Assignment&lt;footref rid="foot01"&gt;&lt;sup&gt;1&lt;/sup&gt;&lt;/footref&gt; of type II iodothyronine deiodinase gene (DIO2) to human chromosome band 14q24.2→q24.3 by in situ hybridization

Araki, Osamu; Murakami, Masami; Morimura, Tadashi; Kamiya, Yûji; Hosoi, Yasuhiro; Kato, Yukari; Mori, Masatomo

doi:10.1159/000015218

Cited by 18 publications

(10 citation statements)

References 5 publications

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“…D2 is encoded by the single-copy dio2 gene located on the long arm of the 14th human chromosome in position 14q24.3 [85,86]. The coding region is divided into two exons by an~7.4-kb intron [85].…”

Section: Specific Properties Of Deiodinasesmentioning

confidence: 99%

Activation and inactivation of thyroid hormone by deiodinases: Local action with general consequences

Gereben

Zeöld

Dentice

et al. 2007

Cell. Mol. Life Sci.

180

141

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The thyroid hormone plays a fundamental role in the development, growth, and metabolic homeostasis in all vertebrates by affecting the expression of different sets of genes. A group of thioredoxin fold-containing selenoproteins known as deiodinases control thyroid hormone action by activating or inactivating the precursor molecule thyroxine that is secreted by the thyroid gland. These pathways ensure regulation of the availability of the biologically active molecule T3, which occurs in a time-and tissue-specific fashion. In addition, because cells and plasma are in equilibrium and deiodination affects central thyroid hormone regulation, these local deiodinase-mediated events can also affect systemic thyroid hormone economy, such as in the case of non-thyroidal illness. Heightened interest in the field has been generated following the discovery that the deiodinases can be a component in both the Sonic hedgehog signaling pathway and the TGR-5 signaling cascade, a G-protein-coupled receptor for bile acids. These new mechanisms involved in deiodinase regulation indicate that local thyroid hormone activation and inactivation play a much broader role than previously thought.

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Section: Specific Properties Of Deiodinasesmentioning

confidence: 99%

Activation and inactivation of thyroid hormone by deiodinases: Local action with general consequences

Gereben

Zeöld

Dentice

et al. 2007

Cell. Mol. Life Sci.

180

141

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“…The denomination of deiodinase 2 [151] (DIO2; Swissprot: q92813, also EC 1.97.1.10) as a selenoenzyme had been debated until Buettner et al showed that the functional SECIS element was present at an unusual far distance (5.4 kb) from the UGA codon in the human enzyme [101]. DIO2 is an ER-membrane protein, whose gene is at 4q24.2-q24.3 [152]. It deiodinates the 5'-position with a preference for T4 over rT3.…”

Section: Deiodinasesmentioning

confidence: 99%

Human selenoproteins at a glance

Gromer

Eubel

Lee

et al. 2005

Cell. Mol. Life Sci.

220

167

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The public perception of selenium has changed significantly over the last decades. Originally mainly known for its high toxicity, it was later recognized as an essential trace element and is now (despite its narrow therapeutic window) almost being marketed as a lifestyle drug. Indeed, some clinical and preclinical studies suggest that selenium supplementation may be beneficial in a large number of clinical conditions. However, its mode of action is unresolved in most of these cases. Selenocysteine - identified as the 21st amino acid used in ribosome-mediated protein synthesis - is incorporated in at least 25 specific, genetically determined human selenoproteins, many of which have only recently been discovered. Restoration of normal selenoprotein levels may be - apart from direct supranutritional effects - one possible explanation for the effects of selenium supplements. In this review we provide a brief but up-to-date overview of what is currently known about these 25 acknowledged human selenoproteins and their synthesis.

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“…In contrast to 5%DI, the type II 5%D prefers T4 over rT3 as substrate and is strictly a phenolic ring 5%-deiodinase with a nanomolar apparent K M for T4. The human gene encoding 5%DII has been mapped to chromosome 14q24.2-q24.3 and consists of two exons and a 7.4-kb intron [28,29]. So far no detailed information on its promoter or regulation is available.…”

Section: Multi-author Review Articlementioning

confidence: 99%

The deiodinase family: selenoenzymes regulating thyroid hormone availability and action

Köhrle¹

2000

CMLS, Cell. Mol. Life Sci.

209

100

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Thyroid hormones control growth, development, differentiation and metabolism in vertebrates. Most of the actions of the active thyroid hormone T3 (3,5,3'-triiodo-L-thyronine) are exerted via ligand-activated nuclear T3 receptors. Activation of the secretory product of the thyroid gland, L-thyroxine (3,3',5,5'-tetraiodo-L-thyronine), or T4, is catalyzed by two enzymes, iodothyronine-5'-deiodinases type I and type II. Inactivation of T4 and T3 occurs via type III iodothyronine-5-deiodinase and to some extent by type I 5'deiodinase. Complementary DNAs (cDNAs) encoding the substrate-binding selenocysteine-containing subunits of the deiodinases were cloned, though some controversy still exists on the type II 5'-deiodinase subunits. Characterization of tissue-specific expression patterns indicates that these selenium-dependent enzymes exert tight control on local and systemic availability of active T3. Thus, deiodinases are envisaged as guardians to the gate of thyroid hormone action mediated by T3 receptors.

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Assignment<footref rid="foot01"><sup>1</sup></footref> of type II iodothyronine deiodinase gene (DIO2) to human chromosome band 14q24.2→q24.3 by in situ hybridization

Cited by 18 publications

References 5 publications

Activation and inactivation of thyroid hormone by deiodinases: Local action with general consequences

Activation and inactivation of thyroid hormone by deiodinases: Local action with general consequences

Human selenoproteins at a glance

The deiodinase family: selenoenzymes regulating thyroid hormone availability and action

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