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Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cells

Diabetes, characterized by high blood glucose level, is a progressive metabolic disease that leads to serious health complications. One of the major pathological consequences associated with diabetes is the accumulation of highly reactive carbonyl compounds called advanced glycation end products (AG...

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Autores principales: Bhattacharya, Reshmee, Saini, Saakshi, Ghosh, Souvik, Roy, Partha, Ali, Nemat, Parvez, Mohammad Khalid, Al-Dosari, Mohammed S., Mishra, Awdhesh Kumar, Singh, Laishram Rajendrakumar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10421908/
https://www.ncbi.nlm.nih.gov/pubmed/37567958
http://dx.doi.org/10.1038/s41598-023-40291-6
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author Bhattacharya, Reshmee
Saini, Saakshi
Ghosh, Souvik
Roy, Partha
Ali, Nemat
Parvez, Mohammad Khalid
Al-Dosari, Mohammed S.
Mishra, Awdhesh Kumar
Singh, Laishram Rajendrakumar
author_facet Bhattacharya, Reshmee
Saini, Saakshi
Ghosh, Souvik
Roy, Partha
Ali, Nemat
Parvez, Mohammad Khalid
Al-Dosari, Mohammed S.
Mishra, Awdhesh Kumar
Singh, Laishram Rajendrakumar
author_sort Bhattacharya, Reshmee
collection PubMed
description Diabetes, characterized by high blood glucose level, is a progressive metabolic disease that leads to serious health complications. One of the major pathological consequences associated with diabetes is the accumulation of highly reactive carbonyl compounds called advanced glycation end products (AGEs). Most of the AGEs are dicarbonyls and have the potential to covalently modify proteins especially at the lysine residues in a non-enzymatic fashion (a process termed as glycation) resulting in the functional impairment and/or toxic gain in function. Therefore, non-toxic small molecules that can inhibit glycation are of interest for the therapeutic intervention of diabetes. In the present communication, we have investigated the effect of organosulfurs (S-allyl cysteine, SAC and N-acetyl cysteine, NAC) that are major principal components of Allium sativa against the glycation of different proteins. We discovered that both SAC and NAC are potent anti-glycating agents. We also found that both SAC and NAC reduce ROS level and inhibit apoptosis caused by protein glycation.
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spelling pubmed-104219082023-08-13 Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cells Bhattacharya, Reshmee Saini, Saakshi Ghosh, Souvik Roy, Partha Ali, Nemat Parvez, Mohammad Khalid Al-Dosari, Mohammed S. Mishra, Awdhesh Kumar Singh, Laishram Rajendrakumar Sci Rep Article Diabetes, characterized by high blood glucose level, is a progressive metabolic disease that leads to serious health complications. One of the major pathological consequences associated with diabetes is the accumulation of highly reactive carbonyl compounds called advanced glycation end products (AGEs). Most of the AGEs are dicarbonyls and have the potential to covalently modify proteins especially at the lysine residues in a non-enzymatic fashion (a process termed as glycation) resulting in the functional impairment and/or toxic gain in function. Therefore, non-toxic small molecules that can inhibit glycation are of interest for the therapeutic intervention of diabetes. In the present communication, we have investigated the effect of organosulfurs (S-allyl cysteine, SAC and N-acetyl cysteine, NAC) that are major principal components of Allium sativa against the glycation of different proteins. We discovered that both SAC and NAC are potent anti-glycating agents. We also found that both SAC and NAC reduce ROS level and inhibit apoptosis caused by protein glycation. Nature Publishing Group UK 2023-08-11 /pmc/articles/PMC10421908/ /pubmed/37567958 http://dx.doi.org/10.1038/s41598-023-40291-6 Text en © The Author(s) 2023, corrected publication 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Bhattacharya, Reshmee
Saini, Saakshi
Ghosh, Souvik
Roy, Partha
Ali, Nemat
Parvez, Mohammad Khalid
Al-Dosari, Mohammed S.
Mishra, Awdhesh Kumar
Singh, Laishram Rajendrakumar
Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cells
title Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cells
title_full Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cells
title_fullStr Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cells
title_full_unstemmed Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cells
title_short Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cells
title_sort organosulfurs, s-allyl cysteine and n-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in ht22 cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10421908/
https://www.ncbi.nlm.nih.gov/pubmed/37567958
http://dx.doi.org/10.1038/s41598-023-40291-6
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