NADPH oxidase mediates β-amyloid peptide-induced activation of ERK in hippocampal organotypic cultures
<p>Abstract</p> <p>Background</p> <p>Previous studies have shown that beta amyloid (Aβ) peptide triggers the activation of several signal transduction cascades in the hippocampus, including the extracellular signal-regulated kinase (ERK) cascade. In this study we sought...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
BMC
2009-10-01
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| Series: | Molecular Brain |
| Online Access: | http://www.molecularbrain.com/content/2/1/31 |
| Summary: | <p>Abstract</p> <p>Background</p> <p>Previous studies have shown that beta amyloid (Aβ) peptide triggers the activation of several signal transduction cascades in the hippocampus, including the extracellular signal-regulated kinase (ERK) cascade. In this study we sought to characterize the cellular localization of phosphorylated, active ERK in organotypic hippocampal cultures after acute exposure to either Aβ (1-42) or nicotine.</p> <p>Results</p> <p>We observed that Aβ and nicotine increased the levels of active ERK in distinct cellular localizations. We also examined whether phospho-ERK was regulated by redox signaling mechanisms and found that increases in active ERK induced by Aβ and nicotine were blocked by inhibitors of NADPH oxidase.</p> <p>Conclusion</p> <p>Our findings indicate that NADPH oxidase-dependent redox signaling is required for Aβ-induced activation of ERK, and suggest a similar mechanism may occur during early stages of Alzheimer's disease.</p> |
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| ISSN: | 1756-6606 |