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

Roberta Vitali1, Vincenzo Cesi, Barbara Tanno

  • 1ENEA Research Center Casaccia, Section of Toxicology and Biomedical Sciences, Via Anguillarese, 301, Rome 00123, Italy.

Biochemical and Biophysical Research Communications
|January 31, 2008
PubMed

Insights

A novel peptide targeting the PARC-interacting region of p53 enhances cancer cell apoptosis. This peptide, delivered via the TAT transduction domain, disrupts the PARC-p53 complex, promoting tumor cell death.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Cellular Biology

Background:

  • Wild-type cytoplasmic p53 plays a crucial role in cancer cell apoptosis.
  • PARC (p53-associated protein) interacts with p53, influencing its cellular localization and function.
  • Targeting protein-protein interactions offers a potential therapeutic strategy in oncology.

Purpose of the Study:

  • To investigate the therapeutic potential of a p53 carboxy-terminal peptide fused to the TAT transduction domain (TAT-p53-C-ter) for cancer treatment.
  • To determine if the tetramerization domain (TD) of p53 is essential for PARC binding.
  • To evaluate the peptide's ability to disrupt the PARC-p53 complex and induce apoptosis in cancer cells.

Main Methods:

  • Utilized a two-hybrid assay to assess the interaction between p53's tetramerization domain and PARC.
  • Developed and employed a TAT-p53-C-ter peptide for targeted delivery into cancer cells.
  • Analyzed p53 nuclear relocation, gene expression changes, and etoposide-induced apoptosis following peptide treatment.

Main Results:

  • The tetramerization domain (TD) of p53 was found to be necessary and sufficient for binding to PARC.
  • The TAT-p53-C-ter peptide effectively disrupted the endogenous PARC-p53 complex within cancer cells.
  • Peptide treatment led to the nuclear translocation of p53, altered p53-dependent gene expression, and enhanced apoptosis induced by etoposide.

Conclusions:

  • PARC-interacting peptides, specifically the TAT-p53-C-ter peptide, demonstrate significant potential for enhancing p53-dependent apoptosis.
  • These peptides represent a promising therapeutic strategy for tumors harboring wild-type cytoplasmic p53.
  • Targeting the PARC-p53 interaction could be a viable approach to improve cancer treatment outcomes.

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