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Most of the inflammatory and proviral effects of tumor necrosis
factor (TNF) are mediated through the activation of the nuclear
transcription factor NF-
PTPase
inhibitors also blocked NF-
Volume 270,
Number 18,
Issue of May 5, pp. 10631-10639, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
B
B. How TNF activates NF-B, however,
is not well understood. We examined the role of protein phosphatases in
the TNF-dependent activation of NF-B. Treatment of human myeloid
ML-1a cells with TNF rapidly activated (within 30 min) NF-B; this
effect was abolished by treating cells with inhibitors of
protein-tyrosine phosphatase (PTPase), including phenylarsine oxide
(PAO), pervanadate, and diamide. The inhibition was dependent on the
dose and occurred whether added before or at the same time as TNF. PAO
also inhibited the activation even when added 15 min after the TNF
treatment of cells. In contrast to inhibitors of PTPase, okadaic acid
and calyculin A, which block serine-threonine phosphatase, had no
effect. The effect of PTPase inhibitors was not due to the modulation
of TNF receptors. Since both dithiothreitol and dimercaptopropanol
reversed the inhibitory effect of PAO, critical sulfhydryl groups in
the PTPase must be involved in NF-B activation by TNF.
B activation induced by phorbol ester,
ceramide, and interleukin-1 but not that activated by okadaic acid. The
degradation of IB protein, a critical step in NF-B
activation, was also abolished by the PTPase inhibitors as revealed by
immunoblotting. Thus, overall, we demonstrate that PTPase is involved
either directly or indirectly in the pathway leading to the activation
of NF-B.
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