Topic: synaptosomes

Pathological protein aggregation and synaptic dysfunction are major contributors to neurodegenerative disorders. However, understanding disease-relevant protein aggregation, such as Beta-amyloid, Alpha-synuclein and Tau aggregation within synapses, remains limited. To address this, we present a novel method for visualizing protein aggregates in individual synaptosomes. We combined Single-molecule Pull Down (SiMPull) and direct Stochastic Optical Reconstruction Microscopy (dSTORM), to immobilize individual synaptosomes and characterize single aggregates within them with ~20nm spatial resolution

Ellagic acid (EA) is a polyphenol that contributes to the nutraceutical properties of pomegranate. In the brain it was reported to control noradrenaline release. Recently, we demonstrated that EA binds α2 receptors (α2R), mimicking the full-agonist clonidine. The study was extended to Urolithins (URO) A, B and C which represent the main metabolites of EA in mammals, following a chronic (14 days) administration of an EA micro-formulation (EAm).“In vitro” studies were carried out on cortical and hippocampal synaptosomes isolated from control mice acutely exposed to the UROs, clonidine and yohimb

Complement recently identified as a “synaptic organizer” in the central nervous system (CNS). Specifically, it emerged that, beside dictating synapse remodelling during development and in neurodegenerative processes, complement also modulates glutamate release from cortical presynaptic terminals (synaptosomes) and astrocytic processes (gliosomes), controlling excitatory transmission and synaptic strength in this brain region. In both particles, the complement-evoked glutamate release relied on glutamate transporters (EAAT1 and 2) working in the reverse mode.We extended our study to synaptosome