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Papers In Press, published online ahead of print December 21, 2004
Institute of Pharmacology, Medical School Hannover, Hannover D-30625
Corresponding Author: Kracht.Michael{at}MH-Hannover.de
Binding sites for the dimeric transcription factor activator protein (AP)-1 are found in numerous immunoregulatory and inflammatory genes. The precise mechanisms by which AP-1 activates, or, represses immune response genes and in particular the roles of individual AP-1 subunits in inflammatory response are largely unknown. We report here that c-FOS and FRA-1, two inducible components of AP-1, are recruited to the endogenous Interleukin (IL)-8 promoter in an IL-1-dependent manner. c-FOS activates IL-8 transcription and synergizes in this effect with p65 NF-B. In contrast, FRA-1 strongly inhibits inducible IL-8 transcription. FRA-1 activation involves its stabilization, ubiquitination and interaction with histone deacetylase (HDAC)-1. Blockade of MEK1 by PD98059 suppresses c-FOS and FRA-1 expression and thus affects two counteractive signals for IL-8 mRNA synthesis simultaneously. This disturbs the inducible recruitment of TATA box binding protein (TBP) and RNA polymerase II to the IL-8 promoter. Additional experiments reveal that, in conjunction with p65 NF-B, the MEK1-ERK-dependent synthesis of c-FOS and FRA-1 serves to adjust the overall expression level of IL-8 in response to two of its physiological inducers, IL-1 and EGF. The, relative to c-FOS, delayed recruitment of FRA-1 to the IL-8 promoter provides an example how AP-1 subunits may dampen excessive chemokine synthesis.
J. Biol. Chem, 10.1074/jbc.M407071200
Submitted on June 24, 2004
Revised on December 15, 2004
Accepted on December 21, 2004
MEK1-dependent delayed expression of FRA-1 counteracts c-FOS and p65 NF-kB-mediated interleukin-8 transcription in response to cytokines or growth factors
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