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Related Experiment Video

Updated: Dec 31, 2025

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

Alpha-synuclein oligomerization increases its effect on promoting NMDA receptor internalization.

Wenjiao Yu^1,2,3,4, Weiwei Yang^1,2,3,4, Xuran Li^1,2,3,4

¹Department of Neurobiology, Xuanwu Hospital of Capital Medical University Beijing, China.

International Journal of Clinical and Experimental Pathology

|January 15, 2020

Summary

This summary is machine-generated.

Parkinson

Keywords:

NMDA receptor endocytosis parkinson’s disease plasma α-synuclein

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Area of Science:

Neuroscience
Cell Biology
Biochemistry

Background:

Alpha-synuclein (α-syn) monomers promote NMDA receptor (NMDAR) internalization.
Oligomeric α-syn, particularly in Parkinson's disease (PD) plasma, may have distinct effects on NMDAR regulation.
Investigating α-syn oligomers' role in NMDAR trafficking is crucial for understanding PD pathogenesis.

Purpose of the Study:

To investigate the effect of different α-syn oligomers on NMDAR internalization in dopaminergic cells.
To compare the potency of α-syn monomers versus oligomers in regulating GluN1 subunit surface expression.
To elucidate the mechanism underlying α-syn-induced NMDAR internalization.

Main Methods:

Preparation of α-syn monomers and oligomers (in PBS, normal control plasma, PD plasma).
Treatment of MES23.5 dopaminergic cells with α-syn species and assessment of NMDAR subunit (GluN1) internalization.
Measurement of Rab5B expression and evaluation of clathrin-mediated endocytosis using pitstop2.

Main Results:

Both α-syn monomers and oligomers entered dopaminergic cells and increased Rab5B expression.
α-syn oligomers, especially those from PD plasma, significantly reduced surface GluN1 levels, indicating internalization.
Oligomer-induced GluN1 internalization was dependent on clathrin-mediated endocytosis.

Conclusions:

α-syn oligomers, particularly those formed in PD plasma, enhance NMDAR GluN1 subunit internalization.
This enhanced internalization is mediated by a clathrin-dependent endocytic pathway.
Findings suggest a novel mechanism by which aggregated α-syn contributes to NMDAR dysfunction in Parkinson's disease.