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Related Experiment Video

Updated: Jun 5, 2026

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

Alpha-synuclein is a cellular ferrireductase.

Paul Davies¹, Dima Moualla, David R Brown

¹Department of Biology and Biochemistry, University of Bath, Bath, United Kingdom.

|January 21, 2011

Summary

This summary is machine-generated.

Alpha-synuclein (αS) acts as a ferrireductase, converting iron (III) to iron (II). This newly discovered function of αS may offer therapeutic targets for neurodegenerative diseases like Parkinson's disease.

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Last Updated: Jun 5, 2026

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Published on: January 5, 2016

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

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Published on: November 25, 2022

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

Area of Science:

Biochemistry
Neuroscience
Molecular Biology

Background:

Alpha-synuclein (αS) is implicated in Parkinson's disease and Lewy body dementias.
The physiological function of normal αS remains unclear despite its disease association.

Purpose of the Study:

To elucidate the physiological function of alpha-synuclein (αS).
To investigate the role of αS in cellular iron metabolism.

Main Methods:

Enzyme kinetics assays were performed on recombinant αS.
αS ferrireductase activity was measured in neuronal cell lysates.
Cellular iron (II) levels were quantified following αS overexpression.

Main Results:

Recombinant αS demonstrated ferrireductase activity with Vmax of 2.72 nmols/min/mg and Km of 23 µM.
αS activity requires copper as a cofactor and NADH as an electron donor.
Overexpression of αS increased intracellular iron (II) levels; disease mutations did not alter activity.

Conclusions:

Alpha-synuclein (αS) functions as a cellular ferrireductase, regulating iron bioavailability.
This ferrireductase activity of αS presents potential therapeutic targets for Parkinson's disease and related dementias.