Cited by 203Parkinson's Disease Mechanisms and TreatmentsNuclear Receptors and SignalingUbiquitin and proteasome pathways

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Proteolytic stress: A unifying concept for the etiopathogenesis of Parkinson’s disease

McNaught, Kevin St. P., Olanow, C. Warren·2003·Annals of Neurology

DOI 10.1002/ana.10512

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Abstract

The etiopathogenesis of Parkinson's disease (PD) has been elusive. Recently, several lines of evidence have converged to suggest that defects in the ubiquitin-proteasome system and proteolytic stress underlie nigral pathology in both familial and sporadic forms of the illness. In support of this concept, mutations in alpha-synuclein that cause the protein to misfold and resist proteasomal degradation cause familial PD. Similarly, mutations in two enzymes involved in the normal function of the ubiquitin-proteasome system, parkin and ubiquitin C-terminal hydrolase L1, are also associated with hereditary PD. Furthermore, structural and function defects in 26/20S proteasomes with accumulation and aggregation of potentially cytotoxic abnormal proteins have been identified in the substantia nigra pars compacta of patients with sporadic PD. Thus, a defect in protein handling appears to be a common factor in sporadic and the various familial forms of PD. This hypothesis may also account for the vulnerability of the substantia nigra pars compacta in PD, why the disorder is age related, and the nature of the Lewy body. It has also facilitated the development of experimental models that recapitulate the behavioral and pathological features of PD, and hopefully will lead to the development of novel neuroprotective therapies for the disorder.

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Authors: McNaught, K. S. P., & Olanow, C. W.
Affiliations: Icahn School of Medicine at Mount Sinai (US)
Corresponding author: Olanow, C. Warren
ORCID: Olanow, C. Warren
Venue: Annals of Neurology
Publisher: Wiley
Published: 2003
Volume: 53
Issue: S3
Pages: S73-S86
ISSN: 0364-5134 (ISSN-L)
1531-8249
DOI: 10.1002/ana.10512
OpenAlex: W2135387829
Cited by: 203
References: 96
Citations by year: 2026: 2 · 2025: 1 · 2024: 3 · 2023: 2 · 2021: 2 · 2020: 7 · 2019: 1 · 2018: 5 · 2017: 3 · 2016: 3 · 2015: 5 · 2014: 5 · 2013: 3 · 2012: 6
FWCI: 3.60
Type: journal article
Language: en
Open access: closed
Licence: doi.wiley.com/10.1002/tdm_license_1.1 (tdm, 4626 d)
Locations: Annals of Neurology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ns033772-09)
National Institute of Neurological Disorders and Stroke (NS 33772)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: Parkinson's disease, ubiquitin-proteasome system, alpha-synuclein, Parkin, UCHL1, substantia nigra pars compacta, Lewy bodies, familial Parkinson's disease, sporadic Parkinson's disease, protein aggregation, neuroprotection
MeSH terms: Cysteine Endopeptidases, Humans, Ligases, Multienzyme Complexes, Nerve Degeneration, Nerve Tissue Proteins, Parkinson Disease, Peptide Hydrolases, Substantia Nigra, Thiolester Hydrolases, Lewy Bodies, Point Mutation, Ubiquitin Thiolesterase, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Synucleins, alpha-Synuclein

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Proteolytic stress: A unifying concept for the etiopathogenesis of Parkinson’s disease

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