Selenoprotein T is a PACAP‐regulated gene involved in intracellular Ca<sup>2+</sup>mobilization and neuroendocrine secretion

Grumolato, Luca; Ghzili, Hafida; Montero-Hadjadje, Maïté; Gasman, Stéphane; Lésage, Jean; Tanguy, Yannick; Galas, Ludovic; Aït-Ali, Djida; Leprince, Jérôme; Guérineau, Nathalie C.; Elkahloun, Abdel G.; Fournier, Alain; Vieau, Didier; Vaudry, Hubert; Anouar, Youssef

doi:10.1096/fj.06-075820

Cited by 128 publications

(122 citation statements)

References 52 publications

Supporting

Mentioning

115

Contrasting

Unclassified

Order By: Relevance

“…114 Altogether these observations suggest an important role for SelT in ontogenesis, tissue maturation/regeneration, and cellular metabolism of nervous and endocrine tissue, with a possible redox action in Ca 2+ homeostasis. 113 Structural analogies characterize SelT and SelW, indicating a potential functional relation, supported by the observation that knockdown of SelT in mouse fibroblasts may be compensated by increased expression of SelW. 116 4.9.…”

Section: Selenoprotein Tmentioning

confidence: 93%

“…112 In mouse and rat cells it localizes in Golgi, ER and possibly in the plasma membrane. 100,113 It is ubiquitously distributed, with high expression in the testes. 58 The expression of SelT is regulated by the trophic neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP).…”

Section: Selenoprotein Tmentioning

confidence: 99%

“…58 The expression of SelT is regulated by the trophic neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP). 113,114 Elevated expression was found in embryonic tissues, followed by a decrease in most adult tissues, excluding the pituitary gland, thyroid and testis. 114 SelT was found to be highly expressed also in the brain of hypoxia-induced mice 115 and in regenerating liver cells after partial hepatectomy.…”

Section: Selenoprotein Tmentioning

confidence: 99%

See 2 more Smart Citations

Selenium biochemistry and its role for human health

Roman¹,

Jitaru²,

Barbante³

2014

Metallomics

605

451

View full text Add to dashboard Cite

Despite its very low level in humans, selenium plays an important and unique role among the (semi)metal trace essential elements because it is the only one for which incorporation into proteins is genetically encoded, as the constitutive part of the 21st amino acid, selenocysteine. Twenty-five selenoproteins have been identified so far in the human proteome. The biological functions of some of them are still unknown, whereas for others there is evidence for a role in antioxidant defence, redox state regulation and a wide variety of specific metabolic pathways. In relation to these functions, the selenoproteins emerged in recent years as possible biomarkers of several diseases such as diabetes and several forms of cancer. Comprehension of the selenium biochemical pathways under normal physiological conditions is therefore an important requisite to elucidate its preventing/therapeutic effect for human diseases. This review summarizes the most recent findings on the biochemistry of active selenium species in humans, and addresses the latest evidence on the link between selenium intake, selenoproteins functionality and beneficial health effects. Primary emphasis is given to the interpretation of biochemical mechanisms rather than epidemiological/observational data. In this context, the review includes the following sections: (1) brief introduction; (2) general nutritional aspects of selenium; (3) global view of selenium metabolic routes; (4) detailed characterization of all human selenoproteins; (5) detailed discussion of the relation between selenoproteins and a variety of human diseases.

show abstract

Section: Selenoprotein Tmentioning

confidence: 93%

Section: Selenoprotein Tmentioning

confidence: 99%

Section: Selenoprotein Tmentioning

confidence: 99%

See 1 more Smart Citation

Selenium biochemistry and its role for human health

Roman¹,

Jitaru²,

Barbante³

2014

Metallomics

605

451

View full text Add to dashboard Cite

show abstract

“…In addition, the loss of SelT resulted in the upregulation of several oxidoreductase genes, including another member of the Rdx family, SelW. In a recent study, SelT was identified as a target of the neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP) (121). Overexpression of SelT in PC12 cells resulted in an increase of the intracellular Ca 2ϩ levels, whereas knockdown of SelT inhibited PACAPstimulated release of Ca 2ϩ from the ER and reduced growth hormone secretion.…”

Section: F Selenoproteins W T H and Vmentioning

confidence: 99%

Selenoproteins: Molecular Pathways and Physiological Roles

Labunskyy

Hatfield

Gladyshev³

2014

Physiological Reviews

999

850

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

“…The specific interactions between Sec and Ca 2+ are of particular relevance because, besides the different roles mentioned above for Ca 2+ , it seems that the key proteins in cell protection against oxidative stress 21 and those which usually participate in the regulation of intracellular Ca 2+ concentration 22 are Sec-containing proteins. In this paper we aim at investigating the preferential way in which Ca 2+ binds to Sec, and at analyzing the effects produced by the doublycharged metal ion on the electron density of the amino acid and on its intrinsic properties, in particular on its propensity to get deprotonated.…”

mentioning

confidence: 99%