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(Received for publication, May 13, 1996, and in revised form, September 18, 1996)
From the SmithKline Beecham Pharmaceuticals, SmithKline Beecham
Pharmaceuticals, Immunopharmacology, UW2532, King of Prussia,
Pennsylvania 19406 and the Interleukin 1
Volume 271, Number 49,
Issue of December 6, 1996
pp. 31496-31501
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
B Proteins Alters
Interleukin-1
-induced Human Rheumatoid Synovial Fibroblast
Prostaglandin E2 Formation
and
Philadelphia College of
Osteopathic Medicine, Philadelphia, Pennsylvania 19131
(IL-1) up-regulates human
rheumatoid synovial fibroblast (RSF) 85-kDa phospholipase
A2 (PLA2) and mitogen-inducible cyclooxygenase
(COX) II. Promoter regions for these genes contain a motif that closely
resembles the "classic" NF
B consensus site. Immunoblot analysis
identified NFB1 (p50), RelA (p65), and c-Rel in RSF. Upon
IL-1-stimulation, p65 and c-Rel but not p50 protein levels were
reduced suggesting nuclear translocation. IL-1-induced RSF nuclear
extracts contained a p65-containing complex, which bound to the
classical NFB consensus motif. An NFB classical oligonucleotide
decoy produced a concentration-dependent decrease in
IL-1-stimulated PGE2 production (IC50 = ~2
µM), indicating a role of NFB. Utilization of
antisense technology showed that p65 but not p50 or c-Rel mediated
IL-1-stimulated PGE2 formation. Treated RSF could not
transcribe COX II or 85-kDa PLA2 mRNA, which reduced
their respective proteins. Interestingly, stimulated IL-8 production
was not inhibited by the classical NFB decoy but was reduced by
treatment with antisense to both p65 and c-Rel supporting preferential
binding of c-Rel-p65 to the "alternative" IL-8 B motif. Taken
together, these data provide the first direct evidence for a role of
p65 in COX II and 85-kDa PLA2 gene induction and support
the IL-1 activation and participation of distinct NFB protein dimers
in RSF prostanoid and IL-8 formation.
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