NDLI: Interference of α-Synuclein Uptake by Monomeric β-Amyloid$_{1–40}$ and Potential Core Acting Site of the Interference

Content Provider	Springer Nature Link
Author	Chan, Daniel K. Y. Braidy, Nady Xu, Ying Hua Chataway, Tim Guo, Feng Guillemin, Gilles J. Teo, Charlie Gai, Wei Ping
Copyright Year	2016
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-Amyloid$_{1–40}$ (Aβ$_{40}$) 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 Aβ$_{40}$, but not β-Amyloid$_{1–42}$ (Aβ$_{42}$) as compared to controls. This finding was further confirmed by enzyme-linked immunosorbent assay (ELISA) with α-Syn uptake reduced from about 80 % (Aβ$_{42}$) to about 20 % (Aβ$_{40}$) relative to controls. To define the region of Aβ$_{40}$ 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 Aβ$_{40}$ and that the core acting site of interference might lie between amino acid residue positions 12–36.
Starting Page	479
Ending Page	485
Page Count	7
File Format	PDF
ISSN	10298428
Journal	Neurotoxicity Research
Volume Number	30
Issue Number	3
e-ISSN	14763524
Language	English
Publisher	Springer US
Publisher Date	2016-06-30
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	α-synuclein β-amyloid$_{1–40}$ β-amyloid$_{1–42}$ α-synuclein uptake Interference Neurosciences Neurology Neurochemistry Pharmacology/Toxicology Neurobiology Cell Biology
Content Type	Text
Resource Type	Article
Subject	Neuroscience Toxicology

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