A single SELENOCYSTEINE containing protein that binds reduced GLUTATHIONE and can act as an antioxidant.
Selenoproteins are proteins that specifically incorporate SELENOCYSTEINE into their amino acid chain. Most selenoproteins are enzymes with the selenocysteine residues being responsible for their catalytic functions.
An extracellular selenoprotein that contains most of the SELENIUM in PLASMA. Selenoprotein P functions as an antioxidant and appears to transport selenium from the LIVER to peripheral tissues.
An element with the atomic symbol Se, atomic number 34, and atomic weight 78.96. It is an essential micronutrient for mammals and other animals but is toxic in large amounts. Selenium protects intracellular structures against oxidative damage. It is an essential component of GLUTATHIONE PEROXIDASE.
An enzyme catalyzing the oxidation of 2 moles of glutathione in the presence of hydrogen peroxide to yield oxidized glutathione and water. EC 1.11.1.9.
A naturally occurring amino acid in both eukaryotic and prokaryotic organisms. It is found in tRNAs and in the catalytic site of some enzymes. The genes for glutathione peroxidase and formate dehydrogenase contain the TGA codon, which codes for this amino acid.
A muscular organ in the mouth that is covered with pink tissue called mucosa, tiny bumps called papillae, and thousands of taste buds. The tongue is anchored to the mouth and is vital for chewing, swallowing, and for speech.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.

Selenoprotein W is a glutathione-dependent antioxidant in vivo. (1/26)

The function of selenoprotein W (Se-W) was investigated by cloning the corresponding cDNA from mouse brain and expressing it in CHO cells and H1299 human lung cancer cells. Overexpression of Se-W markedly reduced the sensitivity of both cell lines to H2O2 cytotoxicity. The intracellular peroxide concentration of the transfected cells was lower than that of the parental cells in the absence or presence of extracellular H2O2. The resistance to oxidative stress conferred by Se-W was dependent on glutathione. Expression of Se-W mutants in which selenocysteine-13 or cysteine-37 was replaced by serine did not confer resistance to H2O2, implicating these residues in the antioxidant activity of Se-W in vivo.  (+info)

Selenoproteins and selenocysteine insertion system in the model plant cell system, Chlamydomonas reinhardtii. (2/26)

Known eukaryotic selenocysteine (Sec)-containing proteins are animal proteins, whereas selenoproteins have not been found in yeast and plants. Surprisingly, we detected selenoproteins in a member of the plant kingdom, Chlamydomonas reinhardtii, and directly identified two of them as phospholipid hydroperoxide glutathione peroxidase and selenoprotein W homologs. Moreover, a selenocysteyl-tRNA was isolated that recognized specifically the Sec codon UGA. Subsequent gene cloning and bioinformatics analyses identified eight additional selenoproteins, including methionine-S-sulfoxide reductase, a selenoprotein specific to Chlamydomonas: Chlamydomonas selenoprotein genes contained selenocysteine insertion sequence (SECIS) elements that were similar, but not identical, to those of animals. These SECIS elements could direct selenoprotein synthesis in mammalian cells, indicating a common origin of plant and animal Sec insertion systems. We found that selenium is required for optimal growth of Chlamydomonas: Finally, evolutionary analyses suggested that selenoproteins present in Chlamydomonas and animals evolved early, and were independently lost in land plants, yeast and some animals.  (+info)

Gene structure and tissue expression of human selenoprotein W, SEPW1, and identification of a retroprocessed pseudogene, SEPW1P. (3/26)

We have determined that the human SEPW1 (selenoprotein W) gene maps to chromosome 19q13.3, spans approximately 6.3 kb and comprises six exons, in contrast to the previously published five exons. The gene lacks canonical TATA and CAAT boxes, but has numerous Sp1 consensus binding sites upstream of multiple transcription start sites. SEPW1 is expressed in all of the 22 tissues assayed, and shows highest expression in skeletal muscle and heart. Additionally, we have also identified a retroprocessed SEPW1 pseudogene, SEPW1P, which maps to chromosome 1p34-35.  (+info)

Different distributions of selenoprotein W and thioredoxin during postnatal brain development and embryogenesis. (4/26)

Whereas the levels of other selenoproteins in the brain decrease when selenium is deficient, the level of selenoprotein W (Se-W) is maintained, suggesting that it has a critical role in the brain. Previously, we reported that Se-W is a GSH-dependent antioxidant [Jeong et al. (2002)]. In this study, the expression of Se-W and thioredoxin (Trx) in the brain and during embrynic development was analyzed by an in situ hybridization technique. Se-W mRNA was highly expressed in the cortex, dentate gyrus, and hippocampus of postnatal rat brains, and in the spinal cord and brain of developing embryos. In contrast, Trx mRNA was highly expressed in the cerebellum, olfactory bulb, and dentate gyrus of postnatal rat brains, and in the liver, telencephalon, and back muscle of developing embryos. Thus these two antioxidant proteins have different and non-overlapping expression patterns. The distribution of Se-W suggests that it plays an important role as an antioxidant in the developing brain and embryo.  (+info)

Selective rescue of selenoprotein expression in mice lacking a highly specialized methyl group in selenocysteine tRNA. (5/26)

