Propagation and spread of pathogenic protein assemblies in neurodegenerative diseases

Jucker, Mathias; Walker, Lary C.

doi:10.1038/s41593-018-0238-6

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

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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The triphasic framework of abnormal protein creation, aggregation or lack of clearance, and propagation is shared by other neurodegenerative diseases such as amyotrophic lateral sclerosis.
“This triphasic framework is also shared by other NDDs, such as amyotrophic lateral sclerosis [4,5].”
From The Impact of Neurotoxin Proteins Trafficked by Primary Cilia and Extracellular Vesicles in Neurodegenerative Diseases (2025) · cites this paper as [5]
The sections on disease progression and propagation describe misfolding, aggregation, and spread of pathogenic proteins, including SOD1 and TDP-43 associated with the ALS spectrum. They do not establish the claimed three-phase framework for ALS or identify a lack of clearance as one of its phases. The paper also qualifies the evidence: some ALS-associated proteins spread in mouse models, while in-vivo evidence remains incomplete for others. No page numbers are available in our copy. (LLM, conf=0.84)
Experimental — accuracy not yet measured
The pathogenesis of Alzheimer's disease, Parkinson's disease, and Huntington's disease can conceptually be broken down into three phases: creation of an abnormal protein, aggregation or lack of clearance, and propagation.
“The pathogenesis of AD, PD, and HD can conceptually be broken down into three phases: (1) creation of an abnormal protein, (2) aggregation or lack of clearance, and (3) propagation.”
From The Impact of Neurotoxin Proteins Trafficked by Primary Cilia and Extracellular Vesicles in Neurodegenerative Diseases (2025) · cites this paper as [5]
The Abstract and “Progression of neurodegenerative diseases and the prion paradigm” describe the emergence, aggregation, and spread of abnormal proteins, including proteins associated with AD, PD, and HD (pages not specified). But the paper does not present these as a three-phase model or identify lack of clearance as the second phase. “Propagation of other neurodegeneration-associated protein assemblies” also says definitive in-vivo evidence for a prion-like mechanism in polyglutamine-containing proteins remains to be demonstrated, making the claim about HD propagation too definite. (LLM, conf=0.86)
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Analysis of Amyloid-β Pathology Spread in Mouse Models Suggests Spread Is Driven by Spatial Proximity, Not Connectivity
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Calcium Dyshomeostasis in Alzheimer’s Disease Pathogenesis
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Canine Cognitive Dysfunction and Alzheimer’s Disease – Two Facets of the Same Disease?
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Gut inflammation triggers C/EBPβ/δ‐secretase‐dependent gut‐to‐brain propagation of Aβ and Tau fibrils in Alzheimer’s disease
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Tau strains shape disease
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Transgenic Mouse Models of Alzheimer’s Disease: An Integrative Analysis
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A physics-based model explains the prion-like features of neurodegeneration in Alzheimer’s disease, Parkinson’s disease, and amyotrophic lateral sclerosis
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Lipid Peroxidation and Antioxidant Supplementation in Neurodegenerative Diseases: A Review of Human Studies
Petrović, S., Arsić, A., Ristić-Medić, D., Cvetković, Z., & Vučić, V. (2020) · Antioxidants · doi:10.3390/antiox9111128 · Cited by 122 · see citing works
The Wnt/Ca2+ pathway is involved in interneuronal communication mediated by tunneling nanotubes
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Green Tea Epigallocatechin-3-gallate (EGCG) Targeting Protein Misfolding in Drug Discovery for Neurodegenerative Diseases
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Biomimetic carbon nanotubes for neurological disease therapeutics as inherent medication
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Imaging transcriptomics of brain disorders
Arnatkeviciute, A., Fulcher, B. D., Bellgrove, M. A., & Fornito, A. (2022) · Biological Psychiatry Global Open Science · doi:10.1016/j.bpsgos.2021.10.002 · Cited by 113 · see citing works
Iatrogenic Alzheimer’s disease in recipients of cadaveric pituitary-derived growth hormone
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Brain Shape Changes Associated With Cerebral Atrophy in Healthy Aging and Alzheimer’s Disease
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The prion-like spreading of α-synuclein: From in vitro to in vivo models of Parkinson’s disease
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Focusing on mitochondria in the brain: from biology to therapeutics
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Hyperphosphorylation Renders Tau Prone to Aggregate and to Cause Cell Death
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Cell-Nonautonomous Regulation of Proteostasis in Aging and DiseasePreprint
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Aβ plaques
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Astrocytes in Tauopathies
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Brain connectomics: time for a molecular imaging perspective?
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Protein-protein interactions in neurodegenerative diseases: A conspiracy theory
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Efficacy and Safety of Probiotics for the Treatment of Alzheimer's Disease, Mild Cognitive Impairment, and Parkinson's Disease: A Systematic Review and Meta-Analysis
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Alternative systems for misfolded protein clearance: life beyond the proteasome
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Acute targeting of pre-amyloid seeds in transgenic mice reduces Alzheimer-like pathology later in life
