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. 2012 Aug 22;32(34):11750–11762. doi: 10.1523/JNEUROSCI.0234-12.2012

Figure 1.

Figure 1.

Characterization of a-syn species and biological effects. a, SDS-PAGE separation of the different a-syn species (monomers, oligomers, HNE-oligomers, and fibrils). Monomers migrate with monomeric molecular weight (15 kDa) whereas a-syn oligomers, a-syn HNE-oligomers, and fibrils display SDS-resistant high molecular weight species. b, Thioflavin T normalized fluorescence assay in the presence of the different a-syn species with excitation and emission wavelengths of 450 and 490 nm, respectively. The a-syn oligomers, a-syn HNE-oligomers, and fibrils interacted with Thioflavin T, suggesting that they display an increased β-sheet structure, typical of oligomeric and fibrillary species. c, AFM analysis of the different a-syn species. No detectable species are shown for monomers; a-syn oligomers and a-syn HNE-oligomers appeared as a heterogeneous population with globular and protofibrillar structures; fibrils displayed fibrillary structures. Scale bar, 500 nm. d, Cytotoxicity of a-syn species in SH-SY5Y cells. LDH activity of SH-SY5Y cells incubated with different a-syn species. LDH release was expressed as relative levels of nontreated (Ctrl) samples. Data are expressed as mean ± SD, n = 3. e, To control a possible overexposure to a-syn we performed immunoblot analysis comparing endogenous a-syn to that from hippocampal slices treated with a-syn oligomers (500 nm; 90 min). We detected an increment of ∼15% incorporation in the slices exposed to exogenous a-syn.