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Protective effect of Nelumbo nucifera extracts on beta amyloid protein induced apoptosis in PC12 cells, in vitro model of Alzheimer’s disease
Alzheimer’s disease (AD) is the most common cause of dementia in the elderly. β-Amyloid (Aβ) has been proposed to play a role in the pathogenesis of AD. Deposits of insoluble Aβ are found in the brains of patients with AD and are one of the pathological hallmarks of the disease, but the underlying s...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Taiwan Food and Drug Administration
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9332666/ https://www.ncbi.nlm.nih.gov/pubmed/29389553 http://dx.doi.org/10.1016/j.jfda.2017.01.007 |
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author | Kumaran, Alaganandam Ho, Cheng Chang Hwang, Lucy Sun |
author_facet | Kumaran, Alaganandam Ho, Cheng Chang Hwang, Lucy Sun |
author_sort | Kumaran, Alaganandam |
collection | PubMed |
description | Alzheimer’s disease (AD) is the most common cause of dementia in the elderly. β-Amyloid (Aβ) has been proposed to play a role in the pathogenesis of AD. Deposits of insoluble Aβ are found in the brains of patients with AD and are one of the pathological hallmarks of the disease, but the underlying signaling pathways are poorly understood. In order to develop antidementia agents with potential therapeutic value, we examined the inhibitory effect of the Nelumbo nucifera seed embryo extracts on to the aggregated amyloid β peptide (agg Aβ(1–40))-induced damage of differentiated PC-12 cells (dPC-12), a well-known cell model for AD. In the present study, seed embryos of N. nucifera were extracted with 70% methanol in water and then separated into hexane, ethyl acetate, n-butanol, and water layers. Among them, only the n-butanol layer showed strong activity and was therefore subjected to separation on Sephadex LH-20 chromatography. Two fractions showing potent activity were found to significantly inhibit Aβ(1–40) toxicity on dPC-12 cells in increasing order of concentration (10–50 μg/mL). Further purification and characterization of these active fractions identified them to be flavonoids such as rutin, orientin, isoorientin, isoquercetrin, and hyperoside. 2,2-Diphenyl-1-picrylhydrazyl hydrate scavenging activity of the extracts was also carried out to ascertain the possible mechanism of the activity. |
format | Online Article Text |
id | pubmed-9332666 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Taiwan Food and Drug Administration |
record_format | MEDLINE/PubMed |
spelling | pubmed-93326662022-08-09 Protective effect of Nelumbo nucifera extracts on beta amyloid protein induced apoptosis in PC12 cells, in vitro model of Alzheimer’s disease Kumaran, Alaganandam Ho, Cheng Chang Hwang, Lucy Sun J Food Drug Anal Original Article Alzheimer’s disease (AD) is the most common cause of dementia in the elderly. β-Amyloid (Aβ) has been proposed to play a role in the pathogenesis of AD. Deposits of insoluble Aβ are found in the brains of patients with AD and are one of the pathological hallmarks of the disease, but the underlying signaling pathways are poorly understood. In order to develop antidementia agents with potential therapeutic value, we examined the inhibitory effect of the Nelumbo nucifera seed embryo extracts on to the aggregated amyloid β peptide (agg Aβ(1–40))-induced damage of differentiated PC-12 cells (dPC-12), a well-known cell model for AD. In the present study, seed embryos of N. nucifera were extracted with 70% methanol in water and then separated into hexane, ethyl acetate, n-butanol, and water layers. Among them, only the n-butanol layer showed strong activity and was therefore subjected to separation on Sephadex LH-20 chromatography. Two fractions showing potent activity were found to significantly inhibit Aβ(1–40) toxicity on dPC-12 cells in increasing order of concentration (10–50 μg/mL). Further purification and characterization of these active fractions identified them to be flavonoids such as rutin, orientin, isoorientin, isoquercetrin, and hyperoside. 2,2-Diphenyl-1-picrylhydrazyl hydrate scavenging activity of the extracts was also carried out to ascertain the possible mechanism of the activity. Taiwan Food and Drug Administration 2017-03-17 /pmc/articles/PMC9332666/ /pubmed/29389553 http://dx.doi.org/10.1016/j.jfda.2017.01.007 Text en © 2018 Taiwan Food and Drug Administration https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC-BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) ). |
spellingShingle | Original Article Kumaran, Alaganandam Ho, Cheng Chang Hwang, Lucy Sun Protective effect of Nelumbo nucifera extracts on beta amyloid protein induced apoptosis in PC12 cells, in vitro model of Alzheimer’s disease |
title | Protective effect of Nelumbo nucifera extracts on beta amyloid protein induced apoptosis in PC12 cells, in vitro model of Alzheimer’s disease |
title_full | Protective effect of Nelumbo nucifera extracts on beta amyloid protein induced apoptosis in PC12 cells, in vitro model of Alzheimer’s disease |
title_fullStr | Protective effect of Nelumbo nucifera extracts on beta amyloid protein induced apoptosis in PC12 cells, in vitro model of Alzheimer’s disease |
title_full_unstemmed | Protective effect of Nelumbo nucifera extracts on beta amyloid protein induced apoptosis in PC12 cells, in vitro model of Alzheimer’s disease |
title_short | Protective effect of Nelumbo nucifera extracts on beta amyloid protein induced apoptosis in PC12 cells, in vitro model of Alzheimer’s disease |
title_sort | protective effect of nelumbo nucifera extracts on beta amyloid protein induced apoptosis in pc12 cells, in vitro model of alzheimer’s disease |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9332666/ https://www.ncbi.nlm.nih.gov/pubmed/29389553 http://dx.doi.org/10.1016/j.jfda.2017.01.007 |
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