Evidence that tumor necrosis factor triggers apoptosis in human endothelial cells by interleukin-1-converting enzyme-like protease-dependent and -independent pathways

Lab Invest. 1997 Sep;77(3):257-67.

Abstract

Cultured human endothelial cells (EC) resist tumor necrosis factor (TNF)-mediated apoptosis. However, the combination of TNF and the protein synthesis inhibitor cycloheximide (CHX) induces apoptosis in up to 50% of EC within 24 hours. TNF + CHX killing is effectively blocked by transfected CrmA protein or treatment with Z-VAD.fmk peptide-both inhibitors of interleukin-1-converting enzyme-like proteases-but not by transfected antiapoptotic proteins Bcl-2, Bcl-XL, or A1. C6-ceramide (cer) can also sensitize EC to TNF-induced apoptosis. TNF + cer killing, which can affect more than 50% of EC, is not effectively inhibited by CrmA or Z-VAD frank, but can be readily blocked by Bcl-2, Bcl-XL, or A1. Both TNF + CHX and TNF+ cer killing are induced by a TNF mutein that only interacts with the type 1 TNF receptor, and both responses can be inhibited by the antiapoptotic protein A20. These data suggest that TNF activates two biochemically separable pathways of EC injury.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Apoptosis / physiology*
  • Caspase 1
  • Cells, Cultured
  • Ceramides / pharmacology
  • Cycloheximide / pharmacology
  • Cysteine Endopeptidases / physiology*
  • Drug Resistance
  • Endopeptidases / physiology*
  • Endothelium, Vascular / cytology
  • Endothelium, Vascular / drug effects*
  • Humans
  • Microscopy, Electron
  • Protein Synthesis Inhibitors / pharmacology
  • Signal Transduction
  • Tumor Necrosis Factor-alpha / pharmacology*

Substances

  • Ceramides
  • Protein Synthesis Inhibitors
  • Tumor Necrosis Factor-alpha
  • Cycloheximide
  • Endopeptidases
  • Cysteine Endopeptidases
  • Caspase 1