Cellular Prion Protein as a Receptor of Toxic Amyloid-β42 Oligomers Is Important for Alzheimer’s Disease
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 sugges...
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| Published in | Frontiers in cellular neuroscience Vol. 13; p. 339 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
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30.07.2019
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| 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 (PrP
) levels. PrP
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 PrP
and AD and the characterization of PrP
binding to Aβ will facilitate the development of novel therapies for AD. |
|---|---|
| AbstractList | 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. 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 (PrP C ) levels. PrP C 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 PrP C and AD and the characterization of PrP C binding to Aβ will facilitate the development of novel therapies for AD. 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 (PrP ) levels. PrP 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 PrP and AD and the characterization of PrP binding to Aβ will facilitate the development of novel therapies for AD. 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 (PrP C ) levels. PrP C 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 PrP C and AD and the characterization of PrP C binding to Aβ will facilitate the development of novel therapies for AD.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 (PrP C ) levels. PrP C 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 PrP C and AD and the characterization of PrP C binding to Aβ will facilitate the development of novel therapies for AD. |
| Author | Yu, Wanpeng Chang, Wenguang Zhao, Yanfang Zhang, Yuan Wang, Yu Zhang, Lei |
| AuthorAffiliation | 1 Institute for Translational Medicine, Qingdao University , Qingdao , China 2 School for Life Science, Institute of Biomedical Research, Shandong University of Technology , Zibo , China |
| AuthorAffiliation_xml | – name: 1 Institute for Translational Medicine, Qingdao University , Qingdao , China – name: 2 School for Life Science, Institute of Biomedical Research, Shandong University of Technology , Zibo , China |
| Author_xml | – sequence: 1 givenname: Yuan surname: Zhang fullname: Zhang, Yuan – sequence: 2 givenname: Yanfang surname: Zhao fullname: Zhao, Yanfang – sequence: 3 givenname: Lei surname: Zhang fullname: Zhang, Lei – sequence: 4 givenname: Wanpeng surname: Yu fullname: Yu, Wanpeng – sequence: 5 givenname: Yu surname: Wang fullname: Wang, Yu – sequence: 6 givenname: Wenguang surname: Chang fullname: Chang, Wenguang |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31417361$$D View this record in MEDLINE/PubMed |
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| Keywords | amyloid-β receptor Alzheimer’s disease cellular prion protein oligomers |
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| SubjectTerms | Alzheimer's disease amyloid-β Binding sites Brain cellular prion protein Cognitive ability Disease Hypotheses Neurofibrillary tangles Neuroscience Neurotoxicity oligomers Pathogenesis Pathology Prion protein Proteins receptor Senile plaques Tau protein |
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| Title | Cellular Prion Protein as a Receptor of Toxic Amyloid-β42 Oligomers Is Important for Alzheimer’s Disease |
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