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J Biol Chem, Vol. 274, Issue 8, 4794-4800, February 19, 1999
From Développement, Vieillissement et Pathologie de la
Rétine, U450, INSERM, Paris 75016, France
Bovine retinal pigmented epithelial cells express
an inducible nitric oxide synthase (NOS-2) after activation with
interferon-
(IFN-) and lipopolysaccharide (LPS). Experiments were
performed to investigate the involvement of interferon regulatory
factor-1 (IRF-1) on NOS-2 induction and its regulation by NOS-2
inhibitors such as pyrrolidine dithiocarbamate (PDTC), an antioxidant,
or protein kinase inhibitors. Analysis by transitory transfections showed that LPS, alone or with IFN-, stimulated activity of the murine NOS-2 promoter fragment linked upstream of luciferase and its
suppression by PDTC and by the different protein kinase inhibitors, genistein (tyrosine kinase inhibitor), PD98059 (mitogen-actived protein
(MAP) kinase kinase inhibitor), and SB 203580 (p38 MAP inhibitor).
Using specific antibodies, we have confirmed that extracellular
signal-regulated kinases and p38 MAP kinase were activated by LPS and
IFN- in retinal pigmented epithelial cells. Analysis by reverse
transcriptase-polymerase chain reaction, Western blot, and
electrophoretic mobility shift assay demonstrated that IFN- alone or
combined with LPS induced an accumulation of IRF-1 mRNA and protein
and IRF-1 DNA binding. Transfections assays with the IRF-1 promoter
showed an induction of this promoter with IFN-, potentiated by LPS.
The decrease of LPS/IFN--induced IRF-1 promoter activity, IRF-1
synthesis, and IRF-1 activation, by PDTC, genistein, PD98059, and SB
203580, could explained in part the inhibition of the NOS-2 induction
by these compounds. Our results demonstrate that IRF-1 is necessary for
NOS-2 induction by LPS and IFN- and that its synthesis requires the
involvement of a redox-sensitive step, the activation of tyrosine
kinases, and extracellular signal-regulated kinases 1/2 and p38 MAP kinases.
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