Upstream control of apoptosis by caspase-2 in serum-deprived primary neurons

Apoptosis. 2005 Dec;10(6):1243-59. doi: 10.1007/s10495-005-1681-x.

Abstract

During development as well as in pathological situations, neurons that fail to find appropriate targets or neurotrophic factors undergo cell death. Using primary cortical neurons subjected to acute serum-deprivation (SD), we have examined caspases activation, mitochondrial dysfunction and cell death parameters. Among a panel of metabolic, signaling and caspases inhibitors only those able to interfere with caspase-2 like activity protect primary neurons against SD-induced cell death. In situ detection and subcellular fractionation demonstrate a very early activation of cytosolic caspase-2, which controls Bax cleavage, relocalization and mitochondrial membrane permeabilization (MMP). Both z-VDVAD-fmk and a siRNA specific for caspase-2 abolish Bax changes, mitochondrial membranes permeabilization, as well as cytochrome c release-dependent activation of caspase-9/caspase-3, nuclear alterations, phosphatidylserine exposure, neurites dismantling and neuronal death. Hence, caspase-2 is an early checkpoint for apoptosis initiation in primary neurons subjected to serum deprivation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis* / drug effects
  • Caspase 2 / deficiency
  • Caspase 2 / metabolism*
  • Cell Survival / drug effects
  • Cells, Cultured
  • Cytochromes c / metabolism
  • Enzyme Activation / drug effects
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Mice
  • Mitochondria / drug effects
  • Mitochondria / enzymology
  • Mitochondria / metabolism
  • Models, Biological
  • Neurons / cytology*
  • Neurons / drug effects
  • Neurons / enzymology*
  • Peptides / pharmacology
  • Protein Transport / drug effects
  • RNA Interference
  • Serum*
  • bcl-2-Associated X Protein / metabolism

Substances

  • Enzyme Inhibitors
  • Peptides
  • bcl-2-Associated X Protein
  • Cytochromes c
  • Caspase 2