Does exogenous AS contribute to endogenous AS? Or is AS, when ingested via dietary consumption denatured or changed in some way making this not an issue?
α-Syn undergoes various post-translational modifications, such as phosphorylation, truncation, ubiquitination, and nitration. Phosphorylation of α-Syn at the serine 129 residue is one of the major pathological markers of PD; 90% of α-Syn is phosphorylated in the brain of patients with PD while only 4% of α-Syn is phosphorylated in healthy brains (Oueslati, 2016; Ghosh et al., 2017). However, there is a great controversy over whether phosphorylation has an active role in the α-Syn aggregation or if it is a response mechanism of cells to try to label and eliminate toxic species of α-Syn (Oueslati, 2016). Smith et al. (2005) proposed that phosphorylation of α-Syn promotes the formation of cytoplasmic inclusions in some cell culture models (Smith et al., 2005). Nevertheless, Oueslati et al. (2013) show that phosphorylation of α-Syn induced by polo-like kinase 2 has no effect on the aggregation and regulates α-Syn clearance via the lysosomal autophagy pathway (Oueslati et al., 2013). Additional lines of evidence show crosstalk between phosphorylation and α-Syn degradation. The inhibition of the ubiquitin-proteasome system (Chau et al., 2009) or the autophagy-lysosomal pathway (Machiya et al., 2010) induced a significant increase in phosphorylated α-Syn in human neuroblastoma, suggesting that phosphorylation regulates the α-Syn degradation.
ncbi.nlm.nih.gov/pmc/articl...
I’m trying to understand the relationship between phosphorylation and proteolytic enzymes.
The Effect of Curcumin on Idiopathic Parkinson Disease: A Clinical and Skin Biopsy Study
Complex 1 inhibitors cause aggregation of a/syn and tau.
