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inhibits SP-A gene expression in lung epithelial
cells via p38 MAPK
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)-
, 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- 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--mediated
inhibition of SP-A mRNA levels. TNF- 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- increased the phosphorylation
of ATF-2, a transcription factor that is a p38 MAPK substrate. We
conclude that TNF- downregulates SP-A gene expression in lung
epithelial cells via the p38 MAPK signal transduction pathway.
tumor necrosis factor-; surfactant protein A; H441 cells; p38
mitogen-activated protein kinase
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