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Related Experiment Video

Updated: Jun 6, 2026

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

Raised calcium promotes α-synuclein aggregate formation.

S Nath¹, J Goodwin, Y Engelborghs

¹Biomolecular Dynamics, Katholieke Universiteit Leuven, Leuven, Belgium.

Molecular and Cellular Neurosciences

|December 15, 2010

Summary

This summary is machine-generated.

Calcium significantly accelerates alpha-synuclein aggregation, a key process in Parkinson's disease. This study shows calcium promotes alpha-synuclein clumping in vitro and in cells, highlighting calcium's role in disease pathology.

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A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

Published on: November 25, 2022

Area of Science:

Biochemistry
Neuroscience
Cell Biology

Background:

Parkinson's and Parkinson's-plus diseases are linked to abnormal alpha-synuclein protein aggregation.
The precise mechanisms driving alpha-synuclein aggregation are not fully understood.
Calcium ions are known to influence protein structure and function.

Purpose of the Study:

To investigate the effect of calcium on alpha-synuclein aggregation in vitro and in vivo.
To determine the role of calcium concentration and flux in promoting alpha-synuclein aggregation.
To explore the potential involvement of surface adsorption in calcium-dependent aggregation.

Main Methods:

In vitro studies using fluorescently labeled monomeric alpha-synuclein incubated with varying calcium concentrations.
Techniques employed: fluorescence microscopy, fluorescence correlation spectroscopy, and scanning electron microscopy.
Cell culture experiments using human 1321N1 cells expressing alpha-synuclein-GFP, with induced intracellular calcium increases.

Main Results:

Calcium accelerated alpha-synuclein aggregation on surfaces and in free solution in a dose-dependent manner.
Surface aggregates formed at low calcium concentrations (half-maximal at 80 μM), while soluble oligomers formed at higher concentrations (half-maximal at 180 μM).
Transient increases in intracellular calcium significantly enhanced cytoplasmic alpha-synuclein aggregation in cultured cells.

Conclusions:

Calcium is a potent accelerator of alpha-synuclein aggregation across different conditions (surface, solution, cellular).
Surface adsorption appears to be a significant factor in the calcium-dependent aggregation mechanism.
These findings provide crucial insights into the molecular mechanisms underlying Parkinson's disease pathogenesis.