Activation of p53-dependent responses in tumor cells treated with a PARC-interacting peptide

Journal Article · Fri Apr 04 00:00:00 EDT 2008 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2008.01.093· OSTI ID:21043686

Vitali, Roberta; Cesi, Vincenzo; Tanno, Barbara ^[1]; Ferrari-Amorotti, Giovanna ^[2]; Dominici, Carlo ^[3]; Calabretta, Bruno ^[2]; Raschella, Giuseppe ^[1]

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1. ENEA Research Center Casaccia, Section of Toxicology and Biomedical Sciences, Via Anguillarese, 301, Rome 00123 (Italy)
2. Department of Biomedical Sciences, University of Modena, Modena (Italy)
3. 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

Related Subjects

60 APPLIED LIFE SCIENCES
APOPTOSIS
GENES
HYBRIDIZATION
NEOPLASMS
PEPTIDES
TUMOR CELLS