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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...

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Autores principales: López-Boado, Yolanda S., Wilson, Carole L., Hooper, Lora V., Gordon, Jeffrey I., Hultgren, Scott J., Parks, William C.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2000
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.
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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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