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Anti-amyloidogenic effect of artemin on α-synuclein

  • Narges Marvastizadeh , Bahareh Dabirmanesh ORCID logo EMAIL logo , Reza H. Sajedi and Khosro Khajeh
Published/Copyright: July 16, 2020

Abstract

α-Synuclein fibrillation is now regarded as a major pathogenic process in Parkinson’s disease and its proteinaceous deposits are also detected in other neurological disorders including Alzheimer's disease. Therefore anti-amyloidegenic compounds may delay or prevent the progression of synucleinopathies disease. Molecular chaperones are group of proteins which mediate correct folding of proteins by preventing unsuitable interactions which may lead to aggregation. The objective of this study was to investigate the anti-amyloidogenic effect of molecular chaperone artemin on α-synuclein. As the concentration of artemin was increased up to 4 μg/ml, a decrease in fibril formation of α-synuclein was observed using thioflavin T (ThT) fluorescence and congo red (CR) assay. Transmission electron microscopy (TEM) images also demonstrated a reduction in fibrils in the presence of artemin. The secondary structure of α-synuclein was similar to its native form prior to fibrillation when incubated with artemin. A cell-based assay has shown that artemin inhibits α-synuclein aggregation and reduce cytotoxicity, apoptosis and reactive oxygen species (ROS) production. Our results revealed that artemin has efficient chaperon activity for preventing α-synuclein fibril formation and toxicity.


Corresponding author: Bahareh Dabirmanesh, Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, P.O. Box 14115-175, Tehran, Iran, E-mail:

Funding source: Tarbiat Modares University

Funding source: Iranian National Science Foundation

Award Identifier / Grant number: 93042561

Acknowledgments

We gratefully appreciate the research council of Tarbiat Modares University and Iranian National Science Foundation (INSF, project 93042561) for their financial support through this investigation.

  1. Conflict of interest statement: The authors declare no competing interest.

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Received: 2019-12-25
Accepted: 2020-04-20
Published Online: 2020-07-16
Published in Print: 2020-09-25

© 2020 Walter de Gruyter GmbH, Berlin/Boston

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