Betulinic acid-induced apoptosis in glioma cells: A sequential requirement for new protein synthesis, formation of reactive oxygen species, and caspase processing

J Pharmacol Exp Ther. 1999 Jun;289(3):1306-12.

Abstract

Betulinic acid (BA), a pentacyclic triterpene, is an experimental cytotoxic agent for malignant melanoma. Here, we show that BA triggers apoptosis in five human glioma cell lines. BA-induced apoptosis requires new protein, but not RNA, synthesis, is independent of p53, and results in p21 protein accumulation in the absence of a cell cycle arrest. BA-induced apoptosis involves the activation of caspases that cleave poly(ADP ribose)polymerase. Interactions of death ligand/receptor pairs of the CD95/CD95 ligand family do not mediate BA-induced caspase activation. BA enhances the levels of BAX and BCL-2 proteins but does not alter the levels of BCL-xS or BCL-xL. Ectopic expression of BCL-2 prevents BA-induced caspase activation, DNA fragmentation, and cell death. Furthermore, BA induces the formation of reactive oxygen species that are essential for BA-triggered cell death. The generation of reactive oxygen species is blocked by BCL-2 and requires new protein synthesis but is unaffected by caspase inhibitors, suggesting that BA toxicity sequentially involves new protein synthesis, formation of reactive oxygen species, and activation of crm-A-insensitive caspases.

MeSH terms

  • Antineoplastic Agents, Phytogenic / toxicity*
  • Apoptosis / drug effects*
  • Betulinic Acid
  • Caspases / metabolism*
  • Cell Cycle / drug effects
  • Cell Division
  • Cell Survival
  • Cyclin-Dependent Kinase Inhibitor p21
  • Cyclins / genetics
  • Cycloheximide / pharmacology
  • Cysteine Proteinase Inhibitors / pharmacology
  • DNA Fragmentation
  • Enzyme Activation
  • Fas Ligand Protein
  • Glioma
  • Humans
  • Kinetics
  • Membrane Glycoproteins / pharmacology
  • Oligopeptides / pharmacology
  • Pentacyclic Triterpenes
  • Proto-Oncogene Proteins / biosynthesis
  • Proto-Oncogene Proteins c-bcl-2 / biosynthesis*
  • Proto-Oncogene Proteins c-bcl-2 / genetics
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • Reactive Oxygen Species / physiology*
  • Triterpenes / toxicity*
  • Tumor Cells, Cultured
  • bcl-2-Associated X Protein
  • bcl-X Protein
  • fas Receptor / drug effects
  • fas Receptor / physiology

Substances

  • Antineoplastic Agents, Phytogenic
  • BAX protein, human
  • BCL2L1 protein, human
  • CDKN1A protein, human
  • Cyclin-Dependent Kinase Inhibitor p21
  • Cyclins
  • Cysteine Proteinase Inhibitors
  • FASLG protein, human
  • Fas Ligand Protein
  • Membrane Glycoproteins
  • Oligopeptides
  • Pentacyclic Triterpenes
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Reactive Oxygen Species
  • Triterpenes
  • aspartyl-glutamyl-valyl-aspartal
  • bcl-2-Associated X Protein
  • bcl-X Protein
  • fas Receptor
  • Cycloheximide
  • Caspases
  • Betulinic Acid