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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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The Down-Regulation of Clusterin Expression Enhances the αSynuclein Aggregation Process.

Chiara Lenzi¹, Ileana Ramazzina^1,2,3, Isabella Russo^4,5

¹Department of Medicine and Surgery, University of Parma, Via Gramsci 14, 43126 Parma, Italy.

International Journal of Molecular Sciences

|October 2, 2020

Summary

Clusterin (CLU) counteracts alpha-synuclein (αSyn) aggregation in Parkinson's Disease (PD). CLU interacts with αSyn and its reduction increases αSyn aggregates, highlighting its role in cellular response to PD pathology.

Keywords:

chaperone clusterin gene expression heat shock protein neurodegeneration protein aggregation proteostasis αSynuclein

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Published on: June 26, 2018

Area of Science:

Neuroscience
Molecular Biology
Cell Biology

Background:

Parkinson's Disease (PD) involves alpha-synuclein (αSyn) aggregation in neurons.
Molecular chaperones, like Clusterin (CLU), manage protein homeostasis and can mitigate toxic aggregation.
CLU's role in PD pathogenesis remains largely unexplored, despite its known function in Alzheimer's Disease.

Purpose of the Study:

To investigate the role of Clusterin (CLU) in the aggregation of alpha-synuclein (αSyn) in Parkinson's Disease models.
To determine if CLU expression is altered in response to αSyn overexpression.
To elucidate the functional significance of CLU in αSyn aggregation and cellular response.

Main Methods:

Utilized SH-SY5Y cells stably overexpressing αSyn (SH-Syn).
Assessed CLU expression levels and its localization within insoluble aggregates.
Investigated the impact of CLU down-regulation on αSyn aggregation and cell viability.
Confirmed the direct interaction between CLU and αSyn using co-immunoprecipitation (co-IP).

Main Results:

αSyn overexpression significantly increased CLU expression, but not other major chaperones (Hsp27, Hsp70, Hsp90).
Induced αSyn aggregation led to CLU accumulating in insoluble protein aggregates.
Down-regulation of CLU resulted in increased αSyn aggregation without affecting cell viability or the Unfolded Protein Response (UPR).
A direct molecular interaction between CLU and αSyn was confirmed via co-IP assays.

Conclusions:

Clusterin (CLU) is upregulated in response to alpha-synuclein (αSyn) burden.
CLU directly interacts with αSyn and is sequestered into insoluble aggregates during PD-like pathology.
CLU plays a protective role by counteracting αSyn aggregation, making it a potential therapeutic target for Parkinson's Disease.