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J Biol Chem, Vol. 273, Issue 9, 5067-5072, February 27, 1998
From the Department of Bioimmunotherapy and Drug Carriers,
University of Texas M. D. Anderson Cancer Center,
Houston, Texas 77030
Tumor necrosis factor (TNF)-mediated apoptotic
signaling has been characterized by activation of specific protease or
protein kinase cascades that regulate the onset of apoptosis. TNF has also been shown to induce oxidative or genotoxic stress in some cell
types, and apoptotic potential may be determined by the cellular response to this stress. To determine the role of genotoxic stress in
TNF-mediated apoptosis, we examined cellular accumulation of p53 in
TNF-treated ME-180 cells selected for apoptotic sensitivity (ME-180S)
or resistance (ME-180R) to TNF. Although TNF was able to activate
receptor-mediated signaling in either cell line, p53 accumulation was
measurable only in apoptotically sensitive ME-180S cells. TNF-induced
changes in p53 levels were detected 1 h after treatment, and peak
levels were measurable 4-8 h after TNF exposure. TNF was unable to
induce p21WAF1 in either cell line but affected the stability of this
protein in apoptotically responsive ME-180S cells. Evidence of p21WAF1
proteolysis was detected by monitoring the appearance of a 16-kDa
immunoblottable p21WAF1 fragment, which became detectable 4 h
after TNF addition and increased in content before the onset of DNA
fragmentation (16-24 h). The kinetics of p21WAF1 proteolysis closely
paralleled those of poly(ADP-ribose) polymerase, suggesting cleavage of
p21WAF1 by activation of an apoptotic protease. Pretreatment of ME-180S
cells with the apoptotic protease inhibitor YVAD blocked TNF-induced
apoptosis and prevented both poly(ADP-ribose) polymerase and p21WAF1
degradation but did not affect p53 induction. These results provide
evidence for the early onset of genotoxic stress in cells committed to
TNF-mediated apoptosis and for divergence in propagation of this signal
in non-responsive cells. In addition, TNF-induced p21WAF1 proteolysis may be mediated by an apoptotic protease and may contribute to the
apoptotic process by disrupting p53 signaling, altering cell cycle
inhibition, and limiting cellular recovery from genotoxic stress.
Tumor Necrosis Factor-induced Apoptosis Stimulates p53
Accumulation and p21WAF1 Proteolysis in ME-180 Cells
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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