Cholesteryl-hemisuccinate-induced apoptosis of promyelocytic leukemia HL-60 cells through a cyclosporin A-insensitive mechanism

Biochem Pharmacol. 2003 Feb 1;65(3):339-48. doi: 10.1016/s0006-2952(02)01518-6.

Abstract

We reported previously that alpha-tocopheryl-succinate (VES) induced apoptosis of cultured human promyelocytic leukemia cells (HL-60) (Free Radic Res 2000;33:407-18). We have now studied the effect of cholesteryl-hemisuccinate (CS) on the fate of HL-60 cells to clarify whether CS has an effect similar to that of VES. CS inhibited the growth of HL-60 cells without differentiation to granulocytes and induced DNA fragmentation and ladder formation. CS inhibited the phosphorylation of pleckstrin homology domain-containing protein kinase B (Akt) and initiated the activation of a caspase cascade. CS triggered the reaction leading to the cleavage of Bid and also released cytochrome c (Cyt. c) from mitochondria. In addition, CS induced mitochondrial membrane depolarization and translocation of Bax to mitochondria in HL-60 cells. However, CS did not induce an increase in the concentration of intracellular calcium ions in HL-60 cells. The membrane depolarization, Cyt. c release, and DNA fragmentation were inhibited by z-VAD-fluoromethylketone (z-VAD-fmk), a pan-caspase inhibitor, but not by cyclosporin A, an inhibitor of membrane permeability transition. These results suggested that CS-induced apoptosis of HL-60 cells might be caused by inhibiting Akt phosphorylation following cleavage of Bid through caspase-8 activation and subsequently via an Apaf complex-caspase cascade pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Chloromethyl Ketones / pharmacology
  • Antineoplastic Agents / pharmacology*
  • Apoptosis*
  • BH3 Interacting Domain Death Agonist Protein
  • Calcium / metabolism
  • Carrier Proteins / metabolism
  • Caspases / metabolism
  • Cell Cycle / drug effects
  • Cell Differentiation / drug effects
  • Cell Division / drug effects
  • Cholesterol Esters / pharmacology*
  • Cyclic AMP / metabolism
  • Cyclosporine / pharmacology*
  • Cytochrome c Group / metabolism
  • DNA Fragmentation / drug effects*
  • Enzyme Activation / drug effects
  • Enzyme Inhibitors / pharmacology
  • HL-60 Cells
  • Humans
  • Leukemia, Myeloid / pathology
  • Membrane Potentials / drug effects
  • Mitochondria / drug effects
  • Mitochondria / enzymology
  • Mitochondria / physiology
  • Phosphorylation / drug effects
  • Protein Serine-Threonine Kinases*
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-akt
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • bcl-2-Associated X Protein

Substances

  • Amino Acid Chloromethyl Ketones
  • Antineoplastic Agents
  • BAX protein, human
  • BH3 Interacting Domain Death Agonist Protein
  • BID protein, human
  • Carrier Proteins
  • Cholesterol Esters
  • Cytochrome c Group
  • Enzyme Inhibitors
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • bcl-2-Associated X Protein
  • benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone
  • Cyclosporine
  • Cyclic AMP
  • AKT1 protein, human
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt
  • Caspases
  • Calcium
  • cholesteryl succinate