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Matrilysin in Epithelial Repair and Defense*

William C. Parks, PhD; Yolanda S. López-Boado, PhD; Carole L. Wilson, PhD
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*From the Division of Allergy and Pulmonary Medicine, Department of Pediatrics, Washington University School of Medicine, St. Louis, MO.

Correspondence to: William C. Parks, PhD, Department of Pediatrics, Box 8208, Washington University School of Medicine, 660 S. Euclid Ave, St. Louis, MO 63110; e-mail: parks_w@kids.wustl.edu



Chest. 2001;120(1_suppl):S36-S41. doi:10.1378/chest.120.1_suppl.S36
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Repair involves an orderly progression of events to reestablish the integrity of the injured tissue. During each stage in this process, secreted proteinases are needed to remodel extracellular matrix, facilitate cell migration, and process latent proteins, among other functions. In lung epithelium, several of these processes are mediated by matrilysin, a matrix metalloproteinase (MMP). Unlike most MMPs, matrilysin is produced by intact, noninjured airway and peribronchial epithelial cells. In other intact epithelial tissues, namely the small intestine, matrilysin functions in host defense by activating the latent form of defensins, a family of antimicrobial peptides. This metalloproteinase may serve a similar function in the lung. Furthermore, in models of airway injury, matrilysin expression is upregulated in migrating epithelial cells, and the activity of this proteinase is required for repair of airway wounds. These observations indicate that matrilysin serves key functions in both epithelial defense and repair.

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