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Selenoprotein P, plasma, 1

selenoprotein P, Sepp1, SeP, selenoprotein P in
This gene encodes a selenoprotein containing multiple selenocysteine (Sec) residues, which are encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This selenoprotein is an extracellular glycoprotein, and is unusual in that it contains 10 Sec residues per polypeptide. It is a heparin-binding protein that appears to be associated with endothelial cells, and has been implicated to function as an antioxidant in the extracellular space. Several transcript variants, encoding either the same or different isoform, have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ethanolaminephosphotransferase, HAD, CAN, Thioredoxin, ACID
Papers on selenoprotein P
Molecular characterization and expression analyses of cDNAs encoding the thioredoxin-interacting protein and selenoprotein P genes and histological changes in Nile tilapia (Oreochromis niloticus) in response to silver nanoparticle exposure.
Srisapoome et al., Bangkok, Thailand. In Gene, Mar 2016
Herein, Nile tilapia thioredoxin-interacting protein (On-TXNIP) and selenoprotein P (On-SEPP) cDNAs were cloned and characterized.
Genetic polymorphisms that affect selenium status and response to selenium supplementation in United Kingdom pregnant women.
Rayman et al., Shenyang, China. In Am J Clin Nutr, Jan 2016
In nonpregnant populations, the selenium status or response to supplementation has been associated with polymorphisms in dimethylglycine dehydrogenase (DMGDH), selenoprotein P (SEPP1) and the glutathione peroxidases [cytosolic glutathione peroxidase (GPx1) and phospholipid glutathione peroxidase (GPx4)].
Selenium speciation in paired serum and cerebrospinal fluid samples of sheep.
Michalke et al., Hannover, Germany. In J Trace Elem Med Biol, Jan 2016
IEC-ICP-DRC-MS technique was able to differentiate the Se species selenoprotein P-bound Se (SePP), selenomethionine, glutathione peroxidase-bound Se (Se-GPx), selenocystine, thioredoxin reductase-bound Se, ovine serum albumin-bound Se (Se-OSA), SeIV and SeVI in ovine serum and CSF.
Effect of Inorganic Dietary Selenium Supplementation on Selenoprotein and Lipid Metabolism Gene Expression Patterns in Liver and Loin Muscle of Growing Lambs.
Pierzchała et al., Poland. In Biol Trace Elem Res, Jan 2016
Significant differences were found in the expression of GPX1, GPX2, SEPM, SEPW1, SEP15, SEPGS2, and TXNRD1 in the liver, and GPX1, SEPP1, SEPN1, SEPW1, SEP15, and MSRB1 in the LD muscle between S and C lambs.
Selenium in the therapy of neurological diseases. Where is it going?
Adamczyk et al., Warsaw, Poland. In Curr Neuropharmacol, Jan 2016
glutathione peroxidases (GPxs), thioredoxin reductases (TrxRs) or selenoprotein P (SelP), are strongly involved in antioxidant defence and in maintaining intercellular reducing conditions.
Pro198Leu polymorphism affects the selenium status and GPx activity in response to Brazil nut intake.
Cozzolino et al., Melbourne, Australia. In Food Funct, Jan 2016
Here, we have conducted a pilot study that examined the effects of a range of single nucleotide polymorphisms (SNPs) in genes encoding the selenoproteins glutathione peroxidase (GPX1) and selenoprotein P (SEPP) in response to selenium supplementation via dietary Brazil nuts, including selenium status, oxidative stress parameters and GPX1 and SEPP gene expression.
DNA damage and oxidative stress response to selenium yeast in the non-smoking individuals: a short-term supplementation trial with respect to GPX1 and SEPP1 polymorphism.
Wasowicz et al., Łódź, Poland. In Eur J Nutr, Jan 2016
METHODS: The trial involved 95 non-smoking individuals, stratified according to GPX1 rs1050450 and SEPP1 rs3877899 genotypes, and supplemented with selenium yeast (200 µg) for 6 weeks.
Redox regulation of FoxO transcription factors.
Monsalve et al., Jena, Germany. In Redox Biol, Dec 2015
superoxide dismutase-2, peroxiredoxins 3 and 5) and peroxisomes (catalase), as well as for antioxidant proteins found extracellularly in plasma (e.g., selenoprotein P and ceruloplasmin).
