Title | Activation of p53-dependent responses in tumor cells treated with a PARC-interacting peptide |
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Publication Type | Articolo su Rivista peer-reviewed |
Year of Publication | 2008 |
Authors | Vitali, Roberta, Cesi Vincenzo, Tanno Barbara, Ferrari-Amorotti G., Dominici C., Calabretta B., and Raschellà Giuseppe |
Journal | Biochemical and Biophysical Research Communications |
Volume | 368 |
Pagination | 350-356 |
ISSN | 0006291X |
Keywords | Apoptosis, article, cancer cell, caspase, Cell Line, controlled study, DNA binding, DNA Topoisomerase IV, doxorubicin, etoposide, Flow cytometry, Gene expression, genotoxicity, human, human cell, Humans, immunocytochemistry, Neoplasms, nuclear localization signal, priority journal, protein domain, protein p53, protein ParC, protein protein interaction, real time polymerase chain reaction, signal transduction, transactivator protein, Tumor, Tumor Suppressor Protein p53, two hybrid system, Western blotting, wild type |
Abstract | 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. |
Notes | cited By 7 |
URL | https://www.scopus.com/inward/record.uri?eid=2-s2.0-39549119777&doi=10.1016%2fj.bbrc.2008.01.093&partnerID=40&md5=6c8de12eebebdc5486cc79890044620c |
DOI | 10.1016/j.bbrc.2008.01.093 |
Citation Key | Vitali2008350 |