NADPH oxidase mediates -amyloid peptide-induced activation of ERK in hippocampal organotypic cultures

Faridis Serrano, Angela Chang, Caterina Hernandez, Robia G. Pautler, J. David Sweatt, Eric Klann

Research output: Contribution to journalArticlepeer-review


Background: Previous studies have shown that beta amyloid (A) 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 A (1-42) or nicotine. Results. We observed that A 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 A and nicotine were blocked by inhibitors of NADPH oxidase. Conclusion. Our findings indicate that NADPH oxidase-dependent redox signaling is required for A-induced activation of ERK, and suggest a similar mechanism may occur during early stages of Alzheimer's disease.

Original languageEnglish (US)
Article number31
JournalMolecular Brain
Issue number1
StatePublished - 2009

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience


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