C-terminal domain of human CAP18 antimicrobial peptide induces apoptosis in oral squamous cell carcinoma SAS-H1 cells

Cancer Lett. 2004 Aug 30;212(2):185-94. doi: 10.1016/j.canlet.2004.04.006.

Abstract

Mammalian myeloid and epithelial cells express many antimicrobiotic peptides that contribute to innate host defense against invading microbes. In the present study, a 27-mer peptide of the C-terminal domain (hCAP18(109-135)) and analogs of the antimicrobial peptide human cathelicidin LL-37/human cationic antimicrobial protein 18 (hCAP18) were examined for tumoricidal activity. In vitro results showed that hCAP18(109-135) induced apoptosis in human oral squamous cell carcinoma (OSCC), SAS-H1 cells. The hCAP18(109-135) induced mitochondrial depolarization and apoptosis in SAS-H1 cells, but not in healthy human gingival fibroblasts (HGF) and human keratinocyte line HaCaT cells. Caspases were not activated during hCAP18(109-135)-induced apoptosis in SAS-H1 cells. The results indicate that hCAP18(109-135) may induce caspase-independent apoptosis in OSCC but not in normal cells. hCAP18(109-135) can therefore be a useful anti-tumor therapeutic agent in the treatment of OSCC.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Infective Agents / pharmacology*
  • Antimicrobial Cationic Peptides / chemistry*
  • Antimicrobial Cationic Peptides / pharmacology*
  • Apoptosis*
  • Carcinoma, Squamous Cell / drug therapy
  • Carcinoma, Squamous Cell / pathology
  • Caspase 3
  • Caspases / metabolism
  • Cathelicidins
  • Cell Death
  • Cell Line, Tumor
  • Cells, Cultured
  • DNA / metabolism
  • DNA Fragmentation
  • Dose-Response Relationship, Drug
  • Enzyme Activation
  • Fibroblasts / metabolism
  • Humans
  • Membrane Potentials
  • Mitochondria / metabolism
  • Mitochondria / pathology
  • Mouth Neoplasms / drug therapy
  • Mouth Neoplasms / pathology
  • Peptides / chemistry*
  • Protein Structure, Tertiary
  • Time Factors

Substances

  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • Cathelicidins
  • Peptides
  • DNA
  • CASP3 protein, human
  • Caspase 3
  • Caspases