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1 stimulates HO-1 via the p38
mitogen-activated protein kinase in A549 pulmonary epithelial
cells
1 Pulmonary, Allergy and Critical Care Medicine and 4 Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213; 2 Division of Pulmonary Medicine, Johns Hopkins University, Baltimore, Maryland 21205; and 3 Section of Nephrology, Yale University School of Medicine, New Haven, Connecticut 06250
In lung
injury and progressive lung diseases, the multifunctional cytokine
transforming growth factor-
1 (TGF-1)
modulates inflammatory responses and wound repair. Heme oxygenase-1
(HO-1) is a stress-inducible protein that has been demonstrated to
confer cytoprotection against oxidative injury and provide a vital
function in maintaining tissue homeostasis. Here we report that
TGF-1 is a potent inducer of HO-1 and examined the
signaling pathway by which TGF-1 regulates HO-1
expression in human lung epithelial cells (A549). TGF-1
(1-5 ng/ml) treatment resulted in a marked time-dependent
induction of HO-1 mRNA in A549 cells, followed by corresponding
increases in HO-1 protein and HO enzymatic activity. Actinomycin D and
cycloheximide inhibited TGF-1-responsive HO-1 mRNA
expression, indicating a requirement for transcription and de novo
protein synthesis. Furthermore, TGF-1 rapidly activated the p38 mitogen-activated protein kinase (p38 MAPK) pathway in A549
cells. A chemical inhibitor of p38 MAPK (SB-203580) abolished TGF-1-inducible HO-1 mRNA expression. Both SB-203580 and
expression of a dominant-negative mutant of p38 MAPK inhibited
TGF-1-induced ho-1 gene activation, as
assayed by luciferase activity of an ho-1
enhancer/luciferase fusion construct (pMHO1luc-33+SX2). These studies
demonstrate the critical intermediacy of the p38 MAPK pathway in the
regulation of HO-1 expression by TGF-1.
heme oxygenase; inflammation; mitogen-activated protein kinase; oxidant stress; transforming growth factor-1
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