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α‐Synuclein involvement in hippocampal synaptic plasticity: role of NO, cGMP, cGK and CaMKII
Author(s) -
Liu Shumin,
Fa Mauro,
Ninan Ipe,
Trinchese Fabrizio,
Dauer William,
Arancio Ottavio
Publication year - 2007
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.1460-9568.2007.05569.x
Subject(s) - cgmp dependent protein kinase , synaptic plasticity , protein kinase a , microbiology and biotechnology , calmodulin , soluble guanylyl cyclase , biology , chemistry , kinase , biochemistry , receptor , mitogen activated protein kinase kinase , guanylate cyclase , enzyme
Synaptic plasticity involves a series of coordinate changes occurring both pre‐ and postsynaptically, of which α‐synuclein is an integral part. We have investigated on mouse primary hippocampal neurons in culture whether redistribution of α‐synuclein during plasticity involves retrograde signaling activation through nitric oxide (NO), cGMP, cGMP‐dependent protein kinase (cGK) and calmodulin‐dependent protein kinase II. We have found that deletion of the α‐synuclein gene blocks both the long‐lasting enhancement of evoked and miniature transmitter release and the increase in the number of functional presynaptic boutons evoked through the NO donor, DEA/NO, and the cGMP analog, 8‐Br‐cGMP. In agreement with these findings both DEA/NO and 8‐Br‐cGMP were capable of producing a long‐lasting increase in number of clusters for α‐synuclein through activation of soluble guanylyl cyclase, cGK and calcium/calmodulin‐dependent protein kinase IIα. Thus, our results suggest that NO, cGMP, GMP‐dependent protein kinase and calmodulin‐dependent protein kinase II play a key role in the redistribution of α‐synuclein during plasticity.