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Bacterial Exposure Induces and Activates Matrilysin in Mucosal Epithelial Cells
Matrilysin, a matrix metalloproteinase, is expressed and secreted lumenally by intact mucosal and glandular epithelia throughout the body, suggesting that its regulation and function are shared among tissues. Because matrilysin is produced in Paneth cells of the murine small intestine, where it part...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2000
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174301/ https://www.ncbi.nlm.nih.gov/pubmed/10725342 |
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author | López-Boado, Yolanda S. Wilson, Carole L. Hooper, Lora V. Gordon, Jeffrey I. Hultgren, Scott J. Parks, William C. |
author_facet | López-Boado, Yolanda S. Wilson, Carole L. Hooper, Lora V. Gordon, Jeffrey I. Hultgren, Scott J. Parks, William C. |
author_sort | López-Boado, Yolanda S. |
collection | PubMed |
description | Matrilysin, a matrix metalloproteinase, is expressed and secreted lumenally by intact mucosal and glandular epithelia throughout the body, suggesting that its regulation and function are shared among tissues. Because matrilysin is produced in Paneth cells of the murine small intestine, where it participates in innate host defense by activation of prodefensins, we speculated that its expression would be influenced by bacterial exposure. Indeed, acute infection (10–90 min) of human colon, bladder, and lung carcinoma cells, primary human tracheal epithelial cells, and human tracheal explants with type 1–piliated Escherichia coli mediated a marked (25–50-fold) and sustained (>24 h) induction of matrilysin production. In addition, bacterial infection resulted in activation of the zymogen form of the enzyme, which was selectively released at the apical surface. Induction of matrilysin was mediated by a soluble, non-LPS bacterial factor and correlated with the release of defensin-like bacteriocidal activity. Bacteria did not induce matrilysin in other cell types, and expression of other metalloproteinases by epithelial cells was not affected by bacteria. Matrilysin was not detected in germ-free mice, but the enzyme was induced after colonization with Bacteroides thetaiotaomicron. These findings indicate that bacterial exposure is a potent and physiologically relevant signal regulating matrilysin expression in epithelial cells. |
format | Text |
id | pubmed-2174301 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2000 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21743012008-05-01 Bacterial Exposure Induces and Activates Matrilysin in Mucosal Epithelial Cells López-Boado, Yolanda S. Wilson, Carole L. Hooper, Lora V. Gordon, Jeffrey I. Hultgren, Scott J. Parks, William C. J Cell Biol Original Article Matrilysin, a matrix metalloproteinase, is expressed and secreted lumenally by intact mucosal and glandular epithelia throughout the body, suggesting that its regulation and function are shared among tissues. Because matrilysin is produced in Paneth cells of the murine small intestine, where it participates in innate host defense by activation of prodefensins, we speculated that its expression would be influenced by bacterial exposure. Indeed, acute infection (10–90 min) of human colon, bladder, and lung carcinoma cells, primary human tracheal epithelial cells, and human tracheal explants with type 1–piliated Escherichia coli mediated a marked (25–50-fold) and sustained (>24 h) induction of matrilysin production. In addition, bacterial infection resulted in activation of the zymogen form of the enzyme, which was selectively released at the apical surface. Induction of matrilysin was mediated by a soluble, non-LPS bacterial factor and correlated with the release of defensin-like bacteriocidal activity. Bacteria did not induce matrilysin in other cell types, and expression of other metalloproteinases by epithelial cells was not affected by bacteria. Matrilysin was not detected in germ-free mice, but the enzyme was induced after colonization with Bacteroides thetaiotaomicron. These findings indicate that bacterial exposure is a potent and physiologically relevant signal regulating matrilysin expression in epithelial cells. The Rockefeller University Press 2000-03-20 /pmc/articles/PMC2174301/ /pubmed/10725342 Text en © 2000 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Original Article López-Boado, Yolanda S. Wilson, Carole L. Hooper, Lora V. Gordon, Jeffrey I. Hultgren, Scott J. Parks, William C. Bacterial Exposure Induces and Activates Matrilysin in Mucosal Epithelial Cells |
title | Bacterial Exposure Induces and Activates Matrilysin in Mucosal Epithelial Cells |
title_full | Bacterial Exposure Induces and Activates Matrilysin in Mucosal Epithelial Cells |
title_fullStr | Bacterial Exposure Induces and Activates Matrilysin in Mucosal Epithelial Cells |
title_full_unstemmed | Bacterial Exposure Induces and Activates Matrilysin in Mucosal Epithelial Cells |
title_short | Bacterial Exposure Induces and Activates Matrilysin in Mucosal Epithelial Cells |
title_sort | bacterial exposure induces and activates matrilysin in mucosal epithelial cells |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174301/ https://www.ncbi.nlm.nih.gov/pubmed/10725342 |
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