Caspase-dependent and independent cell death in rat hepatoma 5123tc cells

Apoptosis. 2000 Jun;5(3):265-75. doi: 10.1023/a:1009608630145.

Abstract

The objective of this study was to establish whether apoptosis in 5123tc rat hepatoma cells required the caspase-3 dependent pathway. Apoptosis was induced by either growth factor deprivation or treatment with a topoisomerase II inhibitor, VM26, in the absence or presence of caspase inhibitors (DEVD-fmk, z-VAD-fmk and BAF). The results indicated that, although these inhibitors at 10 microM concentration completely blocked caspase-3 activity, they had no effect on either the rate of cell death or on any other apoptotic features, e.g., chromatin condensation, DNA fragmentation, protein cleavage, suggesting that caspase-3 was not required to mediate nuclear destruction in these hepatoma cells. At higher concentrations, up to 100 microM, z-VAD-fmk and BAF, but not DEVD-fmk, did block apoptosis, however, they also caused cell swelling and membrane permeabilization, which are the hallmarks of necrotic cell death. Clearly, high concentrations of these inhibitors must have interfered non-specifically with other metabolic pathways, e.g., z-VAD-fmk at a high concentration blocked protein phosphorylation, and caused cell death by a different mechanism.

MeSH terms

  • Amino Acid Chloromethyl Ketones / pharmacology
  • Animals
  • Apoptosis* / drug effects
  • Blotting, Western
  • Carcinoma, Hepatocellular
  • Caspase 3
  • Caspase Inhibitors
  • Caspases / metabolism*
  • Cell Nucleus / metabolism
  • Culture Media, Serum-Free
  • Cysteine Proteinase Inhibitors / pharmacology*
  • DNA Fragmentation
  • Electrophoresis, Gel, Pulsed-Field
  • Electrophoresis, Gel, Two-Dimensional
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Lamins
  • Microscopy, Fluorescence
  • Nuclear Proteins / metabolism
  • Phosphorylation / drug effects
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerases
  • Proteins / metabolism
  • Rats
  • Teniposide / pharmacology
  • Tumor Cells, Cultured

Substances

  • Amino Acid Chloromethyl Ketones
  • Caspase Inhibitors
  • Culture Media, Serum-Free
  • Cysteine Proteinase Inhibitors
  • Enzyme Inhibitors
  • Lamins
  • Nuclear Proteins
  • Proteins
  • benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone
  • Teniposide
  • Parp1 protein, rat
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerases
  • CASP3 protein, human
  • Casp3 protein, rat
  • Caspase 3
  • Caspases