The role of astrocytes in amyloid production and Alzheimer's disease
Alzheimer's disease (AD) is marked by the presence of extracellular amyloid beta (Aβ) plaques, intracellular neurofibrillary tangles (NFTs) and gliosis, activated glial cells, in the brain. It is thought that Aβ plaques trigger NFT formation, neuronal cell death, neuroinflammation and gliosis a...
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| Published in | Open biology Vol. 7; no. 12; p. 170228 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
England
The Royal Society
01.12.2017
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Alzheimer's disease (AD) is marked by the presence of extracellular amyloid beta (Aβ) plaques, intracellular neurofibrillary tangles (NFTs) and gliosis, activated glial cells, in the brain. It is thought that Aβ plaques trigger NFT formation, neuronal cell death, neuroinflammation and gliosis and, ultimately, cognitive impairment. There are increased numbers of reactive astrocytes in AD, which surround amyloid plaques and secrete proinflammatory factors and can phagocytize and break down Aβ. It was thought that neuronal cells were the major source of Aβ. However, mounting evidence suggests that astrocytes may play an additional role in AD by secreting significant quantities of Aβ and contributing to overall amyloid burden in the brain. Astrocytes are the most numerous cell type in the brain, and therefore even minor quantities of amyloid secretion from individual astrocytes could prove to be substantial when taken across the whole brain. Reactive astrocytes have increased levels of the three necessary components for Aβ production: amyloid precursor protein, β-secretase (BACE1) and γ-secretase. The identification of environmental factors, such as neuroinflammation, that promote astrocytic Aβ production, could redefine how we think about developing therapeutics for AD. |
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| AbstractList | Alzheimer's disease (AD) is marked by the presence of extracellular amyloid beta (Aβ) plaques, intracellular neurofibrillary tangles (NFTs) and gliosis, activated glial cells, in the brain. It is thought that Aβ plaques trigger NFT formation, neuronal cell death, neuroinflammation and gliosis and, ultimately, cognitive impairment. There are increased numbers of reactive astrocytes in AD, which surround amyloid plaques and secrete proinflammatory factors and can phagocytize and break down Aβ. It was thought that neuronal cells were the major source of Aβ. However, mounting evidence suggests that astrocytes may play an additional role in AD by secreting significant quantities of Aβ and contributing to overall amyloid burden in the brain. Astrocytes are the most numerous cell type in the brain, and therefore even minor quantities of amyloid secretion from individual astrocytes could prove to be substantial when taken across the whole brain. Reactive astrocytes have increased levels of the three necessary components for Aβ production: amyloid precursor protein, β-secretase (BACE1) and γ-secretase. The identification of environmental factors, such as neuroinflammation, that promote astrocytic Aβ production, could redefine how we think about developing therapeutics for AD. Alzheimer's disease (AD) is marked by the presence of extracellular amyloid beta (Aβ) plaques, intracellular neurofibrillary tangles (NFTs) and gliosis, activated glial cells, in the brain. It is thought that Aβ plaques trigger NFT formation, neuronal cell death, neuroinflammation and gliosis and, ultimately, cognitive impairment. There are increased numbers of reactive astrocytes in AD, which surround amyloid plaques and secrete proinflammatory factors and can phagocytize and break down Aβ. It was thought that neuronal cells were the major source of Aβ. However, mounting evidence suggests that astrocytes may play an additional role in AD by secreting significant quantities of Aβ and contributing to overall amyloid burden in the brain. Astrocytes are the most numerous cell type in the brain, and therefore even minor quantities of amyloid secretion from individual astrocytes could prove to be substantial when taken across the whole brain. Reactive astrocytes have increased levels of the three necessary components for Aβ production: amyloid precursor protein, β-secretase (BACE1) and γ-secretase. The identification of environmental factors, such as neuroinflammation, that promote astrocytic Aβ production, could redefine how we think about developing therapeutics for AD.Alzheimer's disease (AD) is marked by the presence of extracellular amyloid beta (Aβ) plaques, intracellular neurofibrillary tangles (NFTs) and gliosis, activated glial cells, in the brain. It is thought that Aβ plaques trigger NFT formation, neuronal cell death, neuroinflammation and gliosis and, ultimately, cognitive impairment. There are increased numbers of reactive astrocytes in AD, which surround amyloid plaques and secrete proinflammatory factors and can phagocytize and break down Aβ. It was thought that neuronal cells were the major source of Aβ. However, mounting evidence suggests that astrocytes may play an additional role in AD by secreting significant quantities of Aβ and contributing to overall amyloid burden in the brain. Astrocytes are the most numerous cell type in the brain, and therefore even minor quantities of amyloid secretion from individual astrocytes could prove to be substantial when taken across the whole brain. Reactive astrocytes have increased levels of the three necessary components for Aβ production: amyloid precursor protein, β-secretase (BACE1) and γ-secretase. The identification of environmental factors, such as neuroinflammation, that promote astrocytic Aβ production, could redefine how we think about developing therapeutics for AD. |
| Author | Frost, Georgia R. Li, Yue-Ming |
| AuthorAffiliation | 1 Chemical Biology Program, Memorial Sloan Kettering Cancer Center , New York, NY 10065 , USA 3 Pharmacology, Weill Graduate School of Medical Sciences of Cornell University , New York, NY , USA 2 Programs of Neurosciences, Weill Graduate School of Medical Sciences of Cornell University , New York, NY , USA |
| AuthorAffiliation_xml | – name: 1 Chemical Biology Program, Memorial Sloan Kettering Cancer Center , New York, NY 10065 , USA – name: 2 Programs of Neurosciences, Weill Graduate School of Medical Sciences of Cornell University , New York, NY , USA – name: 3 Pharmacology, Weill Graduate School of Medical Sciences of Cornell University , New York, NY , USA |
| Author_xml | – sequence: 1 givenname: Georgia R. surname: Frost fullname: Frost, Georgia R. email: frostg@mskcc.org organization: Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA; Programs of Neurosciences, Weill Graduate School of Medical Sciences of Cornell University, New York, NY, USA – sequence: 2 givenname: Yue-Ming orcidid: 0000-0002-2633-3730 surname: Li fullname: Li, Yue-Ming organization: Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA; Programs of Neurosciences, Weill Graduate School of Medical Sciences of Cornell University, New York, NY, USA; Pharmacology, Weill Graduate School of Medical Sciences of Cornell University, New York, NY, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29237809$$D View this record in MEDLINE/PubMed |
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| Snippet | Alzheimer's disease (AD) is marked by the presence of extracellular amyloid beta (Aβ) plaques, intracellular neurofibrillary tangles (NFTs) and gliosis,... |
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| StartPage | 170228 |
| SubjectTerms | Alzheimer Disease - metabolism Alzheimer Disease - pathology Alzheimer's Disease Amyloid Beta Amyloid beta-Protein Precursor - genetics Amyloid beta-Protein Precursor - metabolism Amyloid Precursor Protein Secretases - genetics Amyloid Precursor Protein Secretases - metabolism Animals Aspartic Acid Endopeptidases - genetics Aspartic Acid Endopeptidases - metabolism Astrocytes - metabolism Astrocytes - pathology Astrogliosis Humans Neuroinflammation Review |
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| Title | The role of astrocytes in amyloid production and Alzheimer's disease |
| URI | https://royalsocietypublishing.org/doi/full/10.1098/rsob.170228 https://www.ncbi.nlm.nih.gov/pubmed/29237809 https://www.proquest.com/docview/1977203251 https://pubmed.ncbi.nlm.nih.gov/PMC5746550 https://doaj.org/article/32d173c1db1f4805b6b9481d5afb58a4 |
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