Selenocysteine (Sec) is the 21st amino acid in the genetic code. Its tRNA is variably methylated on the 2'-O-hydroxyl site of the ribosyl moiety at position 34 (Um34). Herein, we identified a role of Um34 in regulating the expression of some, but not all, selenoproteins. A strain of knock-out transgenic mice was generated, wherein the Sec tRNA gene was replaced with either wild type or mutant Sec tRNA transgenes. The mutant transgene yielded a tRNA that lacked two base modifications, N(6)-isopentenyladenosine at position 37 (i(6)A37) and Um34. Several selenoproteins, including glutathione peroxidases 1 and 3, SelR, and SelT, were not detected in mice rescued with the mutant transgene, whereas other selenoproteins, including thioredoxin reductases 1 and 3 and glutathione peroxidase 4, were expressed in normal or reduced levels. Northern blot analysis suggested that other selenoproteins (e.g. SelW) were also poorly expressed. This novel regulation of protein expression occurred at the level of translation and manifested a tissue-specific pattern. The available data suggest that the Um34 modification has greater influence than the i(6)A37 modification in regulating the expression of various mammalian selenoproteins and Um34 is required for synthesis of several members of this protein class. Many proteins that were poorly rescued appear to be involved in responses to stress, and their expression is also highly dependent on selenium in the diet. Furthermore, their mRNA levels are regulated by selenium and are subject to nonsense-mediated decay. Overall, this study described a novel mechanism of regulation of protein expression by tRNA modification that is in turn regulated by levels of the trace element, selenium.  (+info)

Effects of Se-depletion on glutathione peroxidase and selenoprotein W gene expression in the colon. (6/26)

Selenium (Se)-containing proteins have important roles in protecting cells from oxidative damage. This work investigated the effects of Se-depletion on the expression of the genes encoding selenoproteins in colonic mucosa from rats fed diets of different Se content and in human intestinal Caco-2 cells grown in Se-adequate or Se-depleted culture medium. Se-depletion produced statistically significant (P<0.05) falls in glutathione peroxidase (GPX) 1 mRNA (60-83%) and selenoprotein W mRNA (73%) levels, a small but significant fall in GPX4 mRNA (17-25%) but no significant change in GPX2. The data show that SelW expression in the colon is highly sensitive to Se-depletion.  (+info)

Two major branches of anti-cadmium defense in the mouse: MTF-1/metallothioneins and glutathione. (7/26)

Metal-responsive transcription factor 1 (MTF-1) regulates expression of its target genes in response to various stress conditions, notably heavy metal load, via binding to metal response elements (MREs) in the respective enhancer/promoter regions. Furthermore, it serves a vital function in embryonic liver development. However, targeted deletion of Mtf1 in the liver after birth is no longer lethal. For this study, Mtf1 conditional knockout mice and control littermates were both mock- or cadmium-treated and liver-specific transcription was analyzed. Besides the well-characterized metallothionein genes, several new MTF-1 target genes with MRE motifs in the promoter region emerged. MTF-1 is required for the basal expression of selenoprotein W, muscle 1 gene (Sepw1) that encodes a glutathione-binding and putative antioxidant protein, supporting a role of MTF-1 in the oxidative stress response. Furthermore, MTF-1 mediates the cadmium-induced expression of N-myc downstream regulated gene 1 (Ndrg1), which is induced by several stress conditions and is overexpressed in many cancers. MTF-1 is also involved in the cadmium response of cysteine- and glycine-rich protein 1 gene (Csrp1), which is implicated in cytoskeletal organization. In contrast, MTF-1 represses the basal expression of Slc39a10, a putative zinc transporter. In a pathway independent of MTF-1, cadmium also induced the transcription of genes involved in the synthesis and regeneration of glutathione, a cadmium-binding antioxidant. These data provide strong evidence for two major branches of cellular anti-cadmium defense, one via MTF-1 and its target genes, notably metallothioneins, the other via glutathione, with an apparent overlap in selenoprotein W.  (+info)

Solution structure of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteins. (8/26)

Selenium is a trace element with significant biomedical potential. It is essential in mammals due to its occurrence in several proteins in the form of selenocysteine (Sec). One of the most abundant mammalian Sec-containing proteins is selenoprotein W (SelW). This protein of unknown function has a broad expression pattern and contains a candidate CXXU (where U represents Sec) redox motif. Here, we report the solution structure of the Sec13-->Cys variant of mouse SelW determined through high resolution NMR spectroscopy. The protein has a thioredoxin-like fold with the CXXU motif located in an exposed loop similarly to the redox-active site in thioredoxin. Protein dynamics studies revealed the rigidity of the protein backbone and mobility of two external loops and suggested a role of these loops in interaction with SelW partners. Molecular modeling of structures of other members of the Rdx family based on the SelW structure identified new conserved features in these proteins, including an aromatic cluster and interacting loops. Our previous study suggested an interaction between SelW and 14-3-3 proteins. In the present work, with the aid of NMR spectroscopy, we demonstrated specificity of this interaction and identified mobile loops in SelW as interacting surfaces. This finding suggests that 14-3-3 are redox-regulated proteins.  (+info)

Selenoprotein W is a protein that contains selenocysteine, an amino acid containing selenium. It is primarily found in muscle tissue and plays a role in protecting muscles from oxidative damage and maintaining the proper function of calcium channels. Selenoprotein W has been studied for its potential role in various health conditions related to muscle function and oxidative stress, such as muscular dystrophy and inflammation.

Selenoproteins are a specific group of proteins that contain the essential micronutrient selenium in the form of selenocysteine (Sec), which is a naturally occurring amino acid. Selenocysteine is encoded by the opal codon UGA, which typically serves as a stop codon in mRNA.

There are 25 known human selenoproteins, and they play crucial roles in various physiological processes, including antioxidant defense, DNA synthesis, thyroid hormone metabolism, and immune function. Some of the well-known selenoproteins include glutathione peroxidases (GPxs), thioredoxin reductases (TrxRs), and iodothyronine deiodinases (IDIs).

The presence of selenocysteine in these proteins makes them particularly efficient at catalyzing redox reactions, which involve the gain or loss of electrons. This property is essential for their functions as antioxidants and regulators of cellular signaling pathways.

Deficiencies in selenium can lead to impaired function of selenoproteins, potentially resulting in various health issues, such as increased oxidative stress, weakened immune response, and disrupted thyroid hormone metabolism.

