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Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme

Glycation process refers to reactions between reduction sugars and amino acids that can lead to formation of advanced glycation end products (AGEs) which are related to changes in chemical and functional properties of biological structures that accumulate during aging and diseases. The aim of this s...

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Autores principales: Muraoka, Mariane Yumiko, Justino, Allisson Benatti, Caixeta, Douglas Carvalho, Queiroz, Julia Silveira, Sabino-Silva, Robinson, Salmen Espindola, Foued
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8782344/
https://www.ncbi.nlm.nih.gov/pubmed/35061788
http://dx.doi.org/10.1371/journal.pone.0262369
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author Muraoka, Mariane Yumiko
Justino, Allisson Benatti
Caixeta, Douglas Carvalho
Queiroz, Julia Silveira
Sabino-Silva, Robinson
Salmen Espindola, Foued
author_facet Muraoka, Mariane Yumiko
Justino, Allisson Benatti
Caixeta, Douglas Carvalho
Queiroz, Julia Silveira
Sabino-Silva, Robinson
Salmen Espindola, Foued
author_sort Muraoka, Mariane Yumiko
collection PubMed
description Glycation process refers to reactions between reduction sugars and amino acids that can lead to formation of advanced glycation end products (AGEs) which are related to changes in chemical and functional properties of biological structures that accumulate during aging and diseases. The aim of this study was to perform and analyze in vitro glycation by fructose and methylglyoxal (MGO) using salivary fluid, albumin, lysozyme, and salivary α-amylase (sAA). Glycation effect was analyzed by biochemical and spectroscopic methods. The results were obtained by fluorescence analysis, infrared spectroscopy (total attenuated reflection—Fourier transform, ATR-FTIR) followed by multivariate analysis of principal components (PCA), protein profile, immunodetection, enzymatic activity and oxidative damage to proteins. Fluorescence increased in all glycated samples, except in saliva with fructose. The ATR-FTIR spectra and PCA analysis showed structural changes related to the vibrational mode of glycation of albumin, lysozyme, and salivary proteins. Glycation increased the relative molecular mass (Mr) in protein profile of albumin and lysozyme. Saliva showed a decrease in band intensity when glycated. The analysis of sAA immunoblotting indicated a relative reduction in intensity of its correspondent Mr after sAA glycation; and a decrease in its enzymatic activity was observed. Carbonylation levels increased in all glycated samples, except for saliva with fructose. Thiol content decreased only for glycated lysozyme and saliva with MGO. Therefore, glycation of salivary fluid and sAA may have the potential to identify products derived by glycation process. This opens perspectives for further studies on the use of saliva, an easy and non-invasive collection fluid, to monitor glycated proteins in the aging process and evolution of diseases.
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spelling pubmed-87823442022-01-22 Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme Muraoka, Mariane Yumiko Justino, Allisson Benatti Caixeta, Douglas Carvalho Queiroz, Julia Silveira Sabino-Silva, Robinson Salmen Espindola, Foued PLoS One Research Article Glycation process refers to reactions between reduction sugars and amino acids that can lead to formation of advanced glycation end products (AGEs) which are related to changes in chemical and functional properties of biological structures that accumulate during aging and diseases. The aim of this study was to perform and analyze in vitro glycation by fructose and methylglyoxal (MGO) using salivary fluid, albumin, lysozyme, and salivary α-amylase (sAA). Glycation effect was analyzed by biochemical and spectroscopic methods. The results were obtained by fluorescence analysis, infrared spectroscopy (total attenuated reflection—Fourier transform, ATR-FTIR) followed by multivariate analysis of principal components (PCA), protein profile, immunodetection, enzymatic activity and oxidative damage to proteins. Fluorescence increased in all glycated samples, except in saliva with fructose. The ATR-FTIR spectra and PCA analysis showed structural changes related to the vibrational mode of glycation of albumin, lysozyme, and salivary proteins. Glycation increased the relative molecular mass (Mr) in protein profile of albumin and lysozyme. Saliva showed a decrease in band intensity when glycated. The analysis of sAA immunoblotting indicated a relative reduction in intensity of its correspondent Mr after sAA glycation; and a decrease in its enzymatic activity was observed. Carbonylation levels increased in all glycated samples, except for saliva with fructose. Thiol content decreased only for glycated lysozyme and saliva with MGO. Therefore, glycation of salivary fluid and sAA may have the potential to identify products derived by glycation process. This opens perspectives for further studies on the use of saliva, an easy and non-invasive collection fluid, to monitor glycated proteins in the aging process and evolution of diseases. Public Library of Science 2022-01-21 /pmc/articles/PMC8782344/ /pubmed/35061788 http://dx.doi.org/10.1371/journal.pone.0262369 Text en © 2022 Muraoka et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Muraoka, Mariane Yumiko
Justino, Allisson Benatti
Caixeta, Douglas Carvalho
Queiroz, Julia Silveira
Sabino-Silva, Robinson
Salmen Espindola, Foued
Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme
title Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme
title_full Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme
title_fullStr Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme
title_full_unstemmed Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme
title_short Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme
title_sort fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8782344/
https://www.ncbi.nlm.nih.gov/pubmed/35061788
http://dx.doi.org/10.1371/journal.pone.0262369
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