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- W2048468692 abstract "Abstract Recent studies revealed that activation of extracellular signal-regulated kinase (ERK) may contribute to apoptosis, a cell death process involved in oxidative stress. We investigated phosphorylation of ERK1/2 and oxidative stress after transient focal cerebral ischemia (FCI) using transgenic (Tg) mice that overexpress copper/zinc-superoxide dismutase (SOD1). Mice were subjected to 60 min of middle cerebral artery (MCA) occlusion by intraluminal suture blockade followed by 1, 4 and 24 h of reperfusion. Immunohistochemistry showed that phospho-ERK1/2 was markedly increased in the cortex within the MCA territory at 1 h of reperfusion, followed by a decrease at 24 h. In SOD1 Tg mice, phospho-ERK1/2 was prominently reduced compared with non-ischemic controls, shown by immunohistochemistry. Western blot analysis confirmed a significant decrease in phospho-ERK1/2 1 h after FCI in the ischemic cortex (P" @default.
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- W2048468692 date "2003-06-01" @default.
- W2048468692 modified "2023-09-27" @default.
- W2048468692 title "Attenuation of neuronal cell death by SOD1 is associated with extracellular signal-regulated kinase after transient focal cerebral ischemia in mice" @default.
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- W2048468692 doi "https://doi.org/10.1016/s0531-5131(03)00072-4" @default.
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