Oxidative stress-induced phosphorylation, degradation and aggregation of α-synuclein are linked to upregulated CK2 and cathepsin D
Version of Record online: 15 AUG 2007
European Journal of Neuroscience
Volume 26, Issue 4, pages 863–874, August 2007
How to Cite
Takahashi, M., Ko, L.-w., Kulathingal, J., Jiang, P., Sevlever, D. and Yen, S.-H. C. (2007), Oxidative stress-induced phosphorylation, degradation and aggregation of α-synuclein are linked to upregulated CK2 and cathepsin D. European Journal of Neuroscience, 26: 863–874. doi: 10.1111/j.1460-9568.2007.05736.x
- Issue online: 15 AUG 2007
- Version of Record online: 15 AUG 2007
- Received 2 April 2007, revised 28 June 2007, accepted 2 July 2007
Fig. S1. FeCl2 treatment inhibits proteasomes. (A) Immunoblotting of cell lysates with anti-ubiquitin antibody (Mab 1510, Chemicon). FeCl2-treated samples displayed more high-molecular-weight (HMW) proteins with ubiquitin (ubiq) immunoreactivities. The arrow indicates ubiquitin monomer. (B) Quantitative analysis of ubiquitin-immunoreactive proteins of molecular weight > 75 kDa. Student?s t-test, N = 6, *P < 0.05. (C) Proteasomal activity assay using fluorogenic peptides as substrate. Chymotrypsine-like activity was lower in Fe(+) than Fe(?) controls, and higher in Syn(+) than Syn(?) cells without the FeCl2 treatment, N = 6, *P < 0.05. The specificity of activity assay was verified by analysis of lysates in the presence of the proteasome inhibitor, epoxomicin.
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