Activation of p53-dependent responses in tumor cells treated with a PARC-interacting peptide.
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.
Mesh Terms:
Apoptosis, Cell Line, Tumor, DNA Topoisomerase IV, Humans, Neoplasms, Signal Transduction, Tumor Suppressor Protein p53
Apoptosis, Cell Line, Tumor, DNA Topoisomerase IV, Humans, Neoplasms, Signal Transduction, Tumor Suppressor Protein p53
Biochem. Biophys. Res. Commun.
Date: Apr. 04, 2008
PubMed ID: 18230339
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