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Am J Physiol Lung Cell Mol Physiol 279: L806-L814, 2000;
1040-0605/00 $5.00
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Vol. 279, Issue 5, L806-L814, November 2000

Characterization of rabbit SP-B promoter region responsive to downregulation by tumor necrosis factor-alpha

Kiflu Berhane, Ramgopal K. Margana, and Vijayakumar Boggaram

Department of Molecular Biology, University of Texas Health Science Center at Tyler, Tyler, Texas 75708-3154

Surfactant protein B (SP-B) is essential for the maintenance of biophysical properties and physiological function of pulmonary surfactant. Tumor necrosis factor-alpha (TNF-alpha ), an important mediator of lung inflammation, inhibits surfactant phospholipid and surfactant protein synthesis in the lung. In the present study, we investigated the TNF-alpha inhibition of rabbit SP-B promoter activity in a human lung adenocarcinoma cell line (NCI-H441). Deletion experiments indicated that the TNF-alpha response elements are located within -236 bp of SP-B 5'-flanking DNA. The TNF-alpha response region contained binding sites for nuclear factor-kappa B (NF-kappa B), Sp1/Sp3, thyroid transcription factor (TTF)-1, and hepatocyte nuclear factor (HNF)-3 transcription factors. Inhibitors of NF-kappa B activation such as dexamethasone and N-tosyl-L-phenylalanine chloromethyl ketone and mutation of the NF-kappa B element did not reverse TNF-alpha inhibition of SP-B promoter, indicating that TNF-alpha inhibition of SP-B promoter activity occurs independently of NF-kappa B activation. TNF-alpha treatment decreased the binding activities of TTF-1 and HNF-3 elements without altering the nuclear levels of TTF-1 and HNF-3alpha proteins. Pretreatment of cells with okadaic acid reversed TNF-alpha inhibition of SP-B promoter activity. Taken together these data indicated that in NCI-H441 cells 1) TNF-alpha inhibition of SP-B promoter activity may be caused by decreased binding activities of TTF-1 and HNF-3 elements, 2) the decreased binding activities of TTF-1 and HNF-3alpha are not due to decreased nuclear levels of the proteins, and 3) okadaic acid-sensitive phosphatases may be involved in mediating TNF-alpha inhibition of SP-B promoter activity.

lung; respiratory distress syndrome; gene regulation; cytokines


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