Uhlmann, R. E., Rother, C., Rasmussen, J., Schelle, J., Bergmann, C., Ullrich Gavilanes, E. M., Fritschi, S. K., Buehler, A., Baumann, F., Skodras, A., et al. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-00737-w · Cited by 87 · see citing works
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Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies
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The AAA+ chaperone VCP disaggregates Tau fibrils and generates aggregate seeds in a cellular system
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Evidence of distinct α-synuclein strains underlying disease heterogeneity
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Role of Ubiquitin–Proteasome and Autophagy-Lysosome Pathways in α-Synuclein Aggregate Clearance
Sahoo, S., Padhy, A. A., Kumari, V., & Mishra, P. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02897-1 · Cited by 82 · see citing works
Slow Progressive Accumulation of Oligodendroglial Alpha-Synuclein (α-Syn) Pathology in Synthetic α-Syn Fibril-Induced Mouse Models of Synucleinopathy
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The expression level of alpha-synuclein in different neuronal populations is the primary determinant of its prion-like seeding
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The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model
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Alpha-Synuclein Contribution to Neuronal and Glial Damage in Parkinson’s Disease
Saramowicz, K., Siwecka, N., Galita, G., Kucharska-Lusina, A., Rozpędek‐Kamińska, W., & Majsterek, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010360 · Cited by 76 · see citing works
LAG3 is not expressed in human and murine neurons and does not modulate α‐synucleinopathies
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Serpin Signatures in Prion and Alzheimer’s Diseases
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Highly efficient intercellular spreading of protein misfolding mediated by viral ligand-receptor interactions
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The <scp>NLRP3</scp> inflammasome modulates tau pathology and neurodegeneration in a tauopathy model
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Potential human transmission of amyloid β pathology: surveillance and risks
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Therapy for Alzheimer’s disease: Missing targets and functional markers?
Stoiljković, M., Horváth, T. L., & Hajós, M. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101318 · Cited by 72 · see citing works
Post-translational modifications on RNA-binding proteins: accelerators, brakes, or passengers in neurodegeneration?
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Organotypic slice culture model demonstrates inter-neuronal spreading of alpha-synuclein aggregates
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Cell‐to‐cell transmission of C9orf72 poly‐(Gly‐Ala) triggers key features of ALS/FTD
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Mechanisms Linking Mitochondrial Dysfunction and Proteostasis Failure
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The Gypsy Endogenous Retrovirus Drives Non-Cell-Autonomous Propagation in a Drosophila TDP-43 Model of Neurodegeneration
Chang, Y.-H., & Dubnau, J. (2019) · Current Biology · doi:10.1016/j.cub.2019.07.071 · Cited by 68 · see citing works
The Human Hippocampus in Parkinson’s Disease: An Integrative Stereological and Proteomic Study
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Resting-state global brain activity affects early β-amyloid accumulation in default mode network
Han, F., Liu, X., Mailman, R. B., Huang, X., Liu, X., & Initiative, T. A. D. N. (2023) · Nature Communications · doi:10.1038/s41467-023-43627-y · Cited by 68 · see citing works
Non-polyphenolic natural inhibitors of amyloid aggregation
Ma, L., Yang, C., Zheng, J., Chen, Y., Xiao, Y., & Huang, K. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112197 · Cited by 66 · see citing works
Brain atrophy progression in Parkinson’s disease is shaped by connectivity and local vulnerability
Tremblay, C., Rahayel, S., Vo, A., Morys, F., Shafiei, G., Abbasi, N., Markello, R. D., Gan‐Or, Z., Mišić, B., & Dagher, A. (2021) · Brain Communications · doi:10.1093/braincomms/fcab269 · Cited by 66 · see citing works
Neurodegeneration and neuroinflammation are linked, but independent of alpha‐synuclein inclusions, in a seeding/spreading mouse model of Parkinson's disease
Garcia, P., Jürgens‐Wemheuer, W., Uriarte Huarte, O., Michelucci, A., Masuch, A., Brioschi, S., Weihofen, A., Koncina, E., Coowar, D., Heurtaux, T., et al. (2022) · Glia · doi:10.1002/glia.24149 · Cited by 65 · see citing works
Alzheimer’s disease patient brain extracts induce multiple pathologies in novel vascularized neuroimmune organoids for disease modeling and drug discovery
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Differentially targeted seeding reveals unique pathological alpha-synuclein propagation patterns
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Molecular mechanisms of amyloid formation in living systems
Sinnige, T. (2022) · Chemical Science · doi:10.1039/d2sc01278b · Cited by 64 · see citing works
DNAJC proteins and pathways to parkinsonism
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Progress of immunotherapy of anti-α-synuclein in Parkinson’s disease
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Inefficient quality control of ribosome stalling during APP synthesis generates CAT-tailed species that precipitate hallmarks of Alzheimer’s disease
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Self-citation

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
Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › 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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Propagation and spread of pathogenic protein assemblies in neurodegenerative diseases

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