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J Biol Chem, Vol. 273, Issue 30, 18898-18905, July 24, 1998
From the Department of Cell and Tumor Biology, The Beckman Research
Institute at City of Hope, Duarte, California 91010-3000
Pyrrolidine dithiocarbamate (PDTC) is a thiol
compound widely used to study the activation of redox-sensitive
transcription factors. Although normally used as an antioxidant, PDTC
has been shown to exert pro-oxidant activity on proteins both in
vitro and in vivo. Because p53 redox status has been
shown to alter its DNA binding capability, we decided to test the
effect of PDTC on p53 activation. In this communication, we report that
PDTC inhibits the activation of temperature-sensitive murine
p53Val-135 (TSp53) in the transformed rat embryo fibroblast
line, A1-5, as well as wild-type human p53 in the normal diploid
fibroblast line, WS1neo. In A1-5 cells, PDTC abrogated UV- and
temperature shift-induced TSp53 nuclear translocation and p53-mediated
transactivation of MDM2. PDTC also blocked UV-induced
accumulation of wild-type p53 in WS1neo cells. Continual presence of
PDTC was required for its effect as both UV-induced nuclear
translocation and accumulation resumed after PDTC removal. We next
investigated whether PDTC treatment altered the p53 redox state. We
found that PDTC increased p53 cysteine residue oxidation in
vivo. This represents the first direct evidence showing that the
p53 redox state can be altered in vivo and that increased
oxidation correlates with its inability to perform its downstream
functions.
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