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Selenium and Selenoproteins in Neutrophil Functions. [PDF]
Biol Trace Elem ResLee TJ, Prabhu KS.
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Annual Review of Nutrition, 1993
Selenium exerts its biological activity largely through selenoproteins, which contain the element in the form of selenocysteine. Five selenoproteins have been characterized in animal tissues and there is evidence that a number of others exist. Selenoprotein synthesis is a complex process that has been well characterized in prokaryotic systems but ...
R F, Burk, K E, Hill
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Selenium exerts its biological activity largely through selenoproteins, which contain the element in the form of selenocysteine. Five selenoproteins have been characterized in animal tissues and there is evidence that a number of others exist. Selenoprotein synthesis is a complex process that has been well characterized in prokaryotic systems but ...
R F, Burk, K E, Hill
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BioEssays, 1999
Selenoproteins contain selenium in stoichiometric amounts. Most are synthesized by a process that decodes UGA codons as selenocysteine. Twelve animal selenoproteins have been characterized, and biochemical functions have been described for all but three. Two of these "orphan" selenoproteins are discussed in this paper.
R F, Burk, K E, Hill
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Selenoproteins contain selenium in stoichiometric amounts. Most are synthesized by a process that decodes UGA codons as selenocysteine. Twelve animal selenoproteins have been characterized, and biochemical functions have been described for all but three. Two of these "orphan" selenoproteins are discussed in this paper.
R F, Burk, K E, Hill
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Selenoproteins and cardiovascular stress [PDF]
Thrombosis and Haemostasis, 2015 SummaryDietary selenium (Se) is an essential micronutrient that exerts its biological effects through its incorporation into selenoproteins. This family of proteins contains several antioxidant enzymes such as the glutathione peroxidases, redox-regulating enzymes such as thioredoxin reductases, a methionine sulfoxide reductase, and others.
Peter R Hoffmann, Aaron H Rose
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Selenoprotein expression and function—Selenoprotein W
Biochimica et Biophysica Acta (BBA) - General Subjects, 2009Selenoprotein W (SeW) is a small selenoprotein (85 to 88 amino acids) first identified in sheep suffering from selenium deficiency. The levels are highest in muscle, heart (except rodents) spleen and brain. The deduced amino acid sequence has been obtained for mice, rats, monkeys, humans, sheep, pigs, fish and chickens.
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Cellular and Molecular Life Sciences, 2000
Selenoprotein P (SeP) is an extracellular, monomeric glycoprotein containing up to 10 selenocysteine residues in the polypeptide chain. It is ubiquitously expressed in mammalian tissues, and in human plasma it accounts for at least 40% of the total selenium concentration. SeP binds to heparin and cell membranes, and is associated with endothelial cells.
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Selenoprotein P (SeP) is an extracellular, monomeric glycoprotein containing up to 10 selenocysteine residues in the polypeptide chain. It is ubiquitously expressed in mammalian tissues, and in human plasma it accounts for at least 40% of the total selenium concentration. SeP binds to heparin and cell membranes, and is associated with endothelial cells.
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Selenoproteins and Cancer Prevention
Annual Review of Nutrition, 2012The discovery of multiple selenoproteins has raised tantalizing questions about their role in maintaining normal cellular function. Unfortunately, many of these remain inadequately investigated. While they have a role in maintaining redox balance, other functions are becoming increasingly recognized.
Cindy D, Davis +2 more
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Natural and synthetic selenoproteins
Current Opinion in Chemical Biology, 2014Once considered highly toxic, the element selenium is now recognized as a micronutrient essential for human health. It is inserted co-translationally into many proteins as the non-canonical amino acid selenocysteine, providing the resulting selenoprotein molecules with a range of valuable redox properties; selenocysteine is also increasingly exploited ...
Metanis N, Hilvert D
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Molecular Biology of Selenoproteins
Annual Review of Nutrition, 1990Article de synthese sur la biologie moleculaire des selenoproteines. Etude du metabolisme du selenium (Se), des quatre classes de selenoproteines, de la glutathion peroxidase (GPX) Se-dependante et non dependante, de la phospholipide hydroperoxide GPX, de la GPX plasmatique, de seleno-proteines de mammiferes (rats).
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