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In Vitro Inhibitory Activity of Acca sellowiana Fruit Extract on End Products of Advanced Glycation

INTRODUCTION: Hyperglycemia plays an important role in the pathogenesis of diabetic complications, as it increases protein glycation, as well as the progressive accumulation of advanced glycation end products (AGEs), which are complex structures that produce fluorescence. The glycation reaction rais...

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Autores principales: Muñiz, Alethia, Garcia, Abraham H., Pérez, Rosa M., García, Efren V., González, Daphne E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Healthcare 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5801221/
https://www.ncbi.nlm.nih.gov/pubmed/29168124
http://dx.doi.org/10.1007/s13300-017-0335-7
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author Muñiz, Alethia
Garcia, Abraham H.
Pérez, Rosa M.
García, Efren V.
González, Daphne E.
author_facet Muñiz, Alethia
Garcia, Abraham H.
Pérez, Rosa M.
García, Efren V.
González, Daphne E.
author_sort Muñiz, Alethia
collection PubMed
description INTRODUCTION: Hyperglycemia plays an important role in the pathogenesis of diabetic complications, as it increases protein glycation, as well as the progressive accumulation of advanced glycation end products (AGEs), which are complex structures that produce fluorescence. The glycation reaction raises the levels of protein carbonyl, N (ε)-(carboxymethyl)lysine (CML), and fructosamine and decreases the level of thiol groups. METHODS: In the present study, the antiglycation activity was determined by fluorescence intensity using the bovine serum albumin (BSA)/glucose, CML method, and the level of fructosamine. The oxidation of proteins was determined by the carbonyl protein content and thiol groups. RESULTS: The results show that the hexane extract of Acca sellowiana (FOH) at different concentrations (0.30–5 mg/ml) significantly inhibited the formation of AGEs in the BSA/glucose model during the 4 weeks of the study. FOH reduced the levels of fructosamine and CML. Our results showed a significant effect of FOH in the prevention of oxidative damage of proteins, as well as an effect on the oxidation of thiol groups and carbonyl proteins. CONCLUSION: The present study indicates that FOH is effective in inhibiting the glycation of proteins in vitro, so it can prevent or ameliorate the chronic conditions of diabetes associated with the formation of AGEs.
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spelling pubmed-58012212018-02-12 In Vitro Inhibitory Activity of Acca sellowiana Fruit Extract on End Products of Advanced Glycation Muñiz, Alethia Garcia, Abraham H. Pérez, Rosa M. García, Efren V. González, Daphne E. Diabetes Ther Original Research INTRODUCTION: Hyperglycemia plays an important role in the pathogenesis of diabetic complications, as it increases protein glycation, as well as the progressive accumulation of advanced glycation end products (AGEs), which are complex structures that produce fluorescence. The glycation reaction raises the levels of protein carbonyl, N (ε)-(carboxymethyl)lysine (CML), and fructosamine and decreases the level of thiol groups. METHODS: In the present study, the antiglycation activity was determined by fluorescence intensity using the bovine serum albumin (BSA)/glucose, CML method, and the level of fructosamine. The oxidation of proteins was determined by the carbonyl protein content and thiol groups. RESULTS: The results show that the hexane extract of Acca sellowiana (FOH) at different concentrations (0.30–5 mg/ml) significantly inhibited the formation of AGEs in the BSA/glucose model during the 4 weeks of the study. FOH reduced the levels of fructosamine and CML. Our results showed a significant effect of FOH in the prevention of oxidative damage of proteins, as well as an effect on the oxidation of thiol groups and carbonyl proteins. CONCLUSION: The present study indicates that FOH is effective in inhibiting the glycation of proteins in vitro, so it can prevent or ameliorate the chronic conditions of diabetes associated with the formation of AGEs. Springer Healthcare 2017-11-22 2018-02 /pmc/articles/PMC5801221/ /pubmed/29168124 http://dx.doi.org/10.1007/s13300-017-0335-7 Text en © The Author(s) 2017 https://creativecommons.org/licenses/by-nc/4.0/This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International License (http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) ), which permits any noncommercial use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Original Research
Muñiz, Alethia
Garcia, Abraham H.
Pérez, Rosa M.
García, Efren V.
González, Daphne E.
In Vitro Inhibitory Activity of Acca sellowiana Fruit Extract on End Products of Advanced Glycation
title In Vitro Inhibitory Activity of Acca sellowiana Fruit Extract on End Products of Advanced Glycation
title_full In Vitro Inhibitory Activity of Acca sellowiana Fruit Extract on End Products of Advanced Glycation
title_fullStr In Vitro Inhibitory Activity of Acca sellowiana Fruit Extract on End Products of Advanced Glycation
title_full_unstemmed In Vitro Inhibitory Activity of Acca sellowiana Fruit Extract on End Products of Advanced Glycation
title_short In Vitro Inhibitory Activity of Acca sellowiana Fruit Extract on End Products of Advanced Glycation
title_sort in vitro inhibitory activity of acca sellowiana fruit extract on end products of advanced glycation
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5801221/
https://www.ncbi.nlm.nih.gov/pubmed/29168124
http://dx.doi.org/10.1007/s13300-017-0335-7
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