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A proteomic analysis of the effect of mapk pathway activation on l-glutamate-induced neuronal cell death
Cellular & Molecular Biology Letters volume 12, pages 139–147 (2007)
Abstract
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.
Abbreviations
- Cy2:
-
3-(4-carboxymethyl) phenylmethyl-3’-ethyloxacarbocyanine halide
- Cy3:
-
1-(5-carboxypentile)-1’-propylindocarbocyanine halide
- Cy5:
-
1-(5-carboxypentile)-1’-methylindocarbocyanine halide
- DIGE:
-
differential in gel electrophoresis
- GSH:
-
glutathione
- MAPK:
-
mitogen-activated protein kinase
- MEK:
-
MAPK/ERK kinase
- ROS:
-
reactive oxygen species
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Kang, S., Kim, E.Y., Bahn, Y.J. et al. A proteomic analysis of the effect of mapk pathway activation on l-glutamate-induced neuronal cell death. Cell Mol Biol Lett 12, 139–147 (2007). https://doi.org/10.2478/s11658-006-0057-8
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DOI: https://doi.org/10.2478/s11658-006-0057-8