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Open Access

PDE2, a component of the NO/cGMP signalling in the hippocampus

  • Isabel Schönle1Email author,
  • Angela Neitz2,
  • Thomas Mittmann2,
  • Doris Koesling1 and
  • Evanthia Mergia1
BMC Pharmacology201111(Suppl 1):P63

Published: 1 August 2011


Synaptic PlasticityPhosphodiesteraseHippocampal SliceGlutamate ReleasePDE2 Inhibition


NO/cGMP-mediated signal transduction is involved in synaptic plasticity in various brain regions. NO effects are transduced by the NO receptor guanylyl cyclase (NO-GC) that exists in two isoforms, NO-GC1 and NO-GC2, with indistinguishable regulatory properties. Mice deficient in either NO-GC1 or NO-GC2 revealed that both NO-GC isoforms are required for LTP indicating the existence of two separated NO/cGMP pathways. Recently, we demonstrated a presynaptic role of NO/cGMP in facilitation of glutamate release and indentified eNOS and NO-GC1 as the participating enzymes. Yet, the involved cGMP-hydrolysing phosphodiesterases (PDE) remained unknown.


Here we demonstrate that PDE2 accounts for 50% of cGMP-hydrolysing activity in hippocampal homogenates. In hippocampal slices of WT, NO-GC1 and NO-GC2 KO mice, PDE2 inhibition increased NMDA-induced cGMP levels.


This suggests PDE2 as a component of both NO-GC1- and NO-GC2-mediated signalling pathways. Moreover we analyzed the physiological role of the PDE2 on glutamatergic transmission in the hippocampal CA1 region by single-cell recordings in acute slices.

Authors’ Affiliations

Institute of Pharmacology, Medical School, Ruhr-University Bochum, Bochum, Germany
Institute of Physiol. & Pathophysiol, Univ. Med.-Center of the Joh.-Gutenberg-Univ. Mainz, Germany


© Schönle et al; licensee BioMed Central Ltd. 2011

This article is published under license to BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.