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Cellular prion protein (PrPC) in Caenorhabditis elegans



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Cellular prion protein (PrPC) is a conserved glycoprotein predominantly being expressed in neurons, glial and lymphatic cells. While the pathology of prion diseases based on the misfolded Scrapie prion protein (PrPSc) is well understood, the physiologic function of PrPC remains enigmatic. Therefore, its much debated function in oxidative stress resistance was further investigated by expressing human PrPC in Caenorhabditis elegans (C. elegans). Both under non stressful conditions and under Paraquat exposure, a producer of superoxide anions, nematodes expressing PrPC had a significant increase in lifespan and stress resistance. Interactions with established C. elegans stress pathways were excluded. However, expression of PrPC showed no effect in handling other stressors like hydrogen peroxide, heat and copper ions intoxication. Further testing showed Paraquat resistance being SOD-1 (superoxide dismutase) dependent. However, advantageous resistance of PrPC strains is only achieved via SOD-4 and SOD-5 expression, therefore strongly suggesting that additional resistance of PrPC strains is caused by SOD-1 overexpression, regulated by the potential regulator enzymes SOD-4 and SOD-5.






Cellular prion protein (PrPC) is a conserved glycoprotein predominantly being expressed in neurons, glial and lymphatic cells. While the pathology of prion diseases based on the misfolded Scrapie prion protein (PrPSc) is well understood, the physiologic function of PrPC remains enigmatic. Therefore, its much debated function in oxidative stress resistance was further investigated by expressing human PrPC in Caenorhabditis elegans (C. elegans). Both under non stressful conditions and under Paraquat exposure, a producer of superoxide anions, nematodes expressing PrPC had a significant increase in lifespan and stress resistance. Interactions with established C. elegans stress pathways were excluded. However, expression of PrPC showed no effect in handling other stressors like hydrogen peroxide, heat and copper ions intoxication. Further testing showed Paraquat resistance being SOD-1 (superoxide dismutase) dependent. However, advantageous resistance of PrPC strains is only achieved via SOD-4 and SOD-5 expression, therefore strongly suggesting that additional resistance of PrPC strains is caused by SOD-1 overexpression, regulated by the potential regulator enzymes SOD-4 and SOD-5.


We confirmed that A142. Amazon.com Cellular prion protein PrPC in Caenorhabditis elegans Investigation of the physiologic function of human prion protein in a new model organism . 1 2 This theory has excluded the participation of nucleic acids in prion propagation. Characterization of cellular prion protein PrPC in Caenorhabditis elegans. Cellular prion protein PrPC in Caenorhabditis elegans Investigation of the physiologic function of human prion protein in a new model organism Amazon.co.uk Stahl Marcel Werner Books. The mammalian prion protein PrPc is a cellular protein of unknown function an altered isoform of which PrPsc is a.


Marcel Werner

Buy Cellular Prion Protein Prpc in Caenorhabditis Elegans by Stahl Marcel Werner for 170.99 at Mighty Ape Australia. heftet 2012. Cellular Prion Protein Prpc in Caenorhabditis Elegans Stahl Marcel Werner Amazon.com.mx Libros. relative population size from 0.0 to 1.0 xaxis showing the time frame in days.


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