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Topic: GluN3A

ePoster
3 ePosters

In Neuroscience

Modified synaptic and extrasynaptic distribution of NMDA receptors in cortex of Alzheimer’s disease individuals

Inmaculada Cuchillo-Ibañez, Sergio Escamilla, Javier Sáez-Valero · FENS Forum 2024

We have developed a protocol to isolate synaptic and extrasynaptic membranes from post-mortem human cortex. This allowed us to characterize the distribution of the major brain NMDAR subunits, GluN2B, GluN2A, GluN1 and GluN3A in controls and AD samples. We used specific antibodies and western blots to analyse the level and phosphorylation of the NMDAR subunits. We have found that GluN2B, GluN2A, GluN1 are predominantly at synaptic membranes, while GluN3A is more abundant at extrasynaptic membranes. When the synaptic distribution was analysed in AD fractions, GluN2B and GluN2A showed lower level

ePoster · Neuroscience

Myelin plasticity requires the expression in oligodendrocyte progenitors of NMDA receptors containing GluN3A subunits

Moumita Chatterjee, Alice Staffa, Ana Isabel Navarro Navarro, Ariadna Diaz-Tahoces, Carlos Parras, J. C. Chara Ventura, Carlos Matute, Isabel Perez Otano · FENS Forum 2024

Work over the last decade demonstrates that the myelin sheaths enwrapping axons, classically seen as static insulators, are highly dynamic and respond to axonal activity and experience. This phenomenon, called “myelin plasticity”, goes beyond postnatal stages into adulthood and plays a key role in remodeling neuronal circuits to support adaptive behavior or functional recovery upon injury. Yet the mechanisms are unknown. Here we show that NMDA receptors containing GluN3A subunits are expressed by oligodendrocyte progenitor cells (OPCs) and essentially required for activity-dependent myelin pla

ePoster · Neuroscience

AIMS: Investigate the impact of disrupting specific disulfide bonds in the GluN1 subunit on the early trafficking and functional properties of unconventional NMDARs.METHODS:HEK293 cells and rat hippocampal neurons were used to express wild-type (WT) or mutant forms of GluN1/GluN3A receptors. Surface expression and colocalization of NMDARs with the Golgi apparatus (GA) were observed using fluorescence confocal microscopy. Electrophysiological properties of NMDARs were assessed via patch-clamp technique.RESULTS:Disrupting disulfide bonds in the GluN1 subunit co-transfected with GluN3A subunit le

ePoster · Neuroscience