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Am J Physiol Lung Cell Mol Physiol 284: L557-L565, 2003. First published November 27, 2002; doi:10.1152/ajplung.00195.2002
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Vol. 284, Issue 4, L557-L565, April 2003

TRANSLATIONAL PHYSIOLOGY
Implications for matrix metalloproteinases as modulators of pediatric lung disease

Margaret K. Winkler1, Jane K. Foldes2, Robert C. Bunn3, and John L. Fowlkes3

1 Department of Pediatrics, University of Alabama at Birmingham, Birmingham, Alabama 35233; 2 Department of Pediatrics, University of Kentucky College of Medicine, Lexington, Kentucky 40536; and 3 Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72202

Matrix metalloproteinases (MMPs) are a large family (>20) of cation-dependent proteinases believed to be important modulators of normal human lung development and potentially harmful mediators of lung damage. Little is known about MMP production and secretion by the lung during childhood or how alterations in MMP levels may be involved in lung damage. We examined endotracheal aspirates from children (<19 years) without lung disease for the presence of MMP activity. Only gelatinase activity was detectable, and inhibitor profiles suggest they represented one or more MMPs. Comparison of gelatinase activity, MMP expression, and MMP activity in children without pulmonary disease with children who required mechanical ventilation for respiratory failure show: 1) gelatinase activity was approximately five- to sixfold higher in respiratory failure; 2) MMP-7, MMP-8, and MMP-9 concentrations and MMP-8 and MMP-9 activities were markedly elevated in respiratory failure; and 3) MMP-7, MMP-8, and MMP-9 levels were significantly correlated in children with lung disease. These studies provide compelling evidence that specific MMPs are present in the diseased lung and may participate in the pathogenesis of pediatric respiratory failure.

extracellular matrix; bronchoalveolar lavage


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