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• W4297200533 abstract "Neurodegenerative diseases are associated with a multitude of dysfunctional cellular pathways. One major contributory factor is a redox stress challenge during the development of several protein misfolding conditions including Alzheimer's (AD), Parkinson's disease (PD), and less common conditions such as Creutzfeldt Jakob disease (CJD). CJD is caused by misfolding of the neuronal prion protein and is characterised by a neurotoxic unfolded protein response involving chronic endoplasmic reticulum stress, reduced protein translation and spongiosis leading subsequently to synaptic and neuronal loss. Here we have characterised prion disease in mice to assess redox stress components including nitrergic and oxidative markers associated with neuroinflammatory activation. Aberrant regulation of the homeostasis of several redox metals contributes to the overall cellular redox stress and we have identified altered levels of iron, copper, zinc, and manganese in the hippocampus of prion diseased mice. Our data show that early in disease, there is evidence for oxidative stress in conjunction with reduced antioxidant superoxide dismutase mRNA and protein expression. Moreover, expression of divalent metal transporter proteins was reduced for Atp7b, Atox1, Slc11a2, Slc39a14 at 6-7 weeks but increased for Slc39a14 and Mt1 at 10 weeks of disease. Our data present evidence for a strong pro-oxidant environment and altered redox metal homeostasis in early disease pathology which both may be contributory factors to aggravating this protein misfolding disease." @default.
• W4297200533 created "2022-09-27" @default.
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• W4297200533 date "2022-11-01" @default.
• W4297200533 modified "2023-09-29" @default.
• W4297200533 title "Redox stress and metal dys-homeostasis appear as hallmarks of early prion disease pathogenesis in mice" @default.
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• W4297200533 doi "https://doi.org/10.1016/j.freeradbiomed.2022.09.025" @default.
• W4297200533 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36170956" @default.
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