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. 2015 Jan 24;10(1):e0116641. doi: 10.1371/journal.pone.0116641

Figure 1. Glycosaminoglycans modulation of α-synuclein aggregation and degradation by cathepsin D in vitro.

Figure 1

a) In vitro α-synuclein aggregation in the presence of different GAGs. Commercial α-synuclein (25 μg/mL) was incubated 24 h at 37°C in the presence of 1, 10 or 100 μg/mL of commercial Hep, CS or HS. Monomeric, dimeric and oligomeric forms of α-synuclein were detected by western blot and quantified with ImageJ software. b)Inhibition of cathD degradation of α-synuclein by different commercial GAGs. α-synuclein was incubated in the presence of cathD (50 mU/mL) and pepstatin A, Hep, HS or CS (100 μg/mL) during 30 min at 37°C. Residual α-synuclein was detected by western blot and quantified with ImageJ software. Results are presented as the mean ± S.E.M. *** p<0.01 compared to control.