Topic: glycosylation

Affective disorders, which can be categorized into depressive and bipolar disorders, represent a leading cause of disability worldwide. Despite their considerable prevalence, the intricate molecular and cellular mechanisms underlying these conditions remain elusive, mainly due to their complex etiologies and heterogeneous clinical presentations. Over the past years, the serotonergic system has emerged as a focal point in understanding the pathophysiological and therapeutic responses of affective disorders. Among the major regulators of this system, the serotonin transporter (SERT), which media

Midbrain dopamine (DA) neurons possess complex branching structures and demand significant metabolic resources . This intricate architecture makes these neuron susceptible, emphasizing the role of intracellular trafficking in the early development of Parkinson's disease (PD). Recent genetic screenings in Asian and European populations have unveiled SV2C (synaptic vesicle glycoprotein C) as a newly discovered gene associated with PD. Specifically, the D543N mutation has been linked to PD. It is hypothesized that this mutation introduces a new glycosylation site in the SV2C protein, underscoring

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