correlated with plasma selenium and selenoprotein P. Thyroid hormone levels were not correlated with plasma selenium, selenoproteins or ®sh intake. Conclusions: In this study group, selenium from ®sh intake had a marked impact on all variables studied on selenium status. No impact of selenium status on T3 and T4 levels was observed. The slightly negative correlation of selenium status with TSH levels might indicate a higher TSH secretion at low selenium status.

show abstract

Section: Discussionmentioning

confidence: 99%

Plasma levels of selenium, selenoprotein P and glutathione peroxidase and their correlations to fish intake and serum levels of thyrotropin and thyroid hormones: A study on Latvian fish consumers

et al. 1998

View full text Add to dashboard Cite

show abstract

“…During the early stages of selenoprotein research, identification of selenoproteins was largely dependent on experimental approaches, which included analyses of proteins for the presence of Se by mass spectrometry and detection of radioactive 75 Se that was metabolically incorporated into proteins in the form of Sec (16,20). The first selenoprotein identified was mammalian glutathione peroxidase 1 (GPx1) (103), which was followed by the discovery of bacterial glycine reductase (353) and formate dehydrogenase (7) in 1973.…”

Section: Selenoproteins and Their Distributionmentioning

confidence: 99%

Selenoproteins: Molecular Pathways and Physiological Roles

Labunskyy

Hatfield

Gladyshev³

2014

Physiological Reviews

1,063

835

View full text Add to dashboard Cite

Selenium is an essential micronutrient with important functions in human health and relevance to several pathophysiological conditions. The biological effects of selenium are largely mediated by selenium-containing proteins (selenoproteins) that are present in all three domains of life. Although selenoproteins represent diverse molecular pathways and biological functions, all these proteins contain at least one selenocysteine (Sec), a seleniumcontaining amino acid, and most serve oxidoreductase functions. Sec is cotranslationally inserted into nascent polypeptide chains in response to the UGA codon, whose normal function is to terminate translation. To decode UGA as Sec, organisms evolved the Sec insertion machinery that allows incorporation of this amino acid at specific UGA codons in a process requiring a cis-acting Sec insertion sequence (SECIS) element. Although the basic mechanisms of Sec synthesis and insertion into proteins in both prokaryotes and eukaryotes have been studied in great detail, the identity and functions of many selenoproteins remain largely unknown. In the last decade, there has been significant progress in characterizing selenoproteins and selenoproteomes and understanding their physiological functions. We discuss current knowledge about how these unique proteins perform their functions at the molecular level and highlight new insights into the roles that selenoproteins play in human health.

show abstract

“…By reduction of hydroperoxides to the corresponding alcohols, these enzymes can prevent the production of reactive oxygen radicals and thus may contribute to the protection of the Selenium in Biology 851 Ursini et al, 1982;Brigelius-Flohé et al, 1994 Plasma GPx (pGPx, GPx-3) Takahashi et al, 1987 Gastrointestinal GPx (GI-GPx, GPx-GI, GPx-2) Chu et al, 1993 Iodothyronine deiodinases 5Ј-deiodinase, type I (5ЈDI) Behne et al, 1990;Arthur et al, 1990 5Ј-deiodinase Lee et al, 1999;Watabe et al, 1999;Miranda-Vizuete et al, 1999;Gasdaska et al, 1999 Thioredoxin reductase homologs (SelZf1; SelZf2) Lescure et al, 1999 Selenophosphate synthetase-2 Guimaraes et al, 1996 Functionally undefined 15 kDa selenoprotein of T cells Gladyshev et al, 1998 Selenoprotein P 10 (SelP) Motsenbocker and Tappel organism's macromolecules and biomembranes against oxidation (Sies et al, 1972;Flohé, 1989;Ursini et al, 1995). The role of the cytoplasmic GPx as an 'emergency enzyme' to fight oxidative stress was verified by reverse genetics (Ho et al, 1997;Cheng et al, 1998;de Haan et al, 1998;Fu et al, 1999;Jaeschke et al, 1999) and, in this role, cGPx cannot be substituted by any of the other selenoproteins.…”

Section: Metabolic Function Of Mammalian Selenoproteinsmentioning

confidence: 99%

“…The metabolic activation (Behne et al, 1990;Arthur et al, 1990;Davey et al, 1995), as well as degradation of thyroid hormones (Croteau et al, 1995), were shown to depend on selenium-containing deiodinases. Most surprisingly, selenium was also discovered in a well-documented enzyme of basic metabolic relevance, in thioredoxin reductase (Tamura and Stadtman, 1996).…”

Section: Introduction: Some Historical Landmarksmentioning

confidence: 99%

Selenium in Biology: Facts and Medical Perspectives

Köhrl¹,

Brigelius‐Flohé²,

Böck³

et al. 2000

Biological Chemistry

Self Cite

247

143

View full text Add to dashboard Cite

Several decades after the discovery of selenium as an essential trace element in vertebrates approximately 20 eukaryotic and more than 15 prokaryotic selenoproteins containing the 21 st proteinogenic amino acid, selenocysteine, have been identified, partially characterized or cloned from several species. Many of these proteins are involved in redox reactions with selenocysteine acting as an essential component of the catalytic cycle. Enzyme activities have been assigned to the glutathione peroxidase family, to the thioredoxin reductases, which were recently identified as selenoproteins, to the iodothyronine deiodinases, which metabolize thyroid hormones, and to the selenophosphate synthetase 2, which is involved in selenoprotein biosynthesis. Prokaryotic selenoproteins catalyze redox reactions and formation of selenoethers in (stress-induced) metabolism and energy production of E. coli, of the clostridial cluster XI and of other prokaryotes. Apart from the specific and complex biosynthesis of selenocysteine, selenium also reversibly binds to proteins, is incorporated into selenomethionine in bacteria, yeast and higher plants, or posttranslationally modifies a catalytically essential cysteine residue of CO dehydrogenase. Expression of individual eukaryotic selenoproteins exhibits high tissue specificity, depends on selenium availability, in some cases is regulated by hormones, and if impaired contributes to several pathological conditions. Disturbance of selenoprotein expression or function is associated with deficiency syndromes (Keshan and Kashin-Beck disease), might contribute to tumorigenesis and atherosclerosis, is altered in several bacterial and viral infections, and leads to infertility in male rodents.

show abstract

Identification of type I iodothyronine 5′-deiodinase as a selenoenzyme

Cited by 372 publications

References 17 publications

Plasma levels of selenium, selenoprotein P and glutathione peroxidase and their correlations to fish intake and serum levels of thyrotropin and thyroid hormones: A study on Latvian fish consumers

Plasma levels of selenium, selenoprotein P and glutathione peroxidase and their correlations to fish intake and serum levels of thyrotropin and thyroid hormones: A study on Latvian fish consumers

Selenoproteins: Molecular Pathways and Physiological Roles

Selenium in Biology: Facts and Medical Perspectives

Contact Info

Product

Resources

About