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Attenuation of glycation-induced multiple protein modifications by Indian antidiabetic plant extracts

Context: Protein glycation is the major contributing factor in the development of diabetic complications. The antiglycation potential of medicinal plants provides a promising opportunity as complementary interventions for complications. Objective: To investigate the antiglycation potential of 19 med...

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Autores principales: Tupe, Rashmi S., Kemse, Nisha G., Khaire, Amrita A., Shaikh, Shamim A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7011994/
https://www.ncbi.nlm.nih.gov/pubmed/27608964
http://dx.doi.org/10.1080/13880209.2016.1228683
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author Tupe, Rashmi S.
Kemse, Nisha G.
Khaire, Amrita A.
Shaikh, Shamim A.
author_facet Tupe, Rashmi S.
Kemse, Nisha G.
Khaire, Amrita A.
Shaikh, Shamim A.
author_sort Tupe, Rashmi S.
collection PubMed
description Context: Protein glycation is the major contributing factor in the development of diabetic complications. The antiglycation potential of medicinal plants provides a promising opportunity as complementary interventions for complications. Objective: To investigate the antiglycation potential of 19 medicinal plants extracts using albumin by estimating different indicators: (1) glycation (early and late), (2) albumin oxidation, and (3) amyloid aggregation. Materials and methods: The effect of aqueous plant extracts (1% w/v) on protein glycation was assessed by incubating albumin (10 mg/mL) with fructose (250 mM) for 4 days. Degree of protein glycation in the absence and presence of plant extracts was assessed by estimating fructosamine, advanced glycation end products (AGEs), carbonyls, free thiol group and β-amyloid aggregation. Results: Petroselinum crispum, Boerhavia diffusa, Terminalia chebula, Swertia chirayita and Glycyrrhiza glabra showed significant antiglycating activity. P. crispum and A. barbadensis inhibited the carbonyl stress and protected the thiol group from oxidative damage. There was significant correlation between protein thiols and amyloid inhibition (R = −.69, p < .001). Conclusion: P. crispum, B. diffusa and T. chebula had the most potent antiglycation activity. These plant exerted noticeable antiglycation activity at different glycation modifications of albumin. These findings are important for identifying plants with potential to combat diabetic complications.
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spelling pubmed-70119942020-02-24 Attenuation of glycation-induced multiple protein modifications by Indian antidiabetic plant extracts Tupe, Rashmi S. Kemse, Nisha G. Khaire, Amrita A. Shaikh, Shamim A. Pharm Biol Research Article Context: Protein glycation is the major contributing factor in the development of diabetic complications. The antiglycation potential of medicinal plants provides a promising opportunity as complementary interventions for complications. Objective: To investigate the antiglycation potential of 19 medicinal plants extracts using albumin by estimating different indicators: (1) glycation (early and late), (2) albumin oxidation, and (3) amyloid aggregation. Materials and methods: The effect of aqueous plant extracts (1% w/v) on protein glycation was assessed by incubating albumin (10 mg/mL) with fructose (250 mM) for 4 days. Degree of protein glycation in the absence and presence of plant extracts was assessed by estimating fructosamine, advanced glycation end products (AGEs), carbonyls, free thiol group and β-amyloid aggregation. Results: Petroselinum crispum, Boerhavia diffusa, Terminalia chebula, Swertia chirayita and Glycyrrhiza glabra showed significant antiglycating activity. P. crispum and A. barbadensis inhibited the carbonyl stress and protected the thiol group from oxidative damage. There was significant correlation between protein thiols and amyloid inhibition (R = −.69, p < .001). Conclusion: P. crispum, B. diffusa and T. chebula had the most potent antiglycation activity. These plant exerted noticeable antiglycation activity at different glycation modifications of albumin. These findings are important for identifying plants with potential to combat diabetic complications. Taylor & Francis 2016-09-08 /pmc/articles/PMC7011994/ /pubmed/27608964 http://dx.doi.org/10.1080/13880209.2016.1228683 Text en © 2016 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. http://creativecommons.org/Licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/Licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Tupe, Rashmi S.
Kemse, Nisha G.
Khaire, Amrita A.
Shaikh, Shamim A.
Attenuation of glycation-induced multiple protein modifications by Indian antidiabetic plant extracts
title Attenuation of glycation-induced multiple protein modifications by Indian antidiabetic plant extracts
title_full Attenuation of glycation-induced multiple protein modifications by Indian antidiabetic plant extracts
title_fullStr Attenuation of glycation-induced multiple protein modifications by Indian antidiabetic plant extracts
title_full_unstemmed Attenuation of glycation-induced multiple protein modifications by Indian antidiabetic plant extracts
title_short Attenuation of glycation-induced multiple protein modifications by Indian antidiabetic plant extracts
title_sort attenuation of glycation-induced multiple protein modifications by indian antidiabetic plant extracts
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7011994/
https://www.ncbi.nlm.nih.gov/pubmed/27608964
http://dx.doi.org/10.1080/13880209.2016.1228683
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