Competition between the Brain and Testes under Selenium-Compromised Conditions: Insight into Sex Differences in Selenium Metabolism and Risk of Neurodevelopmental Disease.
Berry et al., Nashville, United States. In J Neurosci, Dec 2015
Male mice lacking two key genes involved in Se metabolism (Scly(-/-)Sepp1(-/-) mice), selenoprotein P (Sepp1) and Sec lyase (Scly), develop severe neurological dysfunction, neurodegeneration, and audiogenic seizures that manifest beginning in early adulthood.
Selenium and the thyroid.
Köhrle, Berlin, Germany. In Curr Opin Endocrinol Diabetes Obes, Oct 2015
SUMMARY: Adequate nutritional supply of selenium that saturates expression of circulating selenoprotein P, together with optimal iodine and iron intake, is required for a healthy and functional thyroid during development, adolescence, adulthood and aging.
Revised reference values for selenium intake.
German Nutrition Society (DGE) et al., Potsdam, Germany. In J Trace Elem Med Biol, Oct 2015
The saturation of selenoprotein P (SePP) in plasma is used as a criterion for the derivation of reference values for selenium intake in adults.
The selenium content of SEPP1 versus selenium requirements in vertebrates.
Ellingsen et al., Bergen, Norway. In Peerj, 2014
Selenoprotein P (SEPP1) distributes selenium (Se) throughout the body via the circulatory system.
Regulation of Selenium Metabolism and Transport.
Hill et al., Nashville, United States. In Annu Rev Nutr, 2014
It responds to selenium deficiency by curtailing excretion and secreting selenoprotein P (Sepp1) into the plasma at the expense of its intracellular selenoproteins.
Long isoform mouse selenoprotein P (Sepp1) supplies rat myoblast L8 cells with selenium via endocytosis mediated by heparin binding properties and apolipoprotein E receptor-2 (ApoER2).
Burk et al., Nashville, United States. In J Biol Chem, 2012
apoER2-mediated uptake of long isoform Sepp1 is responsible for selenium distribution to tissues throughout the body.
Absence of selenoprotein P but not selenocysteine lyase results in severe neurological dysfunction.
Berry et al., Honolulu, United States. In Genes Brain Behav, 2012
the neurological phenotype caused by the absence of Sepp1 is exacerbated in male vs. female mice.
Inverse correlation between serum levels of selenoprotein P and adiponectin in patients with type 2 diabetes.
Takamura et al., Kanazawa, Japan. In Plos One, 2011
Circulating selenoprotein P levels were positively correlated with fasting plasma glucose and negatively associated with both total and high-molecular adiponectin in type 2 diabetics.
Serum selenoprotein P levels in patients with type 2 diabetes and prediabetes: implications for insulin resistance, inflammation, and atherosclerosis.
Choi et al., Seoul, South Korea. In J Clin Endocrinol Metab, 2011
Circulating SeP concentrations were elevated in patients with glucose metabolism dysregulation and were related to various cardiometabolic parameters including insulin resistance, inflammation, and atherosclerosis.
Progression of neurodegeneration and morphologic changes in the brains of juvenile mice with selenoprotein P deleted.
Valentine et al., Nashville, United States. In Brain Res, 2011
Deletion of Sepp1 (and presumably selenium deficiency in the brain) produce both neuronal and axonal degeneration as well as more moderate and potentially reversible neurite changes in the developing brain.
A liver-derived secretory protein, selenoprotein P, causes insulin resistance.
Kaneko et al., Kanazawa, Japan. In Cell Metab, 2010
Both genetic deletion and RNA interference-mediated knockdown of selenoprotein P improved systemic insulin sensitivity and glucose tolerance in mice.
Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3' untranslated region.
Larsen et al., Boston, United States. In Nature, 1991
Selenocysteine is incorporated cotranslationally at UGA codons, normally read as stop codons, in several bacterial proteins and in the mammalian proteins glutathione peroxidase (GPX), selenoprotein P and Type I iodothyronine 5' deiodinase (5'DI).
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