Activation of p53-dependent responses in tumor cells treated with a PARC-interacting peptide
Journal Article
·
· Biochemical and Biophysical Research Communications
- ENEA Research Center Casaccia, Section of Toxicology and Biomedical Sciences, Via Anguillarese, 301, Rome 00123 (Italy)
- Department of Biomedical Sciences, University of Modena, Modena (Italy)
- Department of Pediatrics, La Sapienza University, Rome (Italy)
We tested the activity of a p53 carboxy-terminal peptide containing the PARC-interacting region in cancer cells with wild type cytoplasmic p53. Peptide delivery was achieved by fusing it to the TAT transduction domain (TAT-p53-C-ter peptide). In a two-hybrid assay, the tetramerization domain (TD) of p53 was necessary and sufficient to bind PARC. The TAT-p53-C-ter peptide disrupted the PARC-p53 complex. Peptide treatment caused p53 nuclear relocation, p53-dependent changes in gene expression and enhancement of etoposide-induced apoptosis. These studies suggest that PARC-interacting peptides are promising candidates for the enhancement of p53-dependent apoptosis in tumors with wt cytoplasmic p53.
- OSTI ID:
- 21043686
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 368, Issue 2; Other Information: DOI: 10.1016/j.bbrc.2008.01.093; PII: S0006-291X(08)00128-9; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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