Selenoprotein P is a protein that contains several selenocysteine residues and is encoded by the SEPP1 gene in humans. It is primarily synthesized in the liver and secreted into the bloodstream, where it functions as a major antioxidant and a selenium transport protein. Selenoprotein P plays a crucial role in protecting cells against oxidative stress and has been implicated in various physiological processes, including neuroprotection, fertility, and immune function. Additionally, selenoprotein P has been suggested as a potential biomarker for selenium status and oxidative stress in the body.

Selenium is a trace element that is essential for the proper functioning of the human body. According to the medical definitions provided by the National Institutes of Health (NIH), selenium is a component of several major metabolic pathways, including thyroid hormone metabolism, antioxidant defense systems, and immune function.

Selenium is found in a variety of foods, including nuts (particularly Brazil nuts), cereals, fish, and meat. It exists in several forms, with selenomethionine being the most common form found in food. Other forms include selenocysteine, which is incorporated into proteins, and selenite and selenate, which are inorganic forms of selenium.

The recommended dietary allowance (RDA) for selenium is 55 micrograms per day for adults. While selenium deficiency is rare, chronic selenium deficiency can lead to conditions such as Keshan disease, a type of cardiomyopathy, and Kaschin-Beck disease, which affects the bones and joints.

It's important to note that while selenium is essential for health, excessive intake can be harmful. High levels of selenium can cause symptoms such as nausea, vomiting, hair loss, and neurological damage. The tolerable upper intake level (UL) for selenium is 400 micrograms per day for adults.

Glutathione peroxidase (GPx) is a family of enzymes with peroxidase activity whose main function is to protect the organism from oxidative damage. They catalyze the reduction of hydrogen peroxide, lipid peroxides, and organic hydroperoxides to water or corresponding alcohols, using glutathione (GSH) as a reducing agent, which is converted to its oxidized form (GSSG). There are several isoforms of GPx found in different tissues, including GPx1 (also known as cellular GPx), GPx2 (gastrointestinal GPx), GPx3 (plasma GPx), GPx4 (also known as phospholipid hydroperoxide GPx), and GPx5-GPx8. These enzymes play crucial roles in various biological processes, such as antioxidant defense, cell signaling, and apoptosis regulation.

Selenocysteine (Sec) is a rare, naturally occurring amino acid that contains selenium. It is encoded by the opal (TGA) codon, which typically signals stop translation in mRNA. However, when followed by a specific hairpin-like structure called the Sec insertion sequence (SECIS) element in the 3' untranslated region of the mRNA, the TGA codon is interpreted as a signal for selenocysteine incorporation during protein synthesis.

Selenocysteine plays an essential role in several enzymes involved in antioxidant defense and redox homeostasis, such as glutathione peroxidases, thioredoxin reductases, and iodothyronine deiodinases. These enzymes require selenocysteine for their catalytic activity due to its unique chemical properties, which allow them to neutralize harmful reactive oxygen species (ROS) and maintain proper cellular function.

In summary, selenocysteine is a specialized amino acid containing selenium that is encoded by the TGA codon in mRNA when accompanied by a SECIS element. It is crucial for the activity of several enzymes involved in antioxidant defense and redox homeostasis.

In medical terms, the tongue is a muscular organ in the oral cavity that plays a crucial role in various functions such as taste, swallowing, and speech. It's covered with a mucous membrane and contains papillae, which are tiny projections that contain taste buds to help us perceive different tastes - sweet, salty, sour, and bitter. The tongue also assists in the initial process of digestion by moving food around in the mouth for chewing and mixing with saliva. Additionally, it helps in forming words and speaking clearly by shaping the sounds produced in the mouth.

Proteins are complex, large molecules that play critical roles in the body's functions. They are made up of amino acids, which are organic compounds that are the building blocks of proteins. Proteins are required for the structure, function, and regulation of the body's tissues and organs. They are essential for the growth, repair, and maintenance of body tissues, and they play a crucial role in many biological processes, including metabolism, immune response, and cellular signaling. Proteins can be classified into different types based on their structure and function, such as enzymes, hormones, antibodies, and structural proteins. They are found in various foods, especially animal-derived products like meat, dairy, and eggs, as well as plant-based sources like beans, nuts, and grains.

