In vitro screening on amyloid beta modulation of aqueous extracts from plant seeds

Introduction: Glycation process might contribute to both extensive protein cross-linking and oxidative stress in Alzheimer's disease (AD). The amyloid-like aggregation of glycated bovine serum albumin induces apoptosis in the neuronal cell. Dietary supplementation of antioxidants, vitamins, and...

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Main Authors: Yoshinori Okada, Mizue Okada
Format: Article
Language:English
Published: Wolters Kluwer Medknow Publications 2016-01-01
Series:Journal of Pharmacy and Bioallied Sciences
Subjects:
Online Access:http://www.jpbsonline.org/article.asp?issn=0975-7406;year=2016;volume=8;issue=2;spage=141;epage=145;aulast=Okada
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author Yoshinori Okada
Mizue Okada
author_facet Yoshinori Okada
Mizue Okada
author_sort Yoshinori Okada
collection DOAJ
description Introduction: Glycation process might contribute to both extensive protein cross-linking and oxidative stress in Alzheimer's disease (AD). The amyloid-like aggregation of glycated bovine serum albumin induces apoptosis in the neuronal cell. Dietary supplementation of antioxidants, vitamins, and polyphenols are beneficial to AD, and consumption of fruits and vegetables reduce the risk of AD. We conducted a screening of 14 aqueous extracts from plant seeds (PSAE) for inhibitory activity on amyloid beta (Aβ). Materials and Methods: To examine the effects of PSAE on the Aβ (1–42) concentration, PSAE were analyzed by Aβ (1–42) enzyme-linked immunosorbent assay. Furthermore, we carried out an antiglycation experiment of PSAE and an antiaggregation experiment of PSAE to confirm the modification mechanism of PSAE. PSAE were added to buffer containing D-ribose and albumins. The solutions were incubated at 37 °C for 10 days. After incubation, the products were assayed on a fluorophotometer. Results: PSAE associated differential reduction in the levels of Aβ (1–42) (lettuce; 98.7% ± 2.4%, bitter melon; 95.9% ± 2.6%, and corn; 93.9% ± 2.1%), demonstrating that treatment with lettuce seeds extracts (LSE) effectively decreases Aβ (1–42) concentration. Among the 14 PSAE, LSE exhibited the second greatest potential for antiglycation. Inhibition of aggregates was not recognized in LSE. Conclusion: These results suggest that LSE reduces the toxicity of Aβ by modifying Aβ.
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spelling doaj.art-423415a7e0934a24ac2c0058244baa872022-12-22T02:04:07ZengWolters Kluwer Medknow PublicationsJournal of Pharmacy and Bioallied Sciences0975-74060976-48792016-01-018214114510.4103/0975-7406.171688In vitro screening on amyloid beta modulation of aqueous extracts from plant seedsYoshinori OkadaMizue OkadaIntroduction: Glycation process might contribute to both extensive protein cross-linking and oxidative stress in Alzheimer's disease (AD). The amyloid-like aggregation of glycated bovine serum albumin induces apoptosis in the neuronal cell. Dietary supplementation of antioxidants, vitamins, and polyphenols are beneficial to AD, and consumption of fruits and vegetables reduce the risk of AD. We conducted a screening of 14 aqueous extracts from plant seeds (PSAE) for inhibitory activity on amyloid beta (Aβ). Materials and Methods: To examine the effects of PSAE on the Aβ (1–42) concentration, PSAE were analyzed by Aβ (1–42) enzyme-linked immunosorbent assay. Furthermore, we carried out an antiglycation experiment of PSAE and an antiaggregation experiment of PSAE to confirm the modification mechanism of PSAE. PSAE were added to buffer containing D-ribose and albumins. The solutions were incubated at 37 °C for 10 days. After incubation, the products were assayed on a fluorophotometer. Results: PSAE associated differential reduction in the levels of Aβ (1–42) (lettuce; 98.7% ± 2.4%, bitter melon; 95.9% ± 2.6%, and corn; 93.9% ± 2.1%), demonstrating that treatment with lettuce seeds extracts (LSE) effectively decreases Aβ (1–42) concentration. Among the 14 PSAE, LSE exhibited the second greatest potential for antiglycation. Inhibition of aggregates was not recognized in LSE. Conclusion: These results suggest that LSE reduces the toxicity of Aβ by modifying Aβ.http://www.jpbsonline.org/article.asp?issn=0975-7406;year=2016;volume=8;issue=2;spage=141;epage=145;aulast=OkadaAggregationamyloid βglycationlettuceplant seed
spellingShingle Yoshinori Okada
Mizue Okada
In vitro screening on amyloid beta modulation of aqueous extracts from plant seeds
Journal of Pharmacy and Bioallied Sciences
Aggregation
amyloid β
glycation
lettuce
plant seed
title In vitro screening on amyloid beta modulation of aqueous extracts from plant seeds
title_full In vitro screening on amyloid beta modulation of aqueous extracts from plant seeds
title_fullStr In vitro screening on amyloid beta modulation of aqueous extracts from plant seeds
title_full_unstemmed In vitro screening on amyloid beta modulation of aqueous extracts from plant seeds
title_short In vitro screening on amyloid beta modulation of aqueous extracts from plant seeds
title_sort in vitro screening on amyloid beta modulation of aqueous extracts from plant seeds
topic Aggregation
amyloid β
glycation
lettuce
plant seed
url http://www.jpbsonline.org/article.asp?issn=0975-7406;year=2016;volume=8;issue=2;spage=141;epage=145;aulast=Okada
work_keys_str_mv AT yoshinoriokada invitroscreeningonamyloidbetamodulationofaqueousextractsfromplantseeds
AT mizueokada invitroscreeningonamyloidbetamodulationofaqueousextractsfromplantseeds