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

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

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

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
Volume2
Issue number1
DOIs
StatePublished - Nov 2 2009

Fingerprint

NADPH Oxidase
Extracellular Signal-Regulated MAP Kinases
Amyloid
Peptides
Nicotine
Oxidation-Reduction
Amyloid beta-Peptides
Signal Transduction
Hippocampus
Alzheimer Disease

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience

Cite this

Serrano, F., Chang, A., Hernandez, C. M., Pautler, R. G., Sweatt, J. D., & Klann, E. (2009). NADPH oxidase mediates -amyloid peptide-induced activation of ERK in hippocampal organotypic cultures. Molecular brain, 2(1), [31]. https://doi.org/10.1186/1756-6606-2-31

NADPH oxidase mediates -amyloid peptide-induced activation of ERK in hippocampal organotypic cultures. / Serrano, Faridis; Chang, Angela; Hernandez, Caterina M.; Pautler, Robia G.; Sweatt, J. David; Klann, Eric.

In: Molecular brain, Vol. 2, No. 1, 31, 02.11.2009.

Research output: Contribution to journalArticle

Serrano, F, Chang, A, Hernandez, CM, Pautler, RG, Sweatt, JD & Klann, E 2009, 'NADPH oxidase mediates -amyloid peptide-induced activation of ERK in hippocampal organotypic cultures', Molecular brain, vol. 2, no. 1, 31. https://doi.org/10.1186/1756-6606-2-31
Serrano, Faridis ; Chang, Angela ; Hernandez, Caterina M. ; Pautler, Robia G. ; Sweatt, J. David ; Klann, Eric. / NADPH oxidase mediates -amyloid peptide-induced activation of ERK in hippocampal organotypic cultures. In: Molecular brain. 2009 ; Vol. 2, No. 1.
@article{26040614a85148728b4edeb9d916913f,
title = "NADPH oxidase mediates -amyloid peptide-induced activation of ERK in hippocampal organotypic cultures",
abstract = "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.",
author = "Faridis Serrano and Angela Chang and Hernandez, {Caterina M.} and Pautler, {Robia G.} and Sweatt, {J. David} and Eric Klann",
year = "2009",
month = "11",
day = "2",
doi = "10.1186/1756-6606-2-31",
language = "English (US)",
volume = "2",
journal = "Molecular Brain",
issn = "1756-6606",
publisher = "BioMed Central",
number = "1",

}

TY - JOUR

T1 - NADPH oxidase mediates -amyloid peptide-induced activation of ERK in hippocampal organotypic cultures

AU - Serrano, Faridis

AU - Chang, Angela

AU - Hernandez, Caterina M.

AU - Pautler, Robia G.

AU - Sweatt, J. David

AU - Klann, Eric

PY - 2009/11/2

Y1 - 2009/11/2

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=70350365853&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=70350365853&partnerID=8YFLogxK

U2 - 10.1186/1756-6606-2-31

DO - 10.1186/1756-6606-2-31

M3 - Article

VL - 2

JO - Molecular Brain

JF - Molecular Brain

SN - 1756-6606

IS - 1

M1 - 31

ER -