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In vitro study on the pathological effects of polymorphic α-syn PFFs in <t>dopaminergic</t> neuronal cells. (A) Immunostaining of phosphorylated α-syn (pS129) tended to show varying levels of endogenous α-syn misfolding following treatments with conformationally distinct α-syn PFFs. Neuron- and Aged-membranes did not significantly affect pS129 accumulation. Scale bars, 20 μm. (B) Quantification of pS129 levels in response to distinct α-syn PFF conformations with or without membranes. (C) Immunofluorescence micrographs showing differential formation of intraneuronal α-syn aggregates in response to structurally distinct α-syn PFFs and lipid conditions. Insets show magnified views of α-syn puncta within dopaminergic neurons. Scale bars, 100 μm for main images and 25 μm for insets. (D) Cells treated with distinct α-syn PFFs exhibit differential activation and nuclear translocation of NF-κB. Scale bars, 20 μm. Data show mean ± SD with n = 3. *** P < 0.001, ** P < 0.01, * P < 0.05.
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In vitro study on the pathological effects of polymorphic α-syn PFFs in dopaminergic neuronal cells. (A) Immunostaining of phosphorylated α-syn (pS129) tended to show varying levels of endogenous α-syn misfolding following treatments with conformationally distinct α-syn PFFs. Neuron- and Aged-membranes did not significantly affect pS129 accumulation. Scale bars, 20 μm. (B) Quantification of pS129 levels in response to distinct α-syn PFF conformations with or without membranes. (C) Immunofluorescence micrographs showing differential formation of intraneuronal α-syn aggregates in response to structurally distinct α-syn PFFs and lipid conditions. Insets show magnified views of α-syn puncta within dopaminergic neurons. Scale bars, 100 μm for main images and 25 μm for insets. (D) Cells treated with distinct α-syn PFFs exhibit differential activation and nuclear translocation of NF-κB. Scale bars, 20 μm. Data show mean ± SD with n = 3. *** P < 0.001, ** P < 0.01, * P < 0.05.

Journal: ACS Chemical Neuroscience

Article Title: Lipid Acyl Chain-Driven α‑Synuclein Fibril Polymorphisms and Neuronal Pathologies

doi: 10.1021/acschemneuro.5c00730

Figure Lengend Snippet: In vitro study on the pathological effects of polymorphic α-syn PFFs in dopaminergic neuronal cells. (A) Immunostaining of phosphorylated α-syn (pS129) tended to show varying levels of endogenous α-syn misfolding following treatments with conformationally distinct α-syn PFFs. Neuron- and Aged-membranes did not significantly affect pS129 accumulation. Scale bars, 20 μm. (B) Quantification of pS129 levels in response to distinct α-syn PFF conformations with or without membranes. (C) Immunofluorescence micrographs showing differential formation of intraneuronal α-syn aggregates in response to structurally distinct α-syn PFFs and lipid conditions. Insets show magnified views of α-syn puncta within dopaminergic neurons. Scale bars, 100 μm for main images and 25 μm for insets. (D) Cells treated with distinct α-syn PFFs exhibit differential activation and nuclear translocation of NF-κB. Scale bars, 20 μm. Data show mean ± SD with n = 3. *** P < 0.001, ** P < 0.01, * P < 0.05.

Article Snippet: For immunostaining, dopaminergic neuronal cells were fixed with 4% paraformaldehyde (AR1068, Boster) for 30 min at RT and washed twice using DPBS.

Techniques: In Vitro, Immunostaining, Immunofluorescence, Activation Assay, Translocation Assay