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Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

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α-Synuclein arginylation in the human brain.

Jun Zhao¹, Buyan Pan², Marie Fina¹

¹Department of Biomedical Sciences, University of Pennsylvania School of Veterinary Medicine, Philadelphia, Pennsylvania, 19104, USA.

Translational Neurodegeneration

|April 9, 2022

Summary

Alpha-synuclein (α-syn) arginylation occurs in the human brain at sites linked to neurodegenerative disease. This modification appears to be a protective mechanism against α-syn aggregation and neurodegeneration.

Keywords:

Aging Arginylation Neurodegeneration α-Synuclein

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Published on: August 16, 2020

Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Alpha-synuclein (α-syn) misfolding is central to neurodegenerative disorders.
Previous studies identified α-syn arginylation in mouse brains, with its absence linked to neurodegeneration.

Purpose of the Study:

To investigate α-syn arginylation in human brain pathology.
To explore the functional consequences of α-syn arginylation in neurons.

Main Methods:

Development of novel antibodies for detecting arginylated α-syn.
Utilized Western blotting, biochemical assays, and live neuron experiments.
Analyzed human brain tissue samples.

Main Results:

Identified α-syn arginylation at E46 and E83 in the human brain, sites relevant to Parkinson's disease.
Arginylation levels varied (3-50%) and were concentrated in specific subcellular fractions.
Arginylated α-syn showed reduced S129 phosphorylation and aggregation in neurons.
Arginylation levels inversely correlated with total α-syn and patient age.

Conclusions:

α-syn arginylation may serve as a neuroprotective mechanism.
This modification could prevent abnormal α-syn accumulation during aging and neurodegeneration.