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B
in NF-B Activation by an Oxidative Stress1
*
Laboratory of Virology, Institute of Pathology, University of Liege, Liege, Belgium;
Oncogenesis, Differentiation, and Signal Transduction Laboratory, Institut de Recherche sur le Cancer-Centre Nationale de la Recherche Scientifique, Villejuif, France;
Institut National de la Santé et de la Recherche Médicale, Unit 99, Hôpital Henri Mondor, Creteil, France; and
§
Unit of Infectious Diseases, AZ Sint-Jan, Brugge, Belgium
Activation of transcription factor NF-
B involves the
signal-dependent degradation of basally phosphorylated inhibitors such
as IB
. In response to proinflammatory cytokines or mitogens, the
transduction machinery has recently been characterized, but the
activation mechanism upon oxidative stress remains unknown. In the
present work, we provide several lines of evidence that NF-B
activation in a T lymphocytic cell line (EL4) by hydrogen peroxide
(H2O2) did not involve phosphorylation of the
serine residues 32 and 36 in the amino-terminal part of IB.
Indeed, mutation of Ser32 and Ser36 blocked
IL-1ß- or PMA-induced NF-B activation, but had no effect on its
activation by H2O2. Although IB was
phosphorylated upon exposure to H2O2, tyrosine
residue 42 and the C-terminal PEST (proline-glutamic
acid-serine-threonine) domain played an important role. Indeed,
mutation of tyrosine 42 or serine/threonine residues of the PEST domain
abolished NF-B activation by H2O2, while it
had no effect on activation by IL-1ß or PMA-ionomycin. This
H2O2-inducible phosphorylation was not
dependent on IB kinase activation, but could involve casein kinase
II, because an inhibitor of this enzyme
(5,6-dichloro-1-ß-D-ribofuranosyl-benzimidazole) blocks
NF-B activation. H2O2-induced IB
phosphorylation was followed by its degradation by calpain proteases or
through the proteasome. Taken together, our findings suggest that
NF-B activation by H2O2 involves a new
mechanism that is totally distinct from those triggered by
proinflammatory cytokines or mitogens.
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