Characterization of NO-sensitive guanylyl cyclase: expression in an identified interneuron involved in NO–cGMP-dependent memory formation
Riberio, Maria, Straub, Volko A., Schofield, Michael, Picot, Jo, Benjamin, Paul R., O'Shea, Michael and Korneev, Sergei A. (2008) Characterization of NO-sensitive guanylyl cyclase: expression in an identified interneuron involved in NO–cGMP-dependent memory formation. European Journal of Neuroscience, 28, (6), 1157-1165. (doi:10.1111/j.1460-9568.2008.06416.x).
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In a number of neuronal models of learning signalling by endogenous nitric oxide (NO), produced by the enzyme NO synthase (NOS), is essential for the formation of long-term memory (LTM). For example, in the molluscan model system Lymnaea, NO is required for LTM formation in the first few hours after one-trial reward conditioning. Furthermore, conditioning leads to transient up-regulation of the NOS gene in identified modulatory neurons, the cerebral giant cells (CGCs), which are known to be involved in LTM formation. In Lymnaea nothing is known however about the structure and localization of the major receptor for NO, the soluble guanylyl cyclase (sGC). Here we report on the cloning and characterization of both α and β subunits of NO-sensitive sGC and show that they are coexpressed in the CGCs. Furthermore, our electrophysiological experiments on isolated CGCs show that these neurons respond to NO by generating a prolonged depolarization of the membrane potential. Moreover, we demonstrate that this depolarization is blocked by ODQ, supporting our hypothesis that it is mediated by sGC.
|Keywords:||cerebral giant cell , identified neuron , Lymnaea , mollusc , nitric oxide|
|Subjects:||R Medicine > R Medicine (General)
R Medicine > RZ Other systems of medicine
R Medicine > RC Internal medicine > RC0321 Neuroscience. Biological psychiatry. Neuropsychiatry
|Divisions:||University Structure - Pre August 2011 > School of Medicine
|Date Deposited:||25 Feb 2010|
|Last Modified:||27 Mar 2014 18:52|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
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