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Transmissible Spongiform Encephalopathies (TSEs) Essay

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Prion diseases or transmissible spongiform encephalopathies (TSEs) are a family of rare progressive neurodegenerative disorders that affect both humans and animals. They are distinguished by long incubation periods, characteristic spongiform changes associated with neuronal loss, and a failure to induce inflammatory response. The proteinaceous infectious particles, prion was identified by an American neurologist Stanley B. Prusiner and colleagues in 1982derived from the words protein and infection (Stanley B. Prusiner -Autobiography). Prions are known to Creutzfeldt - Jakob disease (CJD), Gerstmann–Sträussler–Scheinker syndrome and Fatal Familiar Insomnia in humans. In mammals they cause "mad cow disease" in cattle. Prion diseases affect…show more content…
Moreover, different anti-PrP antibodies or their antigen-binding fragments that disrupt the PrP–Aβ interaction were able to block the Aβ-mediated disruption of synaptic plasticity. These findings were deemed exciting because they suggest the involvement of PrPC in Alzheimer's disease (AD) pathogenesis. However, others found that the absence of PrPC did not prevent deficits in hippocampal-dependent behavioral tests upon intracerebral Aβ injection (Krull & Nunnally, 2004).
PrPSc is identified as a surrogate marker and potential TSE agent. PrPSc formation was first detected in the murine neuroblastoma cell line N2a when exposed to mouse-adapted scrapie (Abbott, 2010).Subsequent infection experiments demonstrated susceptibility of N2a cells to several different mouse- adapted scrapie strains. Since then, several cell lines of neuronal and non-neuronal origin have been identified to be susceptible to a stable infection with prions. Once prions have successfully infected a cell line, they can replicate persistently over multiple cell passages, with very few exceptions, without any overt cytopathic effect (Shorter J, Lindquist S (June 2005). Cell lines that have been successfully infected include microglial cells as well as epithelial cells, fibroblasts and myoblasts, which have all been demonstrated to persistently replicate an array of prion strains in vitro. Curiously, a
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