Synaptic localization of a functional NADPH oxidase in the mouse hippocampus

Maria V. Tejada-Simon, Faridis Serrano, Laura E. Villasana, Beatriz I. Kanterewicz, Gang Y. Wu, Mark T. Quinn, Eric Klann

Research output: Contribution to journalArticle

Abstract

Superoxide has been shown to be critical for hippocampal long-term potentiation (LTP) and hippocampus-dependent memory function. A possible source for the generation of superoxide during these processes is NADPH oxidase. The active oxidase consists of two membrane proteins, gp91phox and p22phox, and four cytosolic proteins, p40phox, p47 phox, p67phox, and Rac. Upon stimulation, the cytosolic proteins translocate to the membrane to form a complex with the membrane components, which results in production of superoxide. Here, we determined the presence, localization, and functionality of a NADPH oxidase in mouse hippocampus by examining the NADPH oxidase proteins as well as the production of superoxide. All of the NADPH oxidase proteins were present in hippocampal homogenates and enriched in synaptoneurosome preparations. Immunocytochemical analysis of cultured hippocampal neurons indicated that all NADPH oxidase proteins were localized in neuronal cell bodies as well as dendrites. Furthermore, double labeling analysis using antibodies to p67phox and the presynaptic marker synaptophysin suggest a close association of the NADPH oxidase subunits with synaptic sites. Finally, stimulation of hippocampal slices with phorbol esters triggered translocation of the cytoplasmic NADPH oxidase proteins to the membrane and an increase in superoxide production that was blocked by inhibitors of NADPH oxidase. Taken together, our data suggest that NADPH oxidase is present in mouse hippocampus and might be the source of superoxide production required for LTP and memory function.

Original languageEnglish (US)
Pages (from-to)97-106
Number of pages10
JournalMolecular and Cellular Neuroscience
Volume29
Issue number1
DOIs
StatePublished - May 2005

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NADPH Oxidase
Hippocampus
Superoxides
Long-Term Potentiation
Proteins
Membrane Proteins
Synaptophysin
Membranes
Long-Term Memory
Phorbol Esters
Dendrites
Oxidoreductases
Neurons
Antibodies

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience
  • Developmental Neuroscience

Cite this

Tejada-Simon, M. V., Serrano, F., Villasana, L. E., Kanterewicz, B. I., Wu, G. Y., Quinn, M. T., & Klann, E. (2005). Synaptic localization of a functional NADPH oxidase in the mouse hippocampus. Molecular and Cellular Neuroscience, 29(1), 97-106. https://doi.org/10.1016/j.mcn.2005.01.007

Synaptic localization of a functional NADPH oxidase in the mouse hippocampus. / Tejada-Simon, Maria V.; Serrano, Faridis; Villasana, Laura E.; Kanterewicz, Beatriz I.; Wu, Gang Y.; Quinn, Mark T.; Klann, Eric.

In: Molecular and Cellular Neuroscience, Vol. 29, No. 1, 05.2005, p. 97-106.

Research output: Contribution to journalArticle

Tejada-Simon, MV, Serrano, F, Villasana, LE, Kanterewicz, BI, Wu, GY, Quinn, MT & Klann, E 2005, 'Synaptic localization of a functional NADPH oxidase in the mouse hippocampus', Molecular and Cellular Neuroscience, vol. 29, no. 1, pp. 97-106. https://doi.org/10.1016/j.mcn.2005.01.007
Tejada-Simon MV, Serrano F, Villasana LE, Kanterewicz BI, Wu GY, Quinn MT et al. Synaptic localization of a functional NADPH oxidase in the mouse hippocampus. Molecular and Cellular Neuroscience. 2005 May;29(1):97-106. https://doi.org/10.1016/j.mcn.2005.01.007
Tejada-Simon, Maria V. ; Serrano, Faridis ; Villasana, Laura E. ; Kanterewicz, Beatriz I. ; Wu, Gang Y. ; Quinn, Mark T. ; Klann, Eric. / Synaptic localization of a functional NADPH oxidase in the mouse hippocampus. In: Molecular and Cellular Neuroscience. 2005 ; Vol. 29, No. 1. pp. 97-106.
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