Pardaxin-induced apoptosis enhances antitumor activity in HeLa cells

Peptides. 2011 Jun;32(6):1110-6. doi: 10.1016/j.peptides.2011.04.024. Epub 2011 Apr 30.

Abstract

Pardaxin, a pore-forming antimicrobial peptide that encodes 33 amino acids was isolated from the Red Sea Moses sole, Pardachirus mamoratus. In this study, we investigated its antitumor activity in human fibrosarcoma (HT-1080) cells and epithelial carcinoma (HeLa) cells. In vitro results showed that the synthetic pardaxin peptide had antitumor activity in these two types of cancer cells and that 15μg/ml pardaxin did not lyse human red blood cells. Moreover, this synthetic pardaxin inhibited the proliferation of HT1080 cells in a dose-dependent manner and induced programmed cell death in HeLa cells. DNA fragmentation and increases in the subG1 phase and caspase 8 activities suggest that pardaxin caused HeLa cell death by inducing apoptosis, but had a different mechanism in HT1080 cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis / drug effects*
  • Carcinoma / drug therapy
  • Carcinoma / pathology
  • Caspase 8 / metabolism
  • Cell Proliferation / drug effects
  • Cell-Penetrating Peptides / chemical synthesis
  • Cell-Penetrating Peptides / pharmacology*
  • DNA Fragmentation / drug effects
  • Erythrocytes / drug effects
  • Female
  • Fibrosarcoma / drug therapy
  • Fibrosarcoma / pathology
  • Fish Proteins / chemical synthesis
  • Fish Proteins / pharmacology*
  • Fish Venoms / chemical synthesis
  • Fish Venoms / pharmacology*
  • Fishes, Poisonous / metabolism
  • G1 Phase / drug effects
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Neurotoxins / chemical synthesis
  • Neurotoxins / pharmacology*
  • Organ Specificity
  • Up-Regulation

Substances

  • Cell-Penetrating Peptides
  • Fish Proteins
  • Fish Venoms
  • Neurotoxins
  • pardaxin
  • Caspase 8