a-syn

1
Supplementary Figure 1
A
B
merge
merge
a-syn
a-syn
ThioS
ThioS
a-syn
ubiq
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ubiq
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a-syn
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a-syn
a-syn
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hsp70
hsp70
a-syn
a-syn
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20s
20s
Fig. 1. Microscopic characterization of a-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 b-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 a-subunit, while none of these
proteins are consistently present in small
oligomers. Nuclei were stained with Hoechst 33258
(blue). ThioS thioflavin S, ubiq ubiquitin,
20s a-subunit of the 20S proteasome