CopA3 peptide from Copris tripartitus induces apoptosis in human leukemia cells via a caspase-independent pathway

BMB Rep. 2012 Feb;45(2):85-90. doi: 10.5483/BMBRep.2012.45.2.85.

Abstract

Our previous study demonstrated that CopA3, a disulfide dimer of the coprisin peptide analogue (LLCIALRKK), has antibacterial activity. In this study, we assessed whether CopA3 caused cellular toxicity in various mammalian cell lines. CopA3 selectively caused a marked decrease in cell viability in Jurkat T, U937, and AML-2 cells (human leukemia cells), but was not cytotoxic to Caki or Hela cells. Fragmentation of DNA, a marker of apoptosis, was also confirmed in the leukemia cell lines, but not in the other cells. CopA3-induced apoptosis in leukemia cells was mediated by apoptosis inducing factor (AIF), indicating induction of a caspase-independent signaling pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis / drug effects*
  • Apoptosis Inducing Factor / metabolism
  • Caspases / metabolism*
  • Cell Line, Tumor
  • Coleoptera / metabolism
  • HeLa Cells
  • Humans
  • Insect Proteins / chemical synthesis
  • Insect Proteins / therapeutic use
  • Insect Proteins / toxicity*
  • Jurkat Cells
  • Leukemia / drug therapy
  • Leukemia / metabolism
  • Signal Transduction

Substances

  • Apoptosis Inducing Factor
  • Insect Proteins
  • coprisin peptide, Copris tripartitus
  • Caspases