Cited by 625Alzheimer's disease research and treatmentsPrion Diseases and Protein MisfoldingAmyotrophic Lateral Sclerosis Research

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Protein transmission in neurodegenerative disease

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Peng, Chao, Trojanowski, John Q., Lee, Virginia M.-Y.·2020·Nature Reviews Neurology

DOI 10.1038/s41582-020-0333-7PMC PMC9242841

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Abstract

Most neurodegenerative diseases are characterized by the intracellular or extracellular aggregation of misfolded proteins such as amyloid-β and tau in Alzheimer disease, α-synuclein in Parkinson disease, and TAR DNA-binding protein 43 in amyotrophic lateral sclerosis. Accumulating evidence from both human studies and disease models indicates that intercellular transmission and the subsequent templated amplification of these misfolded proteins are involved in the onset and progression of various neurodegenerative diseases. The misfolded proteins that are transferred between cells are referred to as 'pathological seeds'. Recent studies have made exciting progress in identifying the characteristics of different pathological seeds, particularly those isolated from diseased brains. Advances have also been made in our understanding of the molecular mechanisms that regulate the transmission process, and the influence of the host cell on the conformation and properties of pathological seeds. The aim of this Review is to summarize our current knowledge of the cell-to-cell transmission of pathological proteins and to identify key questions for future investigation.

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4 retracted

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Authors: Peng, C., Trojanowski, J. Q., & Lee, V. M.-Y.
Affiliations: University of California, Los Angeles (US)
University of Pennsylvania (US)
Corresponding author: Lee, Virginia M.-Y.
ORCID: Peng, Chao
Trojanowski, John Q.
Lee, Virginia M.-Y.
Venue: Nature Reviews Neurology
Publisher: Springer Science and Business Media LLC
Published: 2020-03-23
Volume: 16
Issue: 4
Pages: 199-212
ISSN: 1759-4758 (ISSN-L)
1759-4766
DOI: 10.1038/s41582-020-0333-7
PMC: PMC9242841
OpenAlex: W3012646333
Cited by: 625
References: 257
Citations by year: 2026: 73 · 2025: 106 · 2024: 116 · 2023: 99 · 2022: 92 · 2021: 100 · 2020: 39
FWCI: 10.56
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature Reviews Neurology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute on Aging (U19AG062418)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
Keywords: protein transmission, neurodegenerative diseases, protein aggregation, amyloid-beta, tau protein, alpha-synuclein, Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, intercellular protein transfer
MeSH terms: Huntingtin Protein, Alzheimer Disease, Amyotrophic Lateral Sclerosis, Axonal Transport, Brain, Cell Communication, DNA-Binding Proteins, Endocytosis, Humans, Huntington Disease, Membrane Fusion, Neuroglia, Neurons, Parkinson Disease, Amyloid beta-Peptides, tau Proteins, Neurodegenerative Diseases, Genetic Predisposition to Disease, Protein Transport, Nanotubes, alpha-Synuclein, Exosomes, Protein Aggregation, Pathological

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