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Am J Physiol Lung Cell Mol Physiol 284: L671-L679, 2003. First published December 20, 2002; doi:10.1152/ajplung.00220.2002
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Vol. 284, Issue 4, L671-L679, April 2003

Neutrophil elastase increases MUC4 expression in normal human bronchial epithelial cells

Bernard M. Fischer1, Jacob G. Cuellar1, Meredith L. Diehl1, Akira M. deFreytas1, Jin Zhang2, Kermit L. Carraway2, and Judith A. Voynow1

1 Division of Pediatric Pulmonary Medicine, Duke University Medical Center, Durham, North Carolina 27710; and 2 Department of Cell Biology and Anatomy, University of Miami School of Medicine, Miami, Florida 33101

In chronic obstructive pulmonary diseases, the airway epithelium is chronically exposed to neutrophil elastase, an inflammatory protease. The cellular response to neutrophil elastase dictates the balance between epithelial injury and repair. Key regulators of epithelial migration and proliferation are the ErbB receptor tyrosine kinases, including the epidermal growth factor receptor. In this context, we investigated whether neutrophil elastase may regulate expression of MUC4, a membrane-tethered mucin that has recently been identified as a ligand for ErbB2, the major heterodimerization partner of the epidermal growth factor receptor. In normal human bronchial epithelial cells, neutrophil elastase increased MUC4 mRNA levels in both a concentration- and time-dependent manner. RNA stability assays revealed that neutrophil elastase increased MUC4 mRNA levels by prolonging the mRNA half-life from 5 to 21 h. Neutrophil elastase also increased MUC4 glycoprotein levels as determined by Western analysis, using a monoclonal antibody specific for a nontandem repeat MUC4 sequence. Therefore, airway epithelial cells respond to neutrophil elastase exposure by increasing expression of MUC4, a potential activator of epithelial repair mechanisms.

protease; mRNA stability; airway epithelium; mucin glycoprotein


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