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oapen-20.500.12657-55106
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oapen-20.500.12657-551062022-06-01T03:11:43Z Structural and functional aspects of membranes Evangelisti, Elisa bic Book Industry Communication::P Mathematics & science::PS Biology, life sciences::PSB Biochemistry Alzheimer’s disease (AD) is a common form of dementia characterized by the formation of extracellular senile plaques composed of aggregated amyloid peptide (Aβ). The present studies provide evidence that: cell resistance to amyloid toxicity is related to lipid raft cholesterol content. Cholesterol and GM1, affect the susceptibility of Familial Alzheimer’s Disease (FAD) broblasts to Aβ42 oligomers in opposite ways, by modulating amyloid binding to lipid rafts and its subsequent toxic effects. The degree of toxicity of the oligomeric species results from a complex interplay between the structural and physicochemical features of both the oligomers and the cellular membrane. Neuronal differentiation of human mesenchymal stromal cells increases their resistance to Aβ42 aggregate toxicity. 2022-05-31T10:21:16Z 2022-05-31T10:21:16Z 2013 book ONIX_20220531_9788866554455_390 2612-8020 9788866554455 9788866554448 9788892734715 https://library.oapen.org/handle/20.500.12657/55106 eng Premio Tesi di Dottorato application/pdf n/a 9788866554455.pdf https://books.fupress.com/isbn/9788866554455 Firenze University Press 10.36253/978-88-6655-445-5 10.36253/978-88-6655-445-5 bf65d21a-78e5-4ba2-983a-dbfa90962870 9788866554455 9788866554448 9788892734715 31 152 Florence open access
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OAPEN
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DSpace
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| language |
English
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| description |
Alzheimer’s disease (AD) is a common form of dementia characterized by the formation of extracellular senile plaques composed of aggregated amyloid peptide (Aβ). The present studies provide evidence that: cell resistance to amyloid toxicity is related to lipid raft cholesterol content. Cholesterol and GM1, affect the susceptibility of Familial Alzheimer’s Disease (FAD) broblasts to Aβ42 oligomers in opposite ways, by modulating amyloid binding to lipid rafts and its subsequent toxic effects. The degree of toxicity of the oligomeric species results from a complex interplay between the structural and physicochemical features of both the oligomers and the cellular membrane. Neuronal differentiation of human mesenchymal stromal cells increases their resistance to Aβ42 aggregate toxicity.
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| title |
9788866554455.pdf
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| spellingShingle |
9788866554455.pdf
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| title_short |
9788866554455.pdf
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| title_full |
9788866554455.pdf
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| title_fullStr |
9788866554455.pdf
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| title_full_unstemmed |
9788866554455.pdf
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| title_sort |
9788866554455.pdf
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| publisher |
Firenze University Press
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| publishDate |
2022
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| url |
https://books.fupress.com/isbn/9788866554455
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| _version_ |
1771297587544981504
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