... P is the most common selenoprotein found in the plasma. It is unusual because in humans it contains 10 Sec ... Selenoproteins exist in all major domains of life, eukaryotes, bacteria and archaea. Among eukaryotes, selenoproteins appear to ... which shows the presence or absence of selenoprotein genes and accessory genes for the synthesis of selenoproteins in the ... Three selenoproteins, TXNRD1 (TR1), TXNRD2 (TR3) and glutathione peroxidase 4 (GPX4), have been shown to be essential in mouse ...
In molecular biology, the protein domain selenoprotein P (SelP) is the only known eukaryotic selenoprotein that contains ... Fujii M; Saijoh K; Kobayashi T; Fujii S; Lee MJ; Sumino K (October 1997). "Analysis of bovine selenoprotein P-like protein gene ... 2007). "The selenium-rich C-terminal domain of mouse selenoprotein P is necessary for the supply of selenium to brain and ... Binds to heparin in a pH-dependent manner Mostert V (April 2000). "Selenoprotein P: properties, functions, and regulation". ...
... is a protein that in humans is encoded by the SELENOO gene. This gene encodes a selenoprotein that is localized ... "Entrez Gene: Selenoprotein O". Retrieved 2018-05-18. Mabuchi H, Tatami R, Ueda K, Ueda R, Haba T, Kametani T, Watanabe A, ... The exact function of this selenoprotein is not known, but it is thought to have redox activity. [provided by RefSeq, Dec 2016 ... It is the largest mammalian selenoprotein, containing the rare amino acid selenocysteine (Sec). Sec is encoded by the UGA codon ...
Böck, A (2013). "Selenoprotein Synthesis". Encyclopedia of Biological Chemistry. pp. 210-213. doi:10.1016/B978-0-12-378630- ... Mix, H; Lobanov, A; Gladyshev, V (2007). "SECIS elements in the coding regions of selenoprotein transcripts are functional in ... In 2003, a landmark paper described the identification of all known selenoproteins in humans: 25 in total. Similar analyses ...
Liu, Junqiu (2012). Selenoprotein and Mimics. Springer. pp. 289-302. ISBN 978-3-642-22236-8. Huang, Michael (2001). "Room ...
These programs have been used in searches for novel selenoproteins. The SECIS element is found in a wide variety of organisms ... Mix H, Lobanov AV, Gladyshev VN (2007). "SECIS elements in the coding regions of selenoprotein transcripts are functional in ... Wilting R, Schorling S, Persson BC, Böck A (March 1997). "Selenoprotein synthesis in archaea: identification of an mRNA element ... Rother M, Resch A, Wilting R, Böck A (2001). "Selenoprotein synthesis in archaea". BioFactors. 14 (1-4): 75-83. doi:10.1002/ ...
Selenoprotein W is a protein that in humans is encoded by the SEPW1 gene. This gene encodes a selenoprotein, which contains a ... "Entrez Gene: SEPW1 selenoprotein W, 1". Whanger PD (December 2000). "Selenoprotein W: a review". Cellular and Molecular Life ... Overview of all the structural information available in the PDB for UniProt: P63300 (Mouse Selenoprotein W) at the PDBe-KB. v t ... The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for ...
Selenoprotein P is a better indicator of selenium nutritional status, and full expression of it would require more than 66 µg/ ... Papp, Laura Vanda; Lu, Jun; Holmgren, Arne; Khanna, Kum Kum (2007). "From Selenium to Selenoproteins: Synthesis, Identity, and ... Moosmann, B; Behl, C (2004). "Selenoprotein synthesis and side-effects of statins". Lancet. 363 (9412): 892-4. doi:10.1016/ ... Moosmann, B; Behl, C (2004). "Selenoproteins, cholesterol-lowering drugs, and the consequences: Revisiting of the mevalonate ...
Papp, Laura Vanda; Lu, Jun; Holmgren, Arne; Khanna, Kum Kum (1 July 2007). "From Selenium to Selenoproteins: Synthesis, ... Driscoll DM, Copeland PR (2003). "Mechanism and regulation of selenoprotein synthesis". Annual Review of Nutrition. 23 (1): 17- ...
15 kDa selenoprotein is a protein that in humans is encoded by the SEP15 gene. Two alternatively spliced transcript variants ... Studies in mouse suggest that this selenoprotein may have redox function and may be involved in the quality control of protein ... The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for ... This protein is a selenoprotein only found in eukaryotes. This domain has a thioredoxin-like domain and a surface accessible ...
"Entrez Gene: SEPX1 selenoprotein X, 1". Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches ... The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for ... Lescure A, Gautheret D, Carbon P, Krol A (Feb 2000). "Novel selenoproteins identified in silico and in vivo by using a ... This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is ...
Selenoprotein N is a protein that in humans is encoded by the SEPN1 gene. This gene encodes a selenoprotein, which contains a ... The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for ... Lescure A, Gautheret D, Carbon P, Krol A (Dec 1999). "Novel selenoproteins identified in silico and in vivo by using a ... "Entrez Gene: SEPN1 selenoprotein N, 1". "Radiography data for Sepn1". Wellcome Trust Sanger Institute. "Salmonella infection ...
Selenoprotein S, also known as SELS, is a human gene. This gene encodes a selenoprotein, which contains a selenocysteine (Sec) ... "Entrez Gene: SELS selenoprotein S". Ye, Yihong; Shibata Yoko; Yun Chi; Ron David; Rapoport Tom A (Jun 2004). "A membrane ... The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for ... 2007). "The role of the selenoprotein S (SELS) gene -105G>A promoter polymorphism in inflammatory bowel disease and regulation ...
Most selenoproteins contain a single selenocysteine residue. Selenoproteins that exhibit catalytic activity are called ... Selenoproteins contain selenocysteine residues. Selenocysteine is an analogue of the more common cysteine with selenium in ... When cells are grown in the absence of selenium, translation of selenoproteins terminates at the UGA codon, resulting in a ... Böck A, Forchhammer K, Heider J, Baron C (December 1991). "Selenoprotein synthesis: an expansion of the genetic code". Trends ...
Böck, A.; Forchhammer, K.; Heider, J.; Baron, C. (1991). "Selenoprotein synthesis: An expansion of the genetic code". Trends in ...
Selenoprotein P transports the trace element selenium from the liver to the testes and brain, and binds to ApoER2 in these ... Mice that have had their ApoER2 or Selenoprotein P expression knocked out show impaired spermatozoa development and decreased ... Burk RF, Hill KE (November 2009). "Selenoprotein P-expression, functions, and roles in mammals". Biochim. Biophys. Acta. 1790 ( ... "Ribosome stalling during selenoprotein translation exposes a ferroptosis vulnerability". Nature Chemical Biology. 18 (7): 751- ...
Candidate for selenium delivery protein in selenoprotein synthesis". The Journal of Biological Chemistry. 275 (9): 6195-200. ... Labunskyy VM, Hatfield DL, Gladyshev VN (July 2014). "Selenoproteins: molecular pathways and physiological roles". ... enzyme participates in selenoamino acid metabolism by recycling Se from selenocysteine during the degradation of selenoproteins ...
Lee BC, Dikiy A, Kim HY, Gladyshev VN (2009). "Functions and evolution of selenoprotein methionine sulfoxide reductases". ...
Lee BC, Dikiy A, Kim HY, Gladyshev VN (2009). "Functions and evolution of selenoprotein methionine sulfoxide reductases". ...
St Germain DL, Galton VA (August 1997). "The deiodinase family of selenoproteins". Thyroid. 7 (4): 655-68. doi:10.1089/thy. ...
Selenoprotein P is a protein that in humans is encoded by the SEPP1 gene. This gene encodes a selenoprotein containing multiple ... "Entrez Gene: SEPP1 selenoprotein P, plasma, 1". Burk and Hill 2009 "Selenop selenoprotein P [Mus musculus (house mouse)] - Gene ... This selenoprotein is an extracellular glycoprotein, and is unusual in that it contains 10 Sec residues (human, rat, mouse) per ... Hill KE, Lloyd RS, Yang JG, Read R, Burk RF (June 1991). "The cDNA for rat selenoprotein P contains 10 TGA codons in the open ...
Obata, T.; Y. Shiraiwa (2005). "A novel eukaryotic selenoprotein in the haptophyte alga Emiliania huxleyi". Journal of ...
"Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". ...
v t e (Articles with short description, Short description matches Wikidata, Genes on human chromosome 9, Selenoproteins, All ... is required for the translation of mammalian selenoprotein mRNAs". The EMBO Journal. 19 (2): 306-14. doi:10.1093/emboj/19.2.306 ... "SECIS-SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy". The EMBO Journal. 19 (24 ...
"Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". ...
Selenoprotein Canadian Reference Material of selenomethionine Whanger, P. D. (2002). "Selenocompounds in plants and animals and ...
"Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". ...
"Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". ...
... whereas GPX6 is a selenoprotein in humans with cysteine-containing homologues in rodents. In selenoproteins, the amino acid ... Ursini F, Heim S, Kiess M, Maiorino M, Roveri A, Wissing J, Flohé L (1999). "Dual function of the selenoprotein PHGPx during ... Sneddon AA, Wu HC, Farquharson A, Grant I, Arthur JR, Rotondo D, Choe SN, Wahle KW (2004). "Regulation of selenoprotein GPx4 ... Foresta C, Flohé L, Garolla A, Roveri A, Ursini F, Maiorino M (2003). "Male fertility is linked to the selenoprotein ...
Selenoprotein T contains a selenocysteine (Sec) residue at its active site. selenoprotein GRCh38: Ensembl release 89: ... Selenoprotein T, also known as SELT, is a protein that in humans is encoded by the SELT gene. The selenocysteine is encoded by ... "Entrez Gene: SELT selenoprotein T". Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico ... The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for ...
Selenoprotein P is the most common selenoprotein found in the plasma. It is unusual because in humans it contains 10 Sec ... Selenoproteins exist in all major domains of life, eukaryotes, bacteria and archaea. Among eukaryotes, selenoproteins appear to ... which shows the presence or absence of selenoprotein genes and accessory genes for the synthesis of selenoproteins in the ... Three selenoproteins, TXNRD1 (TR1), TXNRD2 (TR3) and glutathione peroxidase 4 (GPX4), have been shown to be essential in mouse ...
A role of Secisbp2 in stabilizing selenoprotein mRNAs in vivo was uncovered. ... Selenoproteins contain the rare amino acid selenocysteine (Sec). Mutations in SECISBP2 in humans lead to reduced selenoprotein ... Secisbp2 is essential for embryonic development and enhances selenoprotein expression Antioxid Redox Signal. 2014 Aug 20;21(6): ... Regarding selenoprotein expression, compensatory nuclear factor, erythroid-derived, like 2 (Nrf2)-dependent gene expression, or ...
This review presents a summary of the current understanding of the role of selenium and selenoproteins in regulating immune ... omic approaches and novel bioinformatics tools has led to new insights regarding the effects of selenium and selenoproteins in ... dietary selenium intake and this nutrient exerts its biological effects mostly through its incorporation into selenoproteins. ... Selenoprotein V. SELENOV, SELV. Testes-specific expression [21].. Selenoprotein W. SELENOW, SELW, SEPW1. Putative antioxidant ...
A study of selenoproteins in atlantic salmon (Salmo salar) using hyphenated mass spectrometry and bioinformatics. In 9th Nordic ... A study of selenoproteins in atlantic salmon (Salmo salar) using hyphenated mass spectrometry and bioinformatics. 9th Nordic ... A study of selenoproteins in atlantic salmon (Salmo salar) using hyphenated mass spectrometry and bioinformatics. / Sele, ... A study of selenoproteins in atlantic salmon (Salmo salar) using hyphenated mass spectrometry and bioinformatics. ...
Application of nuclear methods in the study of selenoproteins Behne, D.; Weiss-Nowak, C.; Kalckloesch, M.; Westphal, C.; ...
The Selenoprotein T subfamily has 5 members , canSARS ...
The Selenoprotein T subfamily has 5 members , canSARS ...
SelenoDB: a database of selenoprotein genes, proteins and SECIS elements. Unpublished. *LicenseThe software and data in ...
SelenoDB: a database of selenoprotein genes, proteins and SECIS elements. Unpublished. *LicenseThe software and data in ...
SelenoDB: a database of selenoprotein genes, proteins and SECIS elements. Unpublished. *LicenseThe software and data in ...
Selenoprotein W1 (SEPW1) Polyclonal Antibody, Cat#CAU22735. Rating Required Select Rating. 1 star (worst). 2 stars. 3 stars ( ...
