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Articles in PresS, published online ahead of print November 27, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00195.2002
Submitted on June 19, 2002
Accepted on November 25, 2002
1 Department of Pediatrics, University of Alabama at Birmingham, Birmingham, AL, USA
2 Department of Pediatrics, University of Kentucky Medical Center, Lexington, KY, USA
3 Department of Pediatrics, University for Arkansas for Medical Sciences, Little Rock, AR, USA; Department of Pediatrics, Arkansas Children's Hospital Research Institute, Little Rock, AR, USA
* To whom correspondence should be addressed. E-mail: MWinkler{at}peds.uab.edu.
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 (ETAs) from children (<19 years) without lung disease for the presence of MMP activity. Only gelatinase activity was detectable and inhibitor profiles suggested 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 showed: 1) gelatinase activity was ~5-6 fold 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.
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