Cited by 271Parkinson's Disease Mechanisms and TreatmentsNeuroinflammation and Neurodegeneration MechanismsNuclear Receptors and Signaling

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

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Wang, Wei, Nguyen, Linh T. T., Burlak, Christopher, Chegini, Fariba, Guo, Feng, Chataway, Tim, Ju, Shulin, Fisher, Oriana S., Miller, David W., Datta, Debajyoti, Wu, Fang, Wu, Chun-Xiang, Landeru, Anuradha, Wells, James A., Cookson, Mark R., Boxer, Matthew B., Thomas, Craig J., Gai, Wei Ping, Ringe, Dagmar, Petsko, Gregory A., Hoang, Quyen Q.·2016·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1610099113PMC PMC5003239

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Abstract

Significance: The aggregation of α-synuclein (aSyn) is a pathological hallmark of Parkinson’s disease. Here we show that the enzymatic component of the innate inflammation system, known as caspase-1, hydrolyzes aSyn, rendering it aggregation-prone.

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10.1073/pnas.0406976102 · DOI
10.3727/000000007783464911 · DOI
10.1016/j.parkreldis.2004.01.005 · DOI
10.1289/ehp.1002839 · DOI
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Authors: Wang, W., Nguyen, L. T. T., Burlak, C., Chegini, F., Guo, F., Chataway, T., Ju, S., Fisher, O. S., Miller, D. W., Datta, D., Wu, F., Wu, C.-X., Landeru, A., Wells, J. A., Cookson, M. R., Boxer, M. B., Thomas, C. J., Gai, W. P., Ringe, D., Petsko, G. A., & Hoang, Q. Q.
Affiliations: Indiana University Indianapolis (US)
University of Minnesota (US)
Flinders University (AU)
Brandeis University (US)
National Institutes of Health (US)
University of California, San Francisco (US)
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202;
Brigham and Women's Hospital (US)
ORCID: Burlak, Christopher
Chataway, Tim
Ju, Shulin
Fisher, Oriana S.
Miller, David W.
Datta, Debajyoti
Wu, Fang
Wells, James A.
Cookson, Mark R.
Thomas, Craig J.
Gai, Wei Ping
Petsko, Gregory A.
Hoang, Quyen Q.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2016-08
Volume: 113
Issue: 34
Pages: 9587-9592
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.1610099113
PMC: PMC5003239
OpenAlex: W2503377259
Cited by: 270
References: 52
Citations by year: 2026: 16 · 2025: 18 · 2024: 22 · 2023: 31 · 2022: 39 · 2021: 41 · 2020: 28 · 2019: 28 · 2018: 32 · 2017: 13 · 2016: 2
FWCI: 18.80
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.pnas.org/preview_site/misc/userlicense.xhtml (vor, 184 d)
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
eScholarship (California Digital Library) (submittedVersion)
IUScholarWorks (Indiana University) (submittedVersion)
Purdue University Indianapolis (Indiana University) (submittedVersion)
Funders: DH | National Institute for Health Research (1R21NS079881-01, 5R01GM111639)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
Keywords: alpha-synuclein, Parkinson's disease, caspase-1, protein truncation, protein aggregation, Lewy bodies, inflammasome, neuroinflammation, neurotoxicity, sporadic Parkinson's disease
MeSH terms: Alum Compounds, Cell Survival, Dipeptides, Gene Expression Regulation, Humans, Lipopolysaccharides, Neurons, Nigericin, Signal Transduction, Lewy Bodies, Caspase 1, Vitamin K 3, RNA, Small Interfering, Cell Line, Tumor, alpha-Synuclein, Interleukin-1beta, Inflammasomes, para-Aminobenzoates, Protein Aggregates

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

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