Knockout models have demonstrated that the selenoprotein machinery, including endoplasmic reticulum-resident selenoproteins ... Knockout models have demonstrated that the selenoprotein machinery, including endoplasmic reticulum-resident selenoproteins ... Knockout models have demonstrated that the selenoprotein machinery, including endoplasmic reticulum-resident selenoproteins ... Knockout models have demonstrated that the selenoprotein machinery, including endoplasmic reticulum-resident selenoproteins ...
Selenium, Selenoprotein Genes and Crohns Disease in a Case-Control Population from Auckland, New Zealand ... Selenoprotein Genes and Crohns Disease in a Case-Control Population from Auckland, New Zealand. Nutrients, 4 (9). pp. 1247- ...
Human Selenoprotein P1, Plasma (SEPP1) ELISA Kit, Cat#EKU07255. Rating Required Select Rating. 1 star (worst). 2 stars. 3 stars ... Intra-assay Precision (Precision within an assay): 3 samples with low, middle and high level Selenoprotein P1, Plasma (SEPP1) ... Inter-assay Precision (Precision between assays): 3 samples with low, middle and high level Selenoprotein P1, Plasma (SEPP1) ... This assay has high sensitivity and excellent specificity for detection of Selenoprotein P1, Plasma (SEPP1). No significant ...
Lectures and seminars Cell and Tumor Biology seminar: Mechanisms of action targeting the cytosolic selenoprotein thioredoxin ... "Mechanisms of action targeting the cytosolic selenoprotein thioredoxin reductase for anticancer therapy" ...
Selenoprotein W (Selenow) is a ~9 kDa selenoprotein suggested to play a beneficial role in resolving inflammation. However, the ... N2 - Selenoprotein W (Selenow) is a ~9 kDa selenoprotein suggested to play a beneficial role in resolving inflammation. However ... AB - Selenoprotein W (Selenow) is a ~9 kDa selenoprotein suggested to play a beneficial role in resolving inflammation. However ... abstract = "Selenoprotein W (Selenow) is a ~9 kDa selenoprotein suggested to play a beneficial role in resolving inflammation. ...
Se alone or combined with VE increased the concentration of selenoprotein P and selenoproteins mRNA level and decreased the ... selenoproteins, and antioxidant enzyme activities in the breast meat of broilers under summer heat stress conditions. A total ... Se alone or combined with VE increased the concentration of selenoprotein P and selenoproteins mRNA level and decreased the ... The Se performs its biological functions mainly through selenoproteins, as Se is mainly incorporated on the selenoprotein ...
Selenoprotein deficiency and high levels of selenium compounds can effectively inhibit hepatocarcinogenesis in transgenic mice ...
Selenoprotein S (SelS) has previously been associated with a range of inflammatory markers, particularly in the context of ... Polymorphisms in the Selenoprotein S gene and subclinical cardiovascular disease in the Diabetes Heart Study. ... View more ,Selenoprotein S (SelS) has previously been associated with a range of inflammatory markers, particularly in the ...
Focusing on selenoproteins of unknown structures, we predict a thioredoxin-like fold for the Selenoprotein N (SelN) family and ... Focusing on selenoproteins of unknown structures, we predict a thioredoxin-like fold for the Selenoprotein N (SelN) family and ... Focusing on selenoproteins of unknown structures, we predict a thioredoxin-like fold for the Selenoprotein N (SelN) family and ... Focusing on selenoproteins of unknown structures, we predict a thioredoxin-like fold for the Selenoprotein N (SelN) family and ...
SELENON: selenoprotein N. *SEPSECS: Sep (O-phosphoserine) tRNA:Sec (selenocysteine) tRNA synthase ...
Selenoprotein GPX1 is a prognostic and chemotherapy-related biomarker for brain lower grade glioma. Title: Selenoprotein GPX1 ... It is also a selenoprotein, containing the rare amino acid selenocysteine (Sec) at its active site. Sec is encoded by the UGA ... The 3 UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) ...
Selenoprotein T (SELENOT), a vital thioredoxin-like selenoprotein, is crucial for ER homeostasis and cardiomyocyte ... Selenoprotein T (SELENOT), a vital thioredoxin-like selenoprotein, is crucial for ER homeostasis and cardiomyocyte ... The Antioxidant Selenoprotein T Mimetic, PSELT, Induces Preconditioning-like Myocardial Protection by Relieving Endoplasmic- ...
... ... Accurate quantification of selenoproteins in human plasma/serum by isotope dilution ICP-MS : focus on selenoprotein P , ...
The micronutrient selenium is essential for selenoprotein production and is transported from the liver to target tissues via ... selenoprotein P (SEPP1). Target tissues also produce SEPP1, which is thought to possess an endogenous antioxidant function. ... The micronutrient selenium is essential for selenoprotein production and is transported from the liver to target tissues via ... Selenoprotein P Influences Colitis-Induced Tumorigenesis by Mediating Stemness and Oxidative Damage. ...
The phenotype and long-term follow-up in 11 patients with juvenile selenoprotein N1-related myopathy. Eur J Paediatr Neurol. ... Rederstorff M, Krol A, Lescure A. Understanding the importance of selenium and selenoproteins in muscle function. Cell Mol Life ... Mutations in the selenocysteine insertion sequence-binding protein 2 gene lead to a multisystem selenoprotein deficiency ...
Selenoprotein P concentrations and risk of progression from mild cognitive impairment to dementia. ... However, little is known about the role of selenoprotein P, the main selenium transporter, which can also have adverse ...
Mouse SEPP1 (Selenoprotein P) CLIA Kit , G-EC-01635 MSRP: Was: Now: $266.00 - $4,134.00 ...
Lipid peroxidation products as a mediator of toxicity and adaptive response - The regulatory role of selenoprotein and vitamin ... Lipid peroxidation products as a mediator of toxicity and adaptive response - The regulatory role of selenoprotein and vitamin ... Lipid peroxidation products as a mediator of toxicity and adaptive response - The regulatory role of selenoprotein and vitamin ... T1 - Lipid peroxidation products as a mediator of toxicity and adaptive response - The regulatory role of selenoprotein and ...
