scrapie/hypoxia

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Protection by anoxia of the scrapie agent and some DNA and RNA viruses irradiated as dry preparations.

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Gingerol-induced hypoxia-inducible factor 1 alpha inhibits human prion peptide-mediated neurotoxicity.

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Prion diseases are a family member of neurodegenerative disorders caused by the accumulation of misfolded-prion proteins (scrapie form of PrP, PrP(Sc)). The accumulation of PrP(Sc) in the brain leads to neurotoxicity by the induction of mitochondrial-apoptotic pathways. Recent studies implicated

Significant reduction of the GLUT3 level, but not GLUT1 level, was observed in the brain tissues of several scrapie experimental animals and scrapie-infected cell lines.

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Glucose transporters 1 (GLUT1) and 3 (GLUT3) belong to the solute carrier family 2 (SLC2, facilitated glucose transporter) and are the two most important glucose transporters (GLUTs) in brain tissue, and between them, GLUT3 is the primary one for neurons, which is responsible for glucose uptake. To

Effect of hyperbaric oxygenation on experimental scrapie in mice.

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The effect of hyperbaric oxygenation upon experimental infection of BALB/c mice with the scrapie agent was investigated by virological methods, histology and electron microscopy. A multiple exposure of scrapie-infected mice to hyberbaric oxygenation during the incubational period led to a certain

Hypoxia-inducible factor-1 α regulates prion protein expression to protect against neuron cell damage.

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The human prion protein fragment, PrP (106-126), may contain a majority of the pathological features associated with the infectious scrapie isoform of PrP, known as PrP(Sc). Based on our previous findings that hypoxia protects neuronal cells from PrP (106-126)-induced apoptosis and increases

Lactoferrin from bovine colostrum regulates prolyl hydroxylase 2 activity and prevents prion protein-mediated neuronal cell damage via cellular prion protein.

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Prion disorders are associated with the conversion of normal cellular prion protein (PrPc) to the abnormal scrapie isoform of prion protein (PrPsc). Recent studies have shown that expression of normal PrPc is regulated by hypoxia-inducible factor-1 alpha (HIF-1α), and that lactoferrin increases

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