Cited by 450Prion Diseases and Protein MisfoldingAlzheimer's disease research and treatmentsAmyotrophic Lateral Sclerosis Research

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Propagation and spread of pathogenic protein assemblies in neurodegenerative diseases

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Jucker, Mathias, Walker, Lary C.·2018·Nature Neuroscience

DOI 10.1038/s41593-018-0238-6PMC PMC6375686

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Abstract

Many neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, are characterized by the progressive appearance of abnormal proteinaceous assemblies in the nervous system. Studies in experimental systems indicate that the assemblies originate from the prion-like seeded aggregation of specific misfolded proteins that proliferate and amass to form the intracellular and/or extracellular lesions typical of each disorder. The host in which the proteopathic seeds arise provides the biochemical and physiological environment that either supports or restricts their emergence, proliferation, self-assembly, and spread. Multiple mechanisms influence the spatiotemporal spread of seeds and the nature of the resulting lesions, one of which is the cellular uptake, release, and transport of seeds along neural pathways and networks. The characteristics of cells and regions in the affected network govern their vulnerability and thereby influence the neuropathological and clinical attributes of the disease. The propagation of pathogenic protein assemblies within the nervous system is thus determined by the interaction of the proteopathic agent and the host milieu.

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Authors: Jucker, M., & Walker, L. C.
Affiliations: German Center for Neurodegenerative Diseases (DE)
Emory University (US)
Corresponding author: Jucker, Mathias
Walker, Lary C.
ORCID: Jucker, Mathias
Walker, Lary C.
Venue: Nature Neuroscience
Publisher: Springer Science and Business Media LLC
Published: 2018-09-26
Volume: 21
Issue: 10
Pages: 1341-1349
ISSN: 1097-6256 (ISSN-L)
1546-1726
DOI: 10.1038/s41593-018-0238-6
PMC: PMC6375686
OpenAlex: W2891544369
Cited by: 450
References: 154
Citations by year: 2026: 50 · 2025: 69 · 2024: 41 · 2023: 59 · 2022: 51 · 2021: 70 · 2020: 66 · 2019: 40 · 2018: 4
FWCI: 4.41
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature Neuroscience (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
DZNE Pub (submittedVersion)
Funders: National Institutes of Health (P51OD011132)
National Institute on Aging (P50AG025688)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
Keywords: neurodegenerative diseases, protein aggregation, prion-like seeding, protein misfolding, Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, seed propagation, neurodegeneration, host-pathogen interaction
MeSH terms: Animals, Cell Communication, Humans, Prions, Neurodegenerative Diseases

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