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Neuronal and ependymal expression of selenoprotein P in the human brain | Journal of Neural Transmission
Description:
Selenoprotein P (SePP) is central to selenium (Se) metabolism in the mammalian organism. Human SePP contains 10 Se atoms that are covalent constituents of the polypeptide chain incorporated as the rare amino acid selenocysteine (Sec). Since hepatocytes secrete SePP into plasma, SePP is commonly regarded as a Se transport protein, although SePP mRNA is expressed in many organs. Gene targeting of SePP in mice leads to neurological dysfunction resulting from Se deficiency and associated reduction of selenoenzyme activities in the brain. However, more recent data revealed that isolated hepatic SePP deficiency does not alter brain Se levels, suggesting a role for SePP locally expressed in the brain. Some of the best characterized and most abundant selenoenzymes, glutathione peroxidases, thioredoxin reductases, and methionine sulfoxide reductase B, play major roles in the cellular defense against reactive oxygen species. Therefore, it was hypothesized that reduced brain Se bioavailability may be involved in the pathogenesis of neurodegenerative disease and normal ageing. We present evidence that human CSF contains SePP and that the human brain expresses SePP mRNA. Moreover, SePP-like immunoreactivity localizes to neurons and ependymal cells and thus appears strategically situated for maintenance and control of Se-dependent anti-oxidative defense systems.
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article, google, scholar, cas, pubmed, brain, selenoprotein, selenium, biol, schweizer, sepp, schomburg, oxidative, köhrle, selenoproteins, essential, function, human, mice, role, reductase, privacy, cookies, content, journal, stress, med, res, burk, hill, cell, free, mol, data, publish, search, gene, glutathione, thioredoxin, disease, neurons, access, development, biochem, radic, mouse, chem, science, germany, information,
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month download article/chapter goldowitz rf burk bar-noy wm williams guigo vn gladyshev yan jn barrett dc%2bd2mxht1yntr%2fp 10 selenocysteine trna[ser]sec oxidative stress-induced apoptosis beck ak hatzopoulos full article pdf saito mj lee reactive oxygen species methionine sulfoxide reductase privacy choices/manage cookies target tissues biochem dyak1cxksf2qsl0%3d 10 chen mj berry article journal human brain published survival-promoting factor bovine selenoprotein p mitochondrial thioredoxin reductase article log selenium deficiency biochem neural transmission aims messenger rna levels oxidative stress hypothesis cytoplasmic thioredoxin reductase rat central neurons cultured central neurons european economic area scope submit manuscript polypeptide chain incorporated neurological dysfunction resulting play major roles appears strategically situated nervous system development related subjects unique physical characteristics cadenas kj davies jakupoglu sg moreno schmahl kr chien wurst gw bornkamm jakupoglu gk przemeck rich domain insertion thyroid hormones rapidly thyrotropin-releasing hormone nitsch ne savaskan brainstem axonal degeneration shibatani jg belter
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- JK Andersen (2004) Oxidative stress in neurodegeneration: cause or consequence?
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headline:Neuronal and ependymal expression of selenoprotein P in the human brain
description:Selenoprotein P (SePP) is central to selenium (Se) metabolism in the mammalian organism. Human SePP contains 10 Se atoms that are covalent constituents of the polypeptide chain incorporated as the rare amino acid selenocysteine (Sec). Since hepatocytes secrete SePP into plasma, SePP is commonly regarded as a Se transport protein, although SePP mRNA is expressed in many organs. Gene targeting of SePP in mice leads to neurological dysfunction resulting from Se deficiency and associated reduction of selenoenzyme activities in the brain. However, more recent data revealed that isolated hepatic SePP deficiency does not alter brain Se levels, suggesting a role for SePP locally expressed in the brain. Some of the best characterized and most abundant selenoenzymes, glutathione peroxidases, thioredoxin reductases, and methionine sulfoxide reductase B, play major roles in the cellular defense against reactive oxygen species. Therefore, it was hypothesized that reduced brain Se bioavailability may be involved in the pathogenesis of neurodegenerative disease and normal ageing. We present evidence that human CSF contains SePP and that the human brain expresses SePP mRNA. Moreover, SePP-like immunoreactivity localizes to neurons and ependymal cells and thus appears strategically situated for maintenance and control of Se-dependent anti-oxidative defense systems.
datePublished:2007-01-25T00:00:00Z
dateModified:2007-01-25T00:00:00Z
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Keywords: Oxidative stress, glutathione peroxidase, selenium, neuron, Purkinje, transport
Neurology
Psychiatry
Neurosciences
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headline:Neuronal and ependymal expression of selenoprotein P in the human brain
description:Selenoprotein P (SePP) is central to selenium (Se) metabolism in the mammalian organism. Human SePP contains 10 Se atoms that are covalent constituents of the polypeptide chain incorporated as the rare amino acid selenocysteine (Sec). Since hepatocytes secrete SePP into plasma, SePP is commonly regarded as a Se transport protein, although SePP mRNA is expressed in many organs. Gene targeting of SePP in mice leads to neurological dysfunction resulting from Se deficiency and associated reduction of selenoenzyme activities in the brain. However, more recent data revealed that isolated hepatic SePP deficiency does not alter brain Se levels, suggesting a role for SePP locally expressed in the brain. Some of the best characterized and most abundant selenoenzymes, glutathione peroxidases, thioredoxin reductases, and methionine sulfoxide reductase B, play major roles in the cellular defense against reactive oxygen species. Therefore, it was hypothesized that reduced brain Se bioavailability may be involved in the pathogenesis of neurodegenerative disease and normal ageing. We present evidence that human CSF contains SePP and that the human brain expresses SePP mRNA. Moreover, SePP-like immunoreactivity localizes to neurons and ependymal cells and thus appears strategically situated for maintenance and control of Se-dependent anti-oxidative defense systems.
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Neurology
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