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Fermented Supernatants of Lactobacillus plantarum GKM3 and Bifidobacterium lactis GKK2 Protect against Protein Glycation and Inhibit Glycated Protein Ligation
With age, protein glycation in organisms increases continuously. Evidence from many studies shows that the accumulation of glycated protein is highly correlated with biological aging and the development of aging-related diseases, so developing a dietary agent to attenuate protein glycation is very m...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9864088/ https://www.ncbi.nlm.nih.gov/pubmed/36678147 http://dx.doi.org/10.3390/nu15020277 |
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author | Lin, Shih-Wei Wu, Chi-Hao Jao, Ya-Chien Tsai, You-Shan Chen, Yen-Lien Chen, Chin-Chu Fang, Tony J. Chau, Chi-Fai |
author_facet | Lin, Shih-Wei Wu, Chi-Hao Jao, Ya-Chien Tsai, You-Shan Chen, Yen-Lien Chen, Chin-Chu Fang, Tony J. Chau, Chi-Fai |
author_sort | Lin, Shih-Wei |
collection | PubMed |
description | With age, protein glycation in organisms increases continuously. Evidence from many studies shows that the accumulation of glycated protein is highly correlated with biological aging and the development of aging-related diseases, so developing a dietary agent to attenuate protein glycation is very meaningful. Previous studies have indicated that lactic acid bacteria-fermented products have diverse biological activities especially in anti-aging, so this study was aimed to investigate the inhibitory effect of the fermented supernatants of Lactobacillus plantarum GKM3 (GKM3) and Bifidobacterium lactis GKK2 (GKK2) on protein glycation. The results show that GKM3- and GKK2-fermented supernatants can significantly inhibit protein glycation by capturing a glycation agent (methylglyoxal) and/or protecting functional groups in protein against methylglyoxal-induced responses. GKM3- and GKK2-fermented supernatants can also significantly inhibit the binding of glycated proteins to the receptor for advanced glycation end products (RAGE). In conclusion, lactic acid bacteria fermentation products have the potential to attenuate biological aging by inhibiting protein glycation. |
format | Online Article Text |
id | pubmed-9864088 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-98640882023-01-22 Fermented Supernatants of Lactobacillus plantarum GKM3 and Bifidobacterium lactis GKK2 Protect against Protein Glycation and Inhibit Glycated Protein Ligation Lin, Shih-Wei Wu, Chi-Hao Jao, Ya-Chien Tsai, You-Shan Chen, Yen-Lien Chen, Chin-Chu Fang, Tony J. Chau, Chi-Fai Nutrients Article With age, protein glycation in organisms increases continuously. Evidence from many studies shows that the accumulation of glycated protein is highly correlated with biological aging and the development of aging-related diseases, so developing a dietary agent to attenuate protein glycation is very meaningful. Previous studies have indicated that lactic acid bacteria-fermented products have diverse biological activities especially in anti-aging, so this study was aimed to investigate the inhibitory effect of the fermented supernatants of Lactobacillus plantarum GKM3 (GKM3) and Bifidobacterium lactis GKK2 (GKK2) on protein glycation. The results show that GKM3- and GKK2-fermented supernatants can significantly inhibit protein glycation by capturing a glycation agent (methylglyoxal) and/or protecting functional groups in protein against methylglyoxal-induced responses. GKM3- and GKK2-fermented supernatants can also significantly inhibit the binding of glycated proteins to the receptor for advanced glycation end products (RAGE). In conclusion, lactic acid bacteria fermentation products have the potential to attenuate biological aging by inhibiting protein glycation. MDPI 2023-01-05 /pmc/articles/PMC9864088/ /pubmed/36678147 http://dx.doi.org/10.3390/nu15020277 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Lin, Shih-Wei Wu, Chi-Hao Jao, Ya-Chien Tsai, You-Shan Chen, Yen-Lien Chen, Chin-Chu Fang, Tony J. Chau, Chi-Fai Fermented Supernatants of Lactobacillus plantarum GKM3 and Bifidobacterium lactis GKK2 Protect against Protein Glycation and Inhibit Glycated Protein Ligation |
title | Fermented Supernatants of Lactobacillus plantarum GKM3 and Bifidobacterium lactis GKK2 Protect against Protein Glycation and Inhibit Glycated Protein Ligation |
title_full | Fermented Supernatants of Lactobacillus plantarum GKM3 and Bifidobacterium lactis GKK2 Protect against Protein Glycation and Inhibit Glycated Protein Ligation |
title_fullStr | Fermented Supernatants of Lactobacillus plantarum GKM3 and Bifidobacterium lactis GKK2 Protect against Protein Glycation and Inhibit Glycated Protein Ligation |
title_full_unstemmed | Fermented Supernatants of Lactobacillus plantarum GKM3 and Bifidobacterium lactis GKK2 Protect against Protein Glycation and Inhibit Glycated Protein Ligation |
title_short | Fermented Supernatants of Lactobacillus plantarum GKM3 and Bifidobacterium lactis GKK2 Protect against Protein Glycation and Inhibit Glycated Protein Ligation |
title_sort | fermented supernatants of lactobacillus plantarum gkm3 and bifidobacterium lactis gkk2 protect against protein glycation and inhibit glycated protein ligation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9864088/ https://www.ncbi.nlm.nih.gov/pubmed/36678147 http://dx.doi.org/10.3390/nu15020277 |
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