MKP-1 contributes to oxidative stress-induced apoptosis via inactivation of ERK1/2 in SH-SY5Y cells
- Authors
- Kim G.S.; Choi Y.K.; Song S.S.; Kim W.-K.; Han B.H.
- Issue Date
- 2005
- Keywords
- Apoptosis; Caspase-3; ERK1/2; MKP-1; Neurons; Oxidative stress; Phosphatases; siRNA; Ubiquitin-proteasome pathway
- Citation
- Biochemical and Biophysical Research Communications, v.338, no.4, pp 1732 - 1738
- Pages
- 7
- Indexed
- SCOPUS
- Journal Title
- Biochemical and Biophysical Research Communications
- Volume
- 338
- Number
- 4
- Start Page
- 1732
- End Page
- 1738
- URI
- https://scholarworks.korea.ac.kr/kumedicine/handle/2020.sw.kumedicine/20135
- DOI
- 10.1016/j.bbrc.2005.10.143
- ISSN
- 0006-291X
1090-2104
- Abstract
- Mitogen-activated protein (MAP) kinase phosphatase-1 (MKP-1) is a dual specificity phosphatase that negatively regulates the MAP kinases. In this study, we found that levels of MKP-1 expression were transiently decreased within 3 h, followed by an increase 6-9 h after H2O 2-induced oxidative stress in human neuroblastoma SH-SY5Y cells. There was a strong negative correlation between MKP-1 expression and ERK1/2 phosphorylation levels. Treatment of cells with a proteasomal inhibitor MG132 decreased the oxidative stress-induced degradation of MKP-1, resulting in dephosphorylation of ERK1/2. MG132 potentiated hydrogen peroxide-induced cell death, which was attenuated by a phosphatase inhibitor sodium orthovanadate. Suppression of MKP-1 expression by transfection with siRNA duplexes specific to MKP-1 transcript resulted in a decrease in oxidative stress-induced cell death. These data therefore suggest that MKP-1, a negative regulator of ERK1/2, plays a proapoptotic role in oxidative stress-induced cell death in a neuronal cell line. © 2005 Elsevier Inc. All rights reserved.
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Collections - 1. Basic Science > Department of Neuroscience > 1. Journal Articles
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