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Papers In Press, published online ahead of print February 13, 2001
J. Biol. Chem, 10.1074/jbc.C100025200
Submitted on January 18, 2001
Revised on February 9, 2001
Accepted on February 12, 2001
East Wing (First floor), Centre for Cellular and Molecular Biology, Hyderabad, Andhra pradesh 500 007
Corresponding Author: gshyam{at}ccmb.ap.nic.in
The tumor suppressor protein p53 is a sequence-specific DNA-binding protein and its biological responses are very often mediated by transcriptional activation of various target genes. Here we show that caspase-1 (interleukin-1b converting enzyme) which plays a role in the production of proinflammatory cytokines and in apoptosis, is a transcriptional target of p53. Caspase-1 mRNA levels increased upon overexpression of p53 by transfection in MCF-7 cells. Human caspase-1 promoter showed a sequence homologous to consensus p53- binding site. This sequence bound to p53 in gel shift assays. A caspase-1 promoter-reporter construct was activated 6-8-fold by co-transfection with normal p53 but not by mutant p53 (His273) in HeLa as well as MCF-7 cells. Mutation of the p53-binding site in caspase-1 promoter abolished transactivation by p53. Treatment of p53 positive MCF-7 cells with DNA-damaging drug doxorubicin, which increases p53 levels, enhanced caspase-1 promoter activity 4-5-fold but similar treatment of MCF-7-mp53 (a clone of MCF-7 cells expressing mutant p53) and p53 negative HeLa cells with doxorubicin did not increase caspase-1 promoter activity. Doxorubicin treatment increased caspase-1 mRNA levels in MCF-7 cells but not in MCF-7-mp53 or HeLa cells. These results show that endogenous p53 can regulate caspase-1 gene expression.
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