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and
phorbol ester independent of NF-
B
Departments of Pediatrics and Environmental Medicine, Strong Children's Research Center, University of Rochester Medical Center, Rochester, New York 14642
Acute lung
inflammation is complicated by altered pulmonary surfactant
phospholipid and protein composition. The proinflammatory cytokine
tumor necrosis factor-
(TNF-) and the phorbol ester 12-O-tetradecanoyl phorbol-13-acetate
(TPA) inhibit expression of surfactant-associated proteins A and B
(SP-A and SP-B), both important for normal surfactant function. The
transcription factor nuclear factor-
B (NF-B) frequently mediates
regulation of gene expression by TPA and TNF-. In the present study,
electrophoretic mobility shift assays (EMSAs) and pyrrolidine
dithiocarbamate (PDTC), an inhibitor of NF-B activation, were
utilized to determine the role of NF-B activation in TPA and TNF-
inhibition of the surfactant proteins in NCI-H441 cells. Pentoxifylline
(PTX), which inhibits TNF- cellular effects without preventing
NF-B activation, was also tested. By EMSA, TPA and TNF- increased
nuclear NF-B binding activity in temporally distinct patterns. PDTC
decreased TPA- and TNF--induced NF-B binding activity but did not
limit their inhibition of SP-A and SP-B mRNAs. PDTC independently
decreased both SP-A and SP-B mRNAs. PTX partially reversed TNF-- but
not TPA-mediated inhibition of SP-A and SP-B mRNAs without altering NF-B binding. The effects of PDTC and PTX on NF-B and the
surfactant proteins suggest that NF-B activation does not mediate
TPA or TNF- inhibition of SP-A and SP-B mRNA accumulation.
tumor necrosis factor-; nuclear factor-B; pyrrolidine
dithiocarbamate; pentoxifylline; dexamethasone; adenocarcinoma
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