Skip to main content
Fig. 5 | Molecular Brain

Fig. 5

From: Broad proteomics analysis of seeding-induced aggregation of α-synuclein in M83 neurons reveals remodeling of proteostasis mechanisms that might contribute to Parkinson’s disease pathogenesis

Fig. 5

Modulation of Larp1 affects α-syn aggregation in M83 primary neurons. A-B The effect of Larp1 knockdown was evaluated on α-syn aggregation in the M83 seeding model. A Shows representative images with non-targeting control siRNA and LARP1 siRNA treatment in M83 neurons stained with pS129 α-syn (green), MAP2 (purple) and nucleus with Hoechst (blue). Scale bars, 50 μm. and (B) shows quantification using high-content image analysis, which indicated that knockdown of Larp1 significantly increased PFF-induced pS129 α-syn aggregation. (N=6 replicates). Data are mean±SD. **p=0.0066 (t-test). C Quantification of PFF-induced endogenous mouse α-syn aggregation in CD1 neurons also suggested that that knockdown of Larp1 resulted in significant increase in aggregation compared to non-targeting control siRNA. (N=6 replicates). Data are mean±SD. ****p<0.0001 (t-test). D WES analysis with Triton X soluble and insoluble fractions isolated from M83 mice with either PBS or PFF treatment showed enrichment of Larp1 in the PBS-treated samples but less enrichment in the PFF treated samples

Back to article page

Molecular Brain

ISSN: 1756-6606