Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cells
Abstract 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 pro...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2023-08-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-023-40291-6 |
| _version_ | 1797452593291591680 |
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| author | Reshmee Bhattacharya Saakshi Saini Souvik Ghosh Partha Roy Nemat Ali Mohammad Khalid Parvez Mohammed S. Al-Dosari Awdhesh Kumar Mishra Laishram Rajendrakumar Singh |
| author_facet | Reshmee Bhattacharya Saakshi Saini Souvik Ghosh Partha Roy Nemat Ali Mohammad Khalid Parvez Mohammed S. Al-Dosari Awdhesh Kumar Mishra Laishram Rajendrakumar Singh |
| author_sort | Reshmee Bhattacharya |
| collection | DOAJ |
| description | Abstract 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. |
| first_indexed | 2024-03-09T15:09:54Z |
| format | Article |
| id | doaj.art-87fa448f336b43d0b379cef4ab4591f5 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-03-09T15:09:54Z |
| publishDate | 2023-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-87fa448f336b43d0b379cef4ab4591f52023-11-26T13:24:57ZengNature PortfolioScientific Reports2045-23222023-08-0113111610.1038/s41598-023-40291-6Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cellsReshmee Bhattacharya0Saakshi Saini1Souvik Ghosh2Partha Roy3Nemat Ali4Mohammad Khalid Parvez5Mohammed S. Al-Dosari6Awdhesh Kumar Mishra7Laishram Rajendrakumar Singh8Dr. B. R. Ambedkar Center for Biomedical Research, University of DelhiDepartment of Biosciences and Bioengineering, IIT RoorkeeDepartment of Biosciences and Bioengineering, IIT RoorkeeDepartment of Biosciences and Bioengineering, IIT RoorkeeDepartment of Pharmacology and Toxicology, College of Pharmacy, King Saud UniversityDepartment of Pharmacognosy, College of Pharmacy, King Saud UniversityDepartment of Pharmacognosy, College of Pharmacy, King Saud UniversityDepartment of Biotechnology, Yeungnam UniversityDr. B. R. Ambedkar Center for Biomedical Research, University of DelhiAbstract 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.https://doi.org/10.1038/s41598-023-40291-6 |
| spellingShingle | Reshmee Bhattacharya Saakshi Saini Souvik Ghosh Partha Roy Nemat Ali Mohammad Khalid Parvez Mohammed S. Al-Dosari Awdhesh Kumar Mishra Laishram Rajendrakumar Singh Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cells Scientific Reports |
| 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 |
| url | https://doi.org/10.1038/s41598-023-40291-6 |
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