Fig. 5: EV-induced proteolysis of human α-syn PFFs produces species that do not aid the aggregation of endogenous α-syn.
From: Proteolytic activities of extracellular vesicles attenuate A-synuclein aggregation
Primary cortical neurons (5div) were treated for 72 h with hPFFs, hPFFs pre-incubated with EVs (Exo) in the presence or absence of protease inhibitors (PIs), as well as EVs alone. Similar incubations were used with monomeric α-syn (mono). Untreated cells were used as control (CTR). A Immunoblotting for α-syn with the Syn-1 antibody revealed that EV association of PFFs produces fragments that do not augment α-syn aggregation. Beta-actin was used as loading control. B Immunoblotting for α-syn with the C-20 confirmed the inability of the EV-degraded PFFs to seed the aggregation of α-syn in neuronal cultures. GAPDH was used as loading control.
