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- W2022131253 abstract "The prion protein is a highly conserved glycoprotein expressed most highly in the synapse. Evidence has recently been put forward to suggest that the prion protein is an antioxidant. However, the functional importance of the prion protein has been disputed; it is claimed that mice genetically ablated to lack prion protein expression are normal and have no specific phenotype. We have reexamined the phenotype of prion protein knockout mice and found that there are multiple biochemical changes in the mice, including increased levels of nuclear factor NF-κB and Mn superoxide dismutase, COX-IV decreased levels of Cu/Zn superoxide dismutase activity, decreased p53, and altered melatonin levels. Additionally, cultured cells from these mice are more sensitive to a range of insults, all linked to increased neuronal sensitivity to oxidative stress. These results imply that prion protein knockout mice are more sensitive to oxidative stress and have an altered phenotype that must be taken into account when considering the additional effects of increased levels of proteins such as Doppel. The implication of these results is that the consequence of genetic ablation of genes must include biochemical analysis as well as analyses of possible developmental and behavioral changes. © 2002 Wiley-Liss, Inc." @default.
- W2022131253 created "2016-06-24" @default.
- W2022131253 creator A5019481679 @default.
- W2022131253 creator A5047374526 @default.
- W2022131253 creator A5091019722 @default.
- W2022131253 date "2001-12-30" @default.
- W2022131253 modified "2023-10-15" @default.
- W2022131253 title "Lack of prion protein expression results in a neuronal phenotype sensitive to stress" @default.
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- W2022131253 doi "https://doi.org/10.1002/jnr.10118" @default.
- W2022131253 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11782965" @default.
- W2022131253 hasPublicationYear "2001" @default.
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