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RI-Mediated Induction of TNF-
Gene Expression in the RBL-2H3 Mast Cell Line: Regulation by a Novel NF-
B-Like Nuclear Binding Complex1
*
Unité Immuno-Allergie, Institut Pasteur,
Unité 363, Institut National de la Santé et de la Recherche Médicale, Institut Cochin de Genetique Moleculaire, Hôpital Cochin, Paris, France; and
Section on Chemical Immunology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892
Using rat basophilic leukemia (RBL-2H3) cells as a model, we
investigated how aggregation of the high affinity receptor for IgE
(Fc
RI) regulates TNF-
gene expression. Antigenic stimulation of
RBL-2H3 cells led to an increase in newly synthesized TNF- mRNA that
was dependent on continuous receptor aggregation and did not require de
novo protein synthesis. Kinetic analysis showed that maximal levels
were achieved at 60 min and waned by 180 min of stimulation.
Concomitant with the transcriptional activation of the TNF- gene,
the rapid appearance and disappearance of a previously uncharacterized
nuclear NF-
B DNA binding activity, comprised of two distinct protein
complexes, were observed. These protein complexes bound to NF-B
sites within the TNF- gene and contained novel proteins (three
species of Mr between 90,000–110,000)
distinct from the classical proteins in NF-B complexes. The induced
NF-B binding activity required continuous receptor stimulation and
induced NF-B-dependent reporter gene expression. Consistent with a
role for the novel NF-B nuclear binding activity in TNF- gene
expression, deletion of several 5' B elements in the TNF-
promoter abolished all measurable FcRI-dependent induction of a
reporter construct. Pharmacologic agents that inhibited the NF-B
binding activity also inhibited TNF- mRNA expression. Our results
demonstrate that a novel NF-B-like nuclear binding activity plays an
important role in regulation of the rapid and transient transcriptional
activation of the TNF- gene via FcRI.
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