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. © 2008 Elsevier Inc. All rights reserved.
|Pages (from-to)||350 - 356|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 4 Apr 2008|
All Science Journal Classification (ASJC) codes
- Molecular Biology
Vitali, R., Cesi, V., Tanno, B., Ferrari-Amorotti, G., Dominici, C., Calabretta, B., & Raschellà, G. (2008). Activation of p53-dependent responses in tumor cells treated with a PARC-interacting peptide. Biochemical and Biophysical Research Communications, 368(2), 350 - 356. https://doi.org/10.1016/j.bbrc.2008.01.093