Caspase-1 causes truncation and aggregation of the Parkinson’s disease-associated protein α-synuclein

Journal:
Proceedings of the National Academy of Sciences of the United States of America
Published:
DOI:
10.1073/pnas.1610099113
Affiliations:
16
Authors:
21

Research Highlight

Cutting the fuse on Parkinson’s disease

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As Parkinson’s disease progresses, increasing numbers of brain cells are lost as toxic protein clumps aggregate in patients’ nerves. But this progression could be stopped by tinkering with the immune system, a study published in The Proceedings of the National Academy of Sciences USA has revealed.

A team of US and Australian scientists, including researchers from Flinders University, have discovered how these clumps of the protein α-synuclein form.

They found that an enzyme called caspase-1, which is released during inflammation, breaks apart α-synuclein in way that leaves it more prone to sticking together. The researchers discovered that α-synuclein clumping could be reduced, and the nerve cell survival improved, by adding a caspase-1 blocking agent.

They scientists propose that changing the immune system’s activity by blocking caspase-1 in patients could be a promising strategy to prevent Parkinson’s disease.

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References

  1. PNAS 113,9587–9592 (2016). doi: 10.1073/pnas.1610099113
Institutions Authors Share
Indiana University (IU), United States of America (USA)
5.000000
0.24
Brandeis University, United States of America (USA)
4.333333
0.21
Centre for Neuroscience (CNS), Australia
4.000000
0.19
NIH NIA Intramural Research Program (IRP), United States of America (USA)
2.000000
0.10
University of California, San Francisco (UCSF), United States of America (USA)
2.000000
0.10
NIH National Center for Advancing Translational Sciences (NCATS), United States of America (USA)
2.000000
0.10
University of Minnesota (UMN), United States of America (USA)
1.000000
0.05
Harvard University, United States of America (USA)
0.333333
0.02
Brigham and Women's Hospital (BWH), United States of America (USA)
0.333333
0.02