Journal article
Expression proteomics to p53 mutation reactivation with PRIMA-1 in breast cancer cells
Biochemical and biophysical research communications, Vol.349(3), pp.1117-1124
2006
Handle:
https://hdl.handle.net/2376/109279
PMID: 16970918
Abstract
PRIMA-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.
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Details
- Title
- Expression proteomics to p53 mutation reactivation with PRIMA-1 in breast cancer cells
- Creators
- Kyunghee Lee - Department of Pharmaceutical Sciences, Washington State University, 259 Wegner Hall, Pullman, WA 99164-6534, USATao Wang - Department of Pharmaceutical Sciences, Washington State University, 259 Wegner Hall, Pullman, WA 99164-6534, USAAndrzej J Paszczynski - Environmental Biotechnology Institute, University of Idaho, Moscow, ID 83844, USASayed S Daoud - Department of Pharmaceutical Sciences, Washington State University, 259 Wegner Hall, Pullman, WA 99164-6534, USA
- Publication Details
- Biochemical and biophysical research communications, Vol.349(3), pp.1117-1124
- Academic Unit
- Pharmaceutical Sciences, Department of
- Publisher
- Elsevier Inc
- Identifiers
- 99900547494901842
- Language
- English
- Resource Type
- Journal article