Interference of α-Synuclein Uptake by Monomeric β-Amyloid1–40 and Potential Core Acting Site of the Interference View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-06-30

AUTHORS

Daniel K. Y. Chan, Nady Braidy, Ying Hua Xu, Tim Chataway, Feng Guo, Gilles J. Guillemin, Charlie Teo, Wei Ping Gai

ABSTRACT

Increasing evidence suggests an important role of alpha-synuclein (α-Syn) in the pathogenesis of Parkinson’s disease (PD). The inter-neuronal spread of α-Syn via exocytosis and endocytosis has been proposed as an explanation for the neuropathological findings of PD in sub-clinical and clinical phases. Therefore, interfering the uptake of α-Syn by neurons may be an important step in slowing or modifying the propagation of the disease. The purposes of our study were to investigate if the uptake of α-Syn fibrils can be specifically interfered with monomeric β-Amyloid1–40 (Aβ40) and to characterise the core acting site of interference. Using a radioisotope-labelled uptake assay, we found an 80 % uptake reduction of α-Syn fibrils in neurons interfered with monomeric Aβ40, but not β-Amyloid1–42 (Aβ42) as compared to controls. This finding was further confirmed by enzyme-linked immunosorbent assay (ELISA) with α-Syn uptake reduced from about 80 % (Aβ42) to about 20 % (Aβ40) relative to controls. To define the region of Aβ40 peptide capable of the interference, we explored shorter peptides with less amino acid residues from both the C-terminus and N-terminus. We found that the interference effect was preserved if amino acid residue was trimmed to position 11 (from N-terminus) and 36 (from C-terminus), but dropped off significantly if residues were trimmed beyond these positions. We therefore deduced that the “core acting site” lies between amino acid residue positions 12–36. These findings suggest α-Syn uptake can be interfered with monomeric Aβ40 and that the core acting site of interference might lie between amino acid residue positions 12–36. More... »

PAGES

479-485

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12640-016-9644-2

DOI

http://dx.doi.org/10.1007/s12640-016-9644-2

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1004248128

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27364697


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