  • citation needed] Besides the selenocysteine-containing selenoproteins, there are also some selenoproteins known from bacterial species, which have selenium bound noncovalently. (wikipedia.org)
  • Thus, even if a selenocysteine-containing selenoprotein is taken up in the diet and used as selenium source, the amino acid must be degraded prior to synthesising a new selenocysteine for incorporation into a selenoprotein. (wikipedia.org)
  • Since lack of selenium deprives the cell of its ability to synthesize selenoproteins, many health effects of low selenium intake are believed to be caused by the lack of one or more specific selenoproteins. (wikipedia.org)
  • The immune system relies on adequate dietary selenium intake and this nutrient exerts its biological effects mostly through its incorporation into selenoproteins. (mdpi.com)
  • The development of high-throughput omic approaches and novel bioinformatics tools has led to new insights regarding the effects of selenium and selenoproteins in human immuno-biology. (mdpi.com)
  • The study was carried out to investigate the effect of dietary selenium (Se) and vitamin E (VE) supplementation on mRNA level of heat shock proteins, selenoproteins, and antioxidant enzyme activities in the breast meat of broilers under summer heat stress conditions. (springeropen.com)
  • The micronutrient selenium is essential for selenoprotein production and is transported from the liver to target tissues via selenoprotein P (SEPP1). (xula.edu)
  • Most of the biological activity of selenium is due to selenoproteins containing selenocysteine, the 21st genetically encoded protein amino acid. (usda.gov)
  • Selenium to selenoproteins - role in COVID-19. (cdc.gov)
  • In molecular biology a selenoprotein is any protein that includes a selenocysteine (Sec, U, Se-Cys) amino acid residue. (wikipedia.org)
  • This may be one reason for the existence of a rather complicated pathway of selenocysteine biosynthesis and specific incorporation into selenoproteins, which avoids the occurrence of the free amino acid as intermediate. (wikipedia.org)
  • About 25 different selenocysteine-containing selenoproteins have so far been observed in human cells and tissues. (wikipedia.org)
  • The selenocysteine insertion sequence (SECIS)-binding protein 2 (Secisbp2) binds to SECIS elements located in the 3'-untranslated region of eukaryotic selenoprotein mRNAs. (nih.gov)
  • Selenoproteins contain the rare amino acid selenocysteine (Sec). Mutations in SECISBP2 in humans lead to reduced selenoprotein expression thereby affecting thyroid hormone-dependent growth and differentiation processes. (nih.gov)
  • It is also a selenoprotein, containing the rare amino acid selenocysteine (Sec) at its active site. (nih.gov)
  • Selenoproteins - What unique properties can arise with selenocysteine in place of cysteine? (aaem.pl)
  • Selenoproteins are proteins that specifically incorporate SELENOCYSTEINE into their amino acid chain. (bvsalud.org)
  • Most selenoproteins are enzymes with the selenocysteine residues being responsible for their catalytic functions. (bvsalud.org)
  • Three selenoproteins, TXNRD1 (TR1), TXNRD2 (TR3) and glutathione peroxidase 4 (GPX4), have been shown to be essential in mouse knockout experiments. (wikipedia.org)
  • Consequences of genetic variations in the glutathione peroxidase 1 selenoprotein. (uic.edu)
  • The overview and meta-analysis of the studies on blood Se and selenoprotein P (SELENOP) levels, as well as glutathione peroxidase (GPX) activity in obese subjects, have yielded heterogenous and even conflicting results. (elsevierpure.com)
  • These observations have recently been confirmed by whole genome analysis, which shows the presence or absence of selenoprotein genes and accessory genes for the synthesis of selenoproteins in the respective organism. (wikipedia.org)
  • The most abundant selenoproteins in mammals are the glutathione peroxidases (5-6 genes) that reduce hydrogen peroxide and lipid hydroperoxides at the expense of glutathione and serve to limit the strength and duration of reactive oxygen signals. (usda.gov)
  • This work hypothesizes that polymorphisms in key glutathione synthesizing enzyme, glutathione S-transferase, and selenoprotein genes underlie inter-individual differences in mercury body burden as assessed by analytical mercury measurement in urine and hair, biomarkers of elemental mercury and methylmercury, respectively. (cdc.gov)
  • Overall, this study suggests that polymorphisms in selenoproteins and glutathione-related genes may influence elimination of mercury in the urine and hair or mercury retention following exposures to elemental mercury (via dental amalgams) and methylmercury (via fish consumption). (cdc.gov)
  • Proteins containing such unspecifically incorporated selenomethionine residues are not regarded as selenoproteins. (wikipedia.org)
  • Lenart, A & Pawłowski, K 2013, ' Intersection of selenoproteins and kinase signalling ', Biochimica et Biophysica Acta - Proteins and Proteomics , vol. 1834, no. 7, pp. 1279-1284. (elsevierpure.com)
  • Recent evidence suggests selenoprotein W and the six other small thioredoxin-like mammalian selenoproteins may serve to transduce hydrogen peroxide signals into regulatory disulfide bonds in specific target proteins. (usda.gov)
  • Glutathione enzyme and selenoprotein polymorphisms associate with mercury biomarker levels in Michigan dental professionals. (cdc.gov)
  • Transcript-specific and gender-selective effects on selenoprotein mRNA abundance were greater in Secisbp2-deficient hepatocytes than in tRNA[Ser]Sec-deficient cells. (nih.gov)
  • Se alone or combined with VE increased the concentration of selenoprotein P and selenoproteins mRNA level and decreased the expression of HSP60 . (springeropen.com)
  • SepSecS is essential for the synthesis of selenoproteins, which are expressed unevenly and stably in the brain ( 3 ). (frontiersin.org)
  • The biallelic deletion of Trsp in mice (which impedes selenoprotein synthesis) resulted in cerebellar hypoplasia, seizure, and developmental delay ( 4 )-phenotypes that are congruent with those described in previous clinical reports of SEPSECS mutations ( 5 - 11 ). (frontiersin.org)
  • SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein. (igbmc.fr)
  • Knockout models have demonstrated that the selenoprotein machinery, including endoplasmic reticulum-resident selenoproteins together with GPXs and thioredoxin reductases (TXNRDs), are tightly related to adipocyte development and functioning. (elsevierpure.com)
  • Several selenoproteins in the endoplasmic reticulum are involved in regulation of protein disulfide formation and unfolded protein response signaling, although their precise biological activities have not been determined. (usda.gov)
  • Despite the massive reduction of Dio1 and Sepp1 mRNAs, significantly more corresponding protein was detected in primary hepatocytes lacking Secisbp2 than in cells lacking tRNA[Ser]Sec. Regarding selenoprotein expression, compensatory nuclear factor, erythroid-derived, like 2 (Nrf2)-dependent gene expression, or embryonic development, phenotypes were always milder in Secisbp2-deficient than in tRNA[Ser]Sec-deficient mice. (nih.gov)
  • Intra-assay Precision (Precision within an assay): 3 samples with low, middle and high level Selenoprotein P1, Plasma (SEPP1) were tested 20 times on one plate, respectively. (biomatik.com)
  • Inter-assay Precision (Precision between assays): 3 samples with low, middle and high level Selenoprotein P1, Plasma (SEPP1) were tested on 3 different plates, 8 replicates in each plate. (biomatik.com)
  • This assay has high sensitivity and excellent specificity for detection of Selenoprotein P1, Plasma (SEPP1). (biomatik.com)
  • No significant cross-reactivity or interference between Selenoprotein P1, Plasma (SEPP1) and analogues was observed. (biomatik.com)
  • Among functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Sec. Selenoprotein P is the most common selenoprotein found in the plasma. (wikipedia.org)
  • Se is central to the function of selenoproteins, which play key roles in many biological functions including redox signaling, antioxidant defense, hormone metabolism, and immune responses. (dtu.dk)
  • Selenoprotein S (SelS) has previously been associated with a range of inflammatory markers, particularly in the context of cardiovascular disease (CVD). (edu.au)
  • In humans, selenoprotein S (SelS) has antioxidant ability, but it is unclear whether SelS affects viral infection. (oncotarget.com)
  • This review broadly discusses the mechanisms of lipid peroxidation and its products, its utility as a biomarker for oxidative stress, the biological effects of lipid peroxidation products, including their action as a mediator of the adaptive response, and the role of the antioxidant system, particularly selenoproteins and vitamin E, in preventing lipid peroxidation and ferroptosis. (elsevierpure.com)
  • Discussing the recent prediction of a protein kinase-like domain in the Selenoprotein O (SelO), we reiterate evidence for an oxidoreductase function alongside the predicted kinase domain. (elsevierpure.com)
  • Focusing on selenoproteins of unknown structures, we predict a thioredoxin-like fold for the Selenoprotein N (SelN) family and use the structure to rationalise effects of the muscular myopathy-linked mutations in the gene coding SelN. (elsevierpure.com)
  • The objective of the present study is to review the current data on Se status in obesity and to discuss the interference between Se and selenoprotein metabolism in adipocyte physiology and obesity pathogenesis. (elsevierpure.com)
  • Furthermore, we set out to combine theoretical selenoprotein predictions with hyphenated analytical techniques to characterize the selenoproteome of salmon liver tissue. (dtu.dk)
  • Lipid hydroperoxides are the major primary products formed and are reduced to the corresponding hydroxides by antioxidative enzymes such as selenoproteins, and/or undergo secondary oxidation, generating various products with electrophilic properties, such as 4-hydroxy-2-nonenal. (elsevierpure.com)
  • This review summarizes the current state of knowledge of the role of selenoproteins in transmitting and regulating reactive oxygen signals. (usda.gov)
  • In conclusion, Se and selenoproteins appear to play an essential role in adipose tissue physiology, although human data are inconsistent. (elsevierpure.com)
  • A selenoprotein differentially expressed and regulated in human and rat brain and other tissues. (bvsalud.org)
  • This hypothesis provides a new framework for predicting and understanding the biological functions of uncharacterized selenoproteins. (usda.gov)
  • The most widely distributed selenoprotein family in Nature is represented by the highly conserved thioredoxin-like selenoprotein W and its homologs that have not yet been assigned specific biological functions. (usda.gov)
  • Dive into the research topics of 'Lipid peroxidation products as a mediator of toxicity and adaptive response - The regulatory role of selenoprotein and vitamin E'. Together they form a unique fingerprint. (elsevierpure.com)
  • Application of nuclear methods in the study of selenoproteins. (iaea.org)
  • A role of Secisbp2 in stabilizing selenoprotein mRNAs in vivo was uncovered. (nih.gov)
  • Selenoprotein W (Selenow) is a ~9 kDa selenoprotein suggested to play a beneficial role in resolving inflammation. (psu.edu)
  • Conditional deletion of Secisbp2 in hepatocytes significantly decreased selenoprotein expression. (nih.gov)
  • The number and expression levels of selenoproteins vary between different animal species with teleost fish featuring a much higher number of selenoproteins compared to vertebrates. (dtu.dk)
  • While selenoproteomes have been well described for many species, a comprehensive analysis of selenoproteins in Atlantic salmon (Salmo salar) has yet to be performed. (dtu.dk)
  • Among eukaryotes, selenoproteins appear to be common in animals, but rare or absent in other phyla-one has been identified in the green alga Chlamydomonas, but almost none in other plants or in fungi. (wikipedia.org)
  • Non-occupational higher exposure to selenoproteins or methylated metabolites concentrations. (cdc.gov)
  • The small, obscure group of selenoprotein oxidoreductases and the huge clan of kinases, the workhorses of cellular signalling, are rarely discussed together. (elsevierpure.com)