Neuroscience 2001 Abstract
| Presentation Number: | 206.18 |
|---|---|
| Abstract Title: | ACTIVATION OF ERK2 BY REOXYGENATION FOLLOWING OXYGEN DEPRIVATION IN MOUSE PRIMARY CULTURED CORTICAL NEURONS. |
| Authors: |
Namura, S.*1,2
; Iihara, K.2
; Nagata, I.2
1Stroke & Brain Protection Lab, Res Inst Nat'l Cardiovascular Ctr, Suita, Japan 2Dept. of Neurosurgery, Nat'l Cardiovascular Ctr, Suita, Japan |
| Primary Theme and Topics |
Neurological and Psychiatric Conditions - Ischemia -- Cellular and molecular mechanisms |
| Secondary Theme and Topics | Neurological and Psychiatric Conditions<br />- Ischemia<br />-- Neuroprotection and tolerance |
| Session: |
206. Ischemia: cellular and molecular mechanisms V Poster |
| Presentation Time: | Sunday, November 11, 2001 2:00 PM-3:00 PM |
| Location: | Exhibit Hall WW-21 |
| Keywords: | MAP KINASE, HYPOXIA, NEUROPROTECTION, OXIDATIVE STRESS |
We previously reported that intraventricular administration of MEK1 inhibitor PD98059 decreases infarct volume after 2 hr of middle cerebral artery occlusion (MCAO) in mice (Proc Natl Acad Sci USA 96:12866–12869, 1999). Moreover, we found that delayed intravenous systemic administration of another MEK inhibitor U0126 during ischemia reduces infarct volume resulting from 3 hr of MCAO in mice (SFN Abstract Part1:286.13, 2000). In the present study, we investigated the role of MEK/ERK pathway in neuronal death induced by 9 hr of oxygen deprivation (OD) by which 70–80% of neurons die at 24 hr after reoxygenation (RO). Nine hour of OD reduced phosphorylation level of ERK2. Two hour of RO following 9 hr of OD increased phosphorylated ERK1/2. Incubation with U0126 inhibited phosphorylation of ERK2 at 0–3 hr after RO in a dose-dependent manner, which was correlated with neuroprotection. The neuroprotection by U0126 was dose-dependent, and maximum protection was achieved at 10 µM. However, U0126 did not reduce the phosphorylation levels of MEK1/2. Rather, U0126 increased the phosphorylation levels of MEK1/2. At concentrations up to 10 µM, U0126 did not affect phosphorylation levels in p38 MAPK, JNK, and p70S6 kinase. Our results indicate that reoxygenation following oxygen deprivation activates ERK2, which may mediate neuronal injury induced by oxidative stress.
Supported by Special Coordiantion Funds for Promoting Science and Technology, STA, Japan (S.N. and I.N.), and Japan Research Foundation for Clinical Pharmacology (S.N.)
Sample Citation:
[Authors]. [Abstract Title]. Program No. XXX.XX. 2001 Neuroscience Meeting Planner. San Diego, CA: Society for Neuroscience, 2001. Online.
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