Evidence that type III iodothyronine deiodinase in rat astrocyte is a selenoprotein.

Ramaugé, Martine; Pallud, Sophie; Esfandiari, Ali; Gavaret, Jean‐Michel; Lennon, Ana Maria; Martineau, Pierre; Courtin, Françoise

doi:10.1210/endo.137.7.8770927

Cited by 40 publications

(22 citation statements)

References 26 publications

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“…Although differences in the rates of turnover of these proteins may be responsible in part for these observations, the results support the emerging concept that there is a hierarchy of expression of selenoproteins within a given cell or tissue (49,50). We have previously reported similar preferential expression of DIII after selenium repletion of glial cells (51). The mechanisms responsible for this differential utilization of selenium within the cell remain poorly defined, but could be secondary to selective alterations in selenoprotein mRNA levels induced by selenium deficiency (52)(53)(54) or differences in the translational efficiency of deiodinase versus GPx mRNAs.…”

Section: Discussionsupporting

confidence: 77%

Expression of the Type II Iodothyronine Deiodinase in Cultured Rat Astrocytes Is Selenium-dependent

Pallud¹,

Lennon²,

Ramaugé³

et al. 1997

Journal of Biological Chemistry

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The iodothyronine deiodinases are a family of selenoproteins that metabolize thyroxine and other thyroid hormones to active and inactive metabolites in a number of tissues including brain. Using primary cultures of rat astroglial cells as a model system, we demonstrate that the mRNA for the type II iodothyronine deiodinase (DII) selenoenzyme is rapidly and markedly induced by forskolin and 8-bromo-cAMP. The induction of DII activity, however, was significantly impaired by culturing cells in selenium-deficient medium for 7 days. Under such conditions, the addition of selenium resulted in a rapid increase in cAMP-induced DII activity that was dose-dependent, with maximal effects noted within 2 h. Cycloheximide blocked this effect of selenium on restoring cAMP-induced DII activity, whereas actinomycin D did not. These data demonstrate that the DII selenoenzyme is expressed in cultured astrocytes and that the induction of DII activity by cAMP analogues appears to be mediated, at least in part, by pretranslational mechanisms. Furthermore, selenium deprivation impairs the expression of DII activity at the level of translation.Recent molecular cloning studies have identified cDNAs that code for a family of structurally related iodothyronine deiodinases (1-4). These oxidoreductases catalyze the removal of iodide from the phenolic (5Ј-position) or the tyrosyl (5-position) ring of thyroxine (T 4 ) 1 to form the active compound 3,5,3Ј-triiodothyronine (T 3 ) or the inactive metabolite 3,3Ј,5Ј-triiodothyronine, respectively (5). Based on both their unique functional properties and the structural information derived from cDNA sequences, three isoforms designated type I, II, and III iodothyronine deiodinases (DI, DII, and DIII, respectively) have been identified.The cDNAs for all three deiodinase isoforms contain within their coding regions an in-frame TGA triplet that has been demonstrated to code for the uncommon amino acid selenocysteine (1, 2, 4, 6, 7). This residue plays an essential role in the function of these enzymes; mutagenesis of the TGA triplet to a cysteine codon markedly reduces catalytic activity (1-3). It thus appears that the more potent nucleophilic capability of selenium, as compared with sulfur, is required for efficient deiodination. This thesis has been underscored by the identification of cDNAs coding for homologues of these enzymes from several fish, amphibian, and mammalian species (3, 8 -10). All such cDNAs isolated to date have demonstrated strict conservation of the active-site selenocysteine codon.Complementary DNAs that code for DII from Rana catesbeiana (3), rat (designated rBAT1-1), and human have been identified most recently (4). The proteins coded by these cDNAs are highly conserved; rBAT1-1 DII demonstrates 73 and 87% amino acid identity to the R. catesbeiana and human homologues, respectively. In addition, expression studies have demonstrated that these enzymes manifest all of the unique characteristics of DII (3, 4, 7).Evidence that the rBAT1-1 DII cDNA and its human and amphibian homo...

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Section: Discussionsupporting

confidence: 77%

Expression of the Type II Iodothyronine Deiodinase in Cultured Rat Astrocytes Is Selenium-dependent

Pallud¹,

Lennon²,

Ramaugé³

et al. 1997

Journal of Biological Chemistry

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“…Even though there is an increased requirement for selenium during pregnancy, decreased selenium levels during this physiological stage have previously been reported [37]. Similar to previous animal studies, our study also showed that the placental D3 expression level was not affected by the maternal serum selenium level [16,17,38].…”

Section: Discussionsupporting

confidence: 90%

Na+/I− Symporter and Type 3 Iodothyronine Deiodinase Gene Expression in Amniotic Membrane and Placenta and Its Relationship to Maternal Thyroid Hormones

