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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20 March 2000
Article|
March 20 2000
Bacterial Exposure Induces and Activates Matrilysin in Mucosal Epithelial Cells
Yolanda S. López-Boado,
Yolanda S. López-Boado
aDepartment of Pediatrics, Allergy and Pulmonary Division,
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Carole L. Wilson,
Carole L. Wilson
aDepartment of Pediatrics, Allergy and Pulmonary Division,
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Lora V. Hooper,
Lora V. Hooper
cDepartment of Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110
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Jeffrey I. Gordon,
Jeffrey I. Gordon
cDepartment of Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110
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Scott J. Hultgren,
Scott J. Hultgren
dDepartment of Molecular Microbiology and Microbial Pathogenesis, Washington University School of Medicine, St. Louis, Missouri 63110
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William C. Parks
William C. Parks
aDepartment of Pediatrics, Allergy and Pulmonary Division,
bDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110
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Yolanda S. López-Boado
aDepartment of Pediatrics, Allergy and Pulmonary Division,
Carole L. Wilson
aDepartment of Pediatrics, Allergy and Pulmonary Division,
Lora V. Hooper
cDepartment of Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110
Jeffrey I. Gordon
cDepartment of Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110
Scott J. Hultgren
dDepartment of Molecular Microbiology and Microbial Pathogenesis, Washington University School of Medicine, St. Louis, Missouri 63110
William C. Parks
aDepartment of Pediatrics, Allergy and Pulmonary Division,
bDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110
Abbreviations used in this paper: LPS, lipopolysaccharide; MMP, matrix metalloproteinase.
Received:
August 24 1999
Revision Requested:
February 08 2000
Accepted:
February 15 2000
Online ISSN: 1540-8140
Print ISSN: 0021-9525
© 2000 The Rockefeller University Press
2000
The Rockefeller University Press
J Cell Biol (2000) 148 (6): 1305–1315.
Article history
Received:
August 24 1999
Revision Requested:
February 08 2000
Accepted:
February 15 2000
Citation
Yolanda S. López-Boado, Carole L. Wilson, Lora V. Hooper, Jeffrey I. Gordon, Scott J. Hultgren, William C. Parks; Bacterial Exposure Induces and Activates Matrilysin in Mucosal Epithelial Cells. J Cell Biol 20 March 2000; 148 (6): 1305–1315. doi: https://doi.org/10.1083/jcb.148.6.1305
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