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Am J Physiol Lung Cell Mol Physiol 283: L418-L427, 2002; doi:10.1152/ajplung.00470.2001
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Vol. 283, Issue 2, L418-L427, August 2002

TNF-alpha inhibits SP-A gene expression in lung epithelial cells via p38 MAPK

Olga L. Miakotina and Jeanne M. Snyder

Department of Anatomy and Cell Biology, College of Medicine, University of Iowa, Iowa City, Iowa 52242-1109

Surfactant protein A (SP-A), the major lung surfactant-associated protein, mediates local defense against pathogens and modulates inflammation in the alveolus. Tumor necrosis factor (TNF)-alpha , a proinflammatory cytokine, inhibits SP-A gene expression in lung epithelial cells. Inhibitors of the phosphatidylinositol 3-kinase pathway, i.e., wortmannin, LY-294002, and rapamycin, did not block the inhibitory effects of TNF-alpha on SP-A mRNA levels. An inhibitor of the p44/42 mitogen-activated protein kinase (MAPK) pathway, PD-98059, was also ineffective. PD-169316 and SB-203580, inhibitors of p38 MAPK, blocked the TNF-alpha -mediated inhibition of SP-A mRNA levels. TNF-alpha increased the phosphorylation of p38 MAPK within 15 min. Anisomycin, an activator of p38 MAPK, increased p38 MAPK phosphorylation and decreased SP-A mRNA levels in a dose-dependent manner. Finally, TNF-alpha increased the phosphorylation of ATF-2, a transcription factor that is a p38 MAPK substrate. We conclude that TNF-alpha downregulates SP-A gene expression in lung epithelial cells via the p38 MAPK signal transduction pathway.

tumor necrosis factor-alpha ; surfactant protein A; H441 cells; p38 mitogen-activated protein kinase


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