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Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet
BACKGROUND: Previous studies suggested that dietary tannin ingestion may induce changes in mouse salivary proteins in addition to the primarily studied proline-rich proteins (PRPs). The aim of the present study was to determine the protein expression changes induced by condensed tannin intake on the...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3018447/ https://www.ncbi.nlm.nih.gov/pubmed/21159160 http://dx.doi.org/10.1186/1477-5956-8-65 |
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author | Lamy, Elsa Graça, Gonçalo da Costa, Gonçalo Franco, Catarina e Silva, Fernando Capela Baptista, Elvira Sales Coelho, Ana Varela |
author_facet | Lamy, Elsa Graça, Gonçalo da Costa, Gonçalo Franco, Catarina e Silva, Fernando Capela Baptista, Elvira Sales Coelho, Ana Varela |
author_sort | Lamy, Elsa |
collection | PubMed |
description | BACKGROUND: Previous studies suggested that dietary tannin ingestion may induce changes in mouse salivary proteins in addition to the primarily studied proline-rich proteins (PRPs). The aim of the present study was to determine the protein expression changes induced by condensed tannin intake on the fraction of mouse whole salivary proteins that are unable to form insoluble tannin-protein complexes. Two-dimensional polyacrylamide gel electrophoresis protein separation was used, followed by protein identification by mass spectrometry. RESULTS: Fifty-seven protein spots were excised from control group gels, and 21 different proteins were identified. With tannin consumption, the expression levels of one α-amylase isoform and one unidentified protein increased, whereas acidic mammalian chitinase and Muc10 decreased. Additionally, two basic spots that stained pink with Coomassie Brilliant Blue R-250 were newly observed, suggesting that some induced PRPs may remain uncomplexed or form soluble complexes with tannins. CONCLUSION: This proteomic analysis provides evidence that other salivary proteins, in addition to tannin-precipitating proteins, are affected by tannin ingestion. Changes in the expression levels of the acidic mammalian chitinase precursor and in one of the 14 salivary α-amylase isoforms underscores the need to further investigate their role in tannin ingestion. |
format | Text |
id | pubmed-3018447 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-30184472011-01-11 Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet Lamy, Elsa Graça, Gonçalo da Costa, Gonçalo Franco, Catarina e Silva, Fernando Capela Baptista, Elvira Sales Coelho, Ana Varela Proteome Sci Research BACKGROUND: Previous studies suggested that dietary tannin ingestion may induce changes in mouse salivary proteins in addition to the primarily studied proline-rich proteins (PRPs). The aim of the present study was to determine the protein expression changes induced by condensed tannin intake on the fraction of mouse whole salivary proteins that are unable to form insoluble tannin-protein complexes. Two-dimensional polyacrylamide gel electrophoresis protein separation was used, followed by protein identification by mass spectrometry. RESULTS: Fifty-seven protein spots were excised from control group gels, and 21 different proteins were identified. With tannin consumption, the expression levels of one α-amylase isoform and one unidentified protein increased, whereas acidic mammalian chitinase and Muc10 decreased. Additionally, two basic spots that stained pink with Coomassie Brilliant Blue R-250 were newly observed, suggesting that some induced PRPs may remain uncomplexed or form soluble complexes with tannins. CONCLUSION: This proteomic analysis provides evidence that other salivary proteins, in addition to tannin-precipitating proteins, are affected by tannin ingestion. Changes in the expression levels of the acidic mammalian chitinase precursor and in one of the 14 salivary α-amylase isoforms underscores the need to further investigate their role in tannin ingestion. BioMed Central 2010-12-15 /pmc/articles/PMC3018447/ /pubmed/21159160 http://dx.doi.org/10.1186/1477-5956-8-65 Text en Copyright ©2010 Lamy et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (<url>http://creativecommons.org/licenses/by/2.0</url>), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Lamy, Elsa Graça, Gonçalo da Costa, Gonçalo Franco, Catarina e Silva, Fernando Capela Baptista, Elvira Sales Coelho, Ana Varela Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet |
title | Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet |
title_full | Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet |
title_fullStr | Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet |
title_full_unstemmed | Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet |
title_short | Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet |
title_sort | changes in mouse whole saliva soluble proteome induced by tannin-enriched diet |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3018447/ https://www.ncbi.nlm.nih.gov/pubmed/21159160 http://dx.doi.org/10.1186/1477-5956-8-65 |
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