Year-end Sale % OFF 
Abstract
The pathological features of Alzheimer’s disease (AD) include senile plaques induced by amyloid-β (Aβ) protein deposits, neurofibrillary tangles formed by aggregates of hyperphosphorylated tau proteins and neuronal cell loss in specific position within the brain. Recent observations have suggested the possibility of an association between AD and cellular prion protein (PrPC) levels. PrPC is a high affinity receptor for oligomeric Aβ and is important for Aβ-induced neurotoxicity and thus plays a critical role in AD pathogenesis. The determination of the relationship between PrPC and AD and the characterization of PrPC binding to Aβ will facilitate the development of novel therapies for AD.
Highlights
Alzheimer’s disease (AD) is a progressive neurodegenerative disorder representing the most common cause of dementia in the elderly
This study revealed Pyk2 as a direct tyrosine kinase of tau that is active downstream of Fyn (Li and Gotz, 2018)
Some literature reports that PrPC deletion does not inhibit the toxic effects of Aβ oligomers
Summary
Alzheimer’s disease (AD) is a progressive neurodegenerative disorder representing the most common cause of dementia in the elderly. Have important implications regarding the pathophysiological consequences of Aβ-PrPC interactions (Zou et al, 2011) These studies strongly suggest that N-terminal residues 23–27 and the 95–110 region of PrPC contain the critical amino acid binding sequence for oligomer Aβ-induced synaptic impairment and neuronal cell death (Figure 2A and Table 1). These soluble recombinant PrP proteins and their fragments are strong inhibitors of the cytotoxic and synaptotoxic effects of Aβ42. A separate study indicated that PrPC shows strong binding to high molecular mass assemblies of Aβ (158–300 kDa) derived from the brains of Alzheimer’s disease patients, but not to small synthetic oligomeric Aβ42 (Dohler et al, 2014).
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
