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pubmed-article:16970918pubmed:abstractTextPRIMA-1 has emerged as a small molecule that restores the wild type function to mutant p53. To identify molecular targets that are involved in PRIMA-1-induced apoptosis, we used a proteomics approach with two-dimensional gel electrophoresis coupled with liquid chromatography-tandem mass spectrometry for protein identification. By comparing the proteome of the PRIMA-1-treated MDA-231 breast carcinoma cells with that of MCF-7 cells, we have identified seven proteins that upregulated only in MDA-231 cells as a result of PRIMA-1-induced apoptosis. The identified proteins are involved in anaerobic glycolysis and in mitochondrial intrinsic apoptosis. Treatment of MDA-231 cells with PRIMA-1 resulted in the release of mitochondrial cytochrome c as well as the activation of caspase-3, which are essential for the execution of apoptosis. We present evidence to suggest that PRIMA-1-induced apoptosis in breast cancer cells with mutated p53 function involved the expression of proteins required for the activation of mitochondrial intrinsic pathway that is glycolysis-relevant.lld:pubmed
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pubmed-article:16970918pubmed:authorpubmed-author:LeeKyungheeKlld:pubmed
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pubmed-article:16970918pubmed:pagination1117-24lld:pubmed
pubmed-article:16970918pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:16970918pubmed:year2006lld:pubmed
pubmed-article:16970918pubmed:articleTitleExpression proteomics to p53 mutation reactivation with PRIMA-1 in breast cancer cells.lld:pubmed
pubmed-article:16970918pubmed:affiliationDepartment of Pharmaceutical Sciences, Washington State University, 259 Wegner Hall, Pullman, WA 99164-6534, USA.lld:pubmed
pubmed-article:16970918pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16970918pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed