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J. Biol. Chem., Vol. 276, Issue 11, 8445-8452, March 16, 2001
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From the Pulmonary-Critical Care Medicine Branch, NHLBI, National
Institutes of Health, Bethesda, Maryland 20892-1434
Inducible nitric-oxide synthase (iNOS) is
an important signaling protein involved in the regulation of biological
processes (e.g. vasodilation, inflammation) and is subject
to transcriptional regulation by cytokines and lipopolysaccharide
(LPS). Full activation of the human iNOS (hiNOS) promoter by cytokines
(i.e., tumor necrosis factor-
Mitogen-activated Protein Kinases Mediate Activator
Protein-1-dependent Human Inducible Nitric-oxide
Synthase Promoter Activation*
,
, interleukin-1
,
interferon-
(IFN-)) required downstream and upstream nuclear
factor-
B (
115, 8283) and activator protein-1 (AP-1) (5115,
5301) transcription factor binding sites. Human lung epithelial
(A549) cells were transiently transfected with luciferase reporter
plasmids containing an 8.3-kilobase human iNOS promoter to
examine the molecular signaling events necessary for hiNOS
transcriptional activation. The combination of LPS and IFN-, but
neither alone, increased hiNOS promoter activity 28-fold, in a reaction
requiring two critical AP-1 (JunD·Fra-2) promoter binding
sites. Mitogen-activated protein kinases (MAPKs) were assessed as
potential activators of AP-1 and the hiNOS promoter. Both
pharmacological and molecular inhibitors of the extracellular signal-related kinase (ERK) and p38 pathways reduced cytokine mixture
(CM)- and LPS/IFN--induced promoter activation. By gel retardation
analysis, the addition of MAP/ERK kinase-1 and p38 inhibitors
significantly diminished AP-1 binding in both CM- and LPS/IFN--stimulated cells. Thus, p38- and ERK-dependent
pathways, through effects on the AP-1 complex, activate the hiNOS
promoter in cells stimulated with CM or LPS/IFN-.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Bldg. 10, Rm. 5N307,
MSC 1434, National Institutes of Health, 9000 Rockville Pike, Bethesda,
MD 20892-1434. Tel.: 301-496-6980; Fax: 301-402-1610; E-mail:
kristofa@nih.gov.
§
Present address: Metabolism Branch, Bldg. 10, Rm. 4B47, NCI,
National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20892.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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