PR-39, a porcine antimicrobial peptide, inhibits apoptosis: involvement of caspase-3

Dev Comp Immunol. 2004 Feb;28(2):163-9. doi: 10.1016/s0145-305x(03)00135-6.

Abstract

The porcine antimicrobial peptide, PR-39, has several activities beyond its function of killing bacteria. Here we report that PR-39 alters macrophage viability by inhibiting apoptosis, which was induced by nutrient depletion, LPS stimulation or camptothecin treatment. This antiapoptotic effect was pronounced resulting in significant reductions in annexin-V binding to externalized phosphatidylserine and was associated with a decrease in caspase-3 activity. These findings suggest that PR-39, a porcine neutrophil-derived antimicrobial peptide, might function in the inflammatory milieu not only to kill bacteria, but also to aid in modulating the viability of inflammatory cells by regulating apoptosis.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Annexin A5 / metabolism
  • Antimicrobial Cationic Peptides / pharmacology*
  • Apoptosis / drug effects*
  • Camptothecin / pharmacology
  • Caspase 3
  • Caspases / metabolism*
  • Cells, Cultured
  • DNA Fragmentation / drug effects
  • Enzyme Inhibitors / pharmacology
  • Lipopolysaccharides / pharmacology*
  • Macrophages / drug effects
  • Macrophages / metabolism*
  • Mice
  • Swine

Substances

  • Annexin A5
  • Antimicrobial Cationic Peptides
  • Enzyme Inhibitors
  • Lipopolysaccharides
  • PR 39
  • Casp3 protein, mouse
  • Caspase 3
  • Caspases
  • Camptothecin