Open Access

A proteomic analysis of the effect of mapk pathway activation on l-glutamate-induced neuronal cell death

  • Sunghyun Kang1,
  • Eun Young Kim1,
  • Young Jae Bahn1,
  • Jin Woong Chung,
  • Do Hee Lee1,
  • Sung Goo Park1,
  • Tae-Sung Yoon1,
  • Byoung Chul Park1 and
  • Kwang-Hee Bae1Email author
Cellular & Molecular Biology LettersAn International Journal200612:57

Received: 16 May 2006

Accepted: 27 July 2006

Published: 24 November 2006


Oxidative stress has been implicated in the pathogenesis of neuronal degenerative diseases. It is also widely known that oxidative stress induces mitogen-activated protein kinase (MAPK) signaling cascades. In this study, we used proteomic analysis to investigate the role of the MAPK pathway in oxidative stress-induced neuronal cell death. The results demonstrated that several proteins, including eukaryotic translation elongation factor 2 (eEF2) and enolase I, showed a differential expression pattern during the neuronal cell death process, and this was MAPK pathway dependent. Several chaperone and cytoskeletal proteins including heat shock protein 70, calreticulin, vimentin, prolyl 4-hydroxylase β polypeptide, and transgelin 2 were up-or down-regulated, despite their expressions not depending on the MAPK pathway. These findings strongly suggest that the expressions of proteins which play protective roles are independent of the MAPK pathway. On the other hand, eEF2 and enolase I may be the downstream targets of the MAPK pathway.

Key words

ApoptosisHT22MAPKOxidative stressReactive oxygen speciesU0126