Activation, involvement and nuclear translocation of c-Jun N-terminal protein kinase 1 and 2 in glutamate-induced apoptosis in cultured rat cortical neurons

Brain Res. 2002 Nov 29;956(2):194-201. doi: 10.1016/s0006-8993(02)03435-2.

Abstract

Previous studies showed that c-Jun N-terminal protein kinase 1 and 2 (JNK1&2) were activated in some cases of excitotoxicity. In the present study, activation, subcellular distribution, involvement and upstream regulation of JNK1&2 were investigated in glutamate-induced excitotoxicity in cultured rat cortical neurons. As indicated by Western immunoblot from whole cellular extracts, while JNK1&2 were not significantly changed, the activated JNK1&2 (diphosphorylated JNK1&2, p-JNK1&2), were rapidly increased at 15 min exposure to 50 microM glutamate and reverted to basal level at 12 h after exposure, followed by a significant increase of apoptotic-like cell death as detected by DAPI (a fluorescent DNA binding dye) staining at 9-18 h after exposure. Blockage of the increase of p-JNK1&2 with JNK1&2 antisense oligodeoxynucleotides significantly prevented the cell death. The increase of p-JNK1&2 was largely prevented by blockage of NMDA receptor (a subtype of glutamate receptor) or protein kinase C (PKC), and each blockage also largely prevented the cell death. Combined blockage of PKC and JNK1&2 had no additive protective effect against cell death. Immunocytochemistry study showed at 15 min of glutamate exposure a whole cellular but mainly nuclear increase of p-JNK1&2, together with mild plasma decrease but large nuclear increase of JNK1&2, all of which were also largely prevented by blockage of NMDA receptor or PKC. These results suggested that mainly downstream of NMDA receptor-PKC pathway JNK1&2 were activated, nuclear translocated and causally involved in the glutamate-induced excitotoxicity, possibly through a nuclear elevation of p-JNK1&2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis* / drug effects
  • Blotting, Western
  • Cell Culture Techniques
  • Cell Nucleus / enzymology
  • Cell Nucleus / genetics
  • Cell Nucleus / metabolism*
  • Enzyme Activation
  • Glutamic Acid
  • Immunohistochemistry
  • Mitogen-Activated Protein Kinase 8
  • Mitogen-Activated Protein Kinase 9
  • Mitogen-Activated Protein Kinases / metabolism*
  • Neocortex / cytology
  • Neocortex / metabolism*
  • Neurons / ultrastructure*
  • Neurotoxins
  • Nitric Oxide Synthase / metabolism
  • Phosphorylation
  • Protein Kinase C / metabolism
  • Rats
  • Rats, Sprague-Dawley
  • Receptors, N-Methyl-D-Aspartate / metabolism
  • Translocation, Genetic

Substances

  • Neurotoxins
  • Receptors, N-Methyl-D-Aspartate
  • Glutamic Acid
  • Nitric Oxide Synthase
  • Mitogen-Activated Protein Kinase 9
  • Protein Kinase C
  • Mitogen-Activated Protein Kinase 8
  • Mitogen-Activated Protein Kinases