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Correlation of expression and activity of matrix metalloproteinase-9 and -2 in human gingival cells of periodontitis patients
PURPOSE: Matrix metalloproteinases (MMPs) are capable of degrading extracellular matrix, and they are inducible enzymes depending on an inflammatory environment such as periodontitis and bacterial infection in periodontal tissue. Gingival inflammation has been postulated to be correlated with the pr...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Korean Academy of Periodontology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3596630/ https://www.ncbi.nlm.nih.gov/pubmed/23507779 http://dx.doi.org/10.5051/jpis.2013.43.1.24 |
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author | Kim, Kyung-A Chung, Soo-Bong Hawng, Eun-Young Noh, Seung-Hyun Song, Kwon-Ho Kim, Hanna-Hyun Kim, Cheorl-Ho Park, Young-Guk |
author_facet | Kim, Kyung-A Chung, Soo-Bong Hawng, Eun-Young Noh, Seung-Hyun Song, Kwon-Ho Kim, Hanna-Hyun Kim, Cheorl-Ho Park, Young-Guk |
author_sort | Kim, Kyung-A |
collection | PubMed |
description | PURPOSE: Matrix metalloproteinases (MMPs) are capable of degrading extracellular matrix, and they are inducible enzymes depending on an inflammatory environment such as periodontitis and bacterial infection in periodontal tissue. Gingival inflammation has been postulated to be correlated with the production of MMP-2 and MMP-9. The objective of this study was to quantify the expression and activity of MMP-9 and -2, and to determine the correlation between activity and expression of these MMPs in human gingival tissues with periodontitis. METHODS: The gingival tissues of 13 patients were homogenized in 500 µL of phosphate buffered saline with a protease inhibitor cocktail. The expression and activity of MMP-2 and -9 were measured by enzyme-linked immunosorbent assay and Western blot analysis, and quantified by a densitometer. For the correlation line, statistical analysis was performed using the Systat software package. RESULTS: MMP-9 was highly expressed in all gingival tissue samples, whereas MMP-2 was underexpressed compared with MMP-9. MMP-9 activity increased together with the MMP-9 expression level, with a positive correlation (r=0.793, P=0.01). The correlation was not observed in MMP-2. CONCLUSIONS: The expression of MMP-2 and -9 might contribute to periodontal physiological and pathological processes, and the degree of MMP-9 expression and activity are predictive indicators relevant to the progression of periodontitis. |
format | Online Article Text |
id | pubmed-3596630 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Korean Academy of Periodontology |
record_format | MEDLINE/PubMed |
spelling | pubmed-35966302013-03-18 Correlation of expression and activity of matrix metalloproteinase-9 and -2 in human gingival cells of periodontitis patients Kim, Kyung-A Chung, Soo-Bong Hawng, Eun-Young Noh, Seung-Hyun Song, Kwon-Ho Kim, Hanna-Hyun Kim, Cheorl-Ho Park, Young-Guk J Periodontal Implant Sci Research Article PURPOSE: Matrix metalloproteinases (MMPs) are capable of degrading extracellular matrix, and they are inducible enzymes depending on an inflammatory environment such as periodontitis and bacterial infection in periodontal tissue. Gingival inflammation has been postulated to be correlated with the production of MMP-2 and MMP-9. The objective of this study was to quantify the expression and activity of MMP-9 and -2, and to determine the correlation between activity and expression of these MMPs in human gingival tissues with periodontitis. METHODS: The gingival tissues of 13 patients were homogenized in 500 µL of phosphate buffered saline with a protease inhibitor cocktail. The expression and activity of MMP-2 and -9 were measured by enzyme-linked immunosorbent assay and Western blot analysis, and quantified by a densitometer. For the correlation line, statistical analysis was performed using the Systat software package. RESULTS: MMP-9 was highly expressed in all gingival tissue samples, whereas MMP-2 was underexpressed compared with MMP-9. MMP-9 activity increased together with the MMP-9 expression level, with a positive correlation (r=0.793, P=0.01). The correlation was not observed in MMP-2. CONCLUSIONS: The expression of MMP-2 and -9 might contribute to periodontal physiological and pathological processes, and the degree of MMP-9 expression and activity are predictive indicators relevant to the progression of periodontitis. Korean Academy of Periodontology 2013-02 2013-02-28 /pmc/articles/PMC3596630/ /pubmed/23507779 http://dx.doi.org/10.5051/jpis.2013.43.1.24 Text en Copyright © 2013 Korean Academy of Periodontology http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/). |
spellingShingle | Research Article Kim, Kyung-A Chung, Soo-Bong Hawng, Eun-Young Noh, Seung-Hyun Song, Kwon-Ho Kim, Hanna-Hyun Kim, Cheorl-Ho Park, Young-Guk Correlation of expression and activity of matrix metalloproteinase-9 and -2 in human gingival cells of periodontitis patients |
title | Correlation of expression and activity of matrix metalloproteinase-9 and -2 in human gingival cells of periodontitis patients |
title_full | Correlation of expression and activity of matrix metalloproteinase-9 and -2 in human gingival cells of periodontitis patients |
title_fullStr | Correlation of expression and activity of matrix metalloproteinase-9 and -2 in human gingival cells of periodontitis patients |
title_full_unstemmed | Correlation of expression and activity of matrix metalloproteinase-9 and -2 in human gingival cells of periodontitis patients |
title_short | Correlation of expression and activity of matrix metalloproteinase-9 and -2 in human gingival cells of periodontitis patients |
title_sort | correlation of expression and activity of matrix metalloproteinase-9 and -2 in human gingival cells of periodontitis patients |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3596630/ https://www.ncbi.nlm.nih.gov/pubmed/23507779 http://dx.doi.org/10.5051/jpis.2013.43.1.24 |
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