The Journal of Neuroscience, February 25, 2004, ():
Clearance of 
-Synuclein Oligomeric Intermediates via the Lysosomal Degradation Pathway
J. Neurosci. Lee et al.
24: 1888
Supplemental data
Figure 1. Microscopic characterization of -syn aggregates in differentiated SH-SY5Y cells. A, Small punctate aggregates (arrows). These aggregates were demonstrated to be oligomeric intermediates of fibrillar inclusion bodies. B, Mature fibrillar inclusion bodies (arrowheads). The strong thioflavin S fluorescence of the large pericentriolar inclusion bodies indicates that the inclusion bodies contain -sheet-rich fibrils; in contrast, the small oligomeric intermediates fail to interact with this dye. The large inclusion bodies also contain other protein components, such as ubiquitin, hsp70, and the 20S proteasome -subunit, whereas none of these proteins is consistently present in small oligomers. Nuclei were stained with Hoechst 33258 (blue). ThioS, Thioflavin S; ubiq, ubiquitin; 20S, -subunit of the 20S proteasome.
Files in this Data Supplement:
- Supplementary Fig. 1
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Figure 1. Microscopic characterization of -syn aggregates in differentiated SH-SY5Y cells. A, Small punctate aggregates (arrows). These aggregates were demonstrated to be oligomeric intermediates of fibrillar inclusion bodies. B, Mature fibrillar inclusion bodies (arrowheads). The strong thioflavin S fluorescence of the large pericentriolar inclusion bodies indicates that the inclusion bodies contain -sheet-rich fibrils; in contrast, the small oligomeric intermediates fail to interact with this dye. The large inclusion bodies also contain other protein components, such as ubiquitin, hsp70, and the 20S proteasome -subunit, whereas none of these proteins is consistently present in small oligomers. Nuclei were stained with Hoechst 33258 (blue). ThioS, Thioflavin S; ubiq, ubiquitin; 20S, -subunit of the 20S proteasome.