Aktürk

Oruç

Danışman

et al. 2013

Biol Trace Elem Res

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Placental type 3 iodothyronine deiodinase (D3) potentially protects the fetus from the elevated maternal thyroid hormones. Na− symporter (NIS) is a plasma membrane glycoprotein, which mediates active iodide uptake. Our objectives were to establish the distribution of NIS and D3 gene expressions in the placenta and the amniotic membrane and to investigate the relationship between placental D3 and NIS gene expressions and maternal iodine, selenium, and thyroid hormone status. Thyroid hormones, urinary iodine concentration (UIC), and selenium levels were measured in 49 healthy term pregnant women. NIS and D3 gene expressions were studied with the total mRNA RT-PCR method in tissues from maternal placenta (n=49), fetal placenta (n=9), and amniotic membrane (n=9). NIS and D3 gene expressions were shown in the fetal and maternal sides of the placenta and amniotic membrane. Mean blood selenium level was 66±26.5 μg/l, and median UIC was 143 μg/l. We could not demonstrate any statistically significant relationship of spot UIC and blood selenium with NIS and D3 expression (p>0.05). Positive correlations were found between NIS and thyroxine-binding globulin (TBG) (r=0.3, p=0.042) and between D3 and preoperative glucose levels (r=0.4, p=0.006). D3 and NIS genes are expressed in term placenta and amniotic membrane; thus, in addition to placenta, amniotic membrane contributes to regulation of maternofetal iodine and thyroid hormone transmission. Further studies are needed to clarify the relationship between maternal glucose levels and placental D3 expression and between TBG and placental NIS expression.

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“…Chu et al (1999) found that the addition of RA increased the expression of GPX2 mRNA in a human mammary cell line, and other in vitro studies have shown that RA increased the activity of iodothyronine deiodinases (ID1 and ID3) in cell systems (Ramauge et al 1996;Menth et al 2005). However, very little data is available to explore the effects of RA on the bovine mammary epithelial cells (BMEC).…”

Section: Introductionmentioning

confidence: 99%

Effects of retinoic acid on the synthesis of selenoprotein and the antioxidative indices of bovine mammary epithelial cells in vitro

Jin¹,

Yan²,

Shi³

et al. 2016

CZECH J ANIM SCI

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The present study was conducted to examine the effects of retinoic acid (RA) on the synthesis of selenoprotein and the antioxidative indices of bovine mammary epithelial cells (BMEC) in vitro and to explore the antioxidative mechanisms of RA in the BMEC. The subconfluenced BMEC were divided into six treatments with six replicates per treatment and cultured in a Dulbecco's Modified Eagle's Medium/F12 media (10% fetal bovine serum, 5 µg/ml ovine prolactin, 10 ng/ml epidermal growth factor, 1 g/ml hydrocortisone, 0.5% insulin-transferrin-selenium) containing different levels of RA (0 (control), 0.05, 0.1, 0.2, 1 or 2 mg/ml) for 24 h. Addition of RA promoted the proliferation of BMEC, increased the activities of catalase, superoxide dismutase, total antioxidant capacity, glutathione peroxidase (GPX), thioredoxin reductase (TRXR), and the content of selenoprotein P (SELP) in a dose-dependent manner (P < 0.05). The optimal RA dose was 1 μg/ml. However, positive effect of RA tended to be suppressed when RA was increased to 2 μg/ml. The expressions of mRNA and protein of GPX in BMEC were up-regulated by RA in a quadratic dose-response relationship (P < 0.01), and the addition of 1 μg/ml RA showed the best effect. The mRNA expressions of TRXR1 and SELP as well as the protein expression of TRXR1 were higher at 1-2 μg/ml RA. These results suggested that RA promoted antioxidant function of BMEC by regulating the synthesis of selenoprotein including GPX, TRXR, and SELP in vitro. Keywords: vitamin A; antioxidant function; dairy cowsList of abbreviations: BMEC = bovine mammary epithelial cells, NO = nitric oxide, VA = vitamin A, GPX = glutathione peroxidase, TRXR = thioredoxin reductase, ROS = reactive oxygen species, MDA = malondialdehyde, SELP = selenoprotein P, RA = retinoic acid, ID = iodothyronine deiodinases, BW = body weight, DMEM = Dulbecco's Modified Eagle's Medium, DMSO = dimethyl sulfoxide, MTT = methyl thiazolyl tetrazolium, DTNB = dithio-bis-nitrobenzoic acid, GAPDH = glyceraldehyde phosphate dehydrogenase, SOD = superoxide dismutase, CAT = catalase, T-AOC = total antioxidant capacity, iNOS = inducible nitric oxide synthase, MAPK = mitogen-activated protein kinase, RT = reverse transcriptase, RT-PCR = real-time polymerase chain reaction, PBS = phosphate buffered solution

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Evidence that type III iodothyronine deiodinase in rat astrocyte is a selenoprotein.

Cited by 40 publications

References 26 publications

Expression of the Type II Iodothyronine Deiodinase in Cultured Rat Astrocytes Is Selenium-dependent

Expression of the Type II Iodothyronine Deiodinase in Cultured Rat Astrocytes Is Selenium-dependent

Na+/I− Symporter and Type 3 Iodothyronine Deiodinase Gene Expression in Amniotic Membrane and Placenta and Its Relationship to Maternal Thyroid Hormones

Effects of retinoic acid on the synthesis of selenoprotein and the antioxidative indices of bovine mammary epithelial cells in vitro

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