Protein transmission in neurodegenerative disease
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...
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| Published in | Nature reviews. Neurology Vol. 16; no. 4; pp. 199 - 212 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
01.04.2020
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1759-4758 1759-4766 1759-4766 |
| DOI | 10.1038/s41582-020-0333-7 |
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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.
In this Review, Peng et al. summarize the evidence for cell-to-cell transmission of pathological proteins in neurodegenerative diseases such as Alzheimer disease and Parkinson disease, and identify key questions for future investigation.
Key points
Cell-to-cell transmission and the subsequent amplification of pathological proteins is emerging as a common mechanism for the progression of various neurodegenerative diseases.
Transmission within the CNS as well as from the peripheral nervous system to the CNS has been reported for multiple pathological proteins.
Multiple molecular mechanisms involved in the secretion, uptake and transport of pathological seeds have been identified.
Neurodegenerative disease-related pathological proteins are conformationally diverse.
Various factors can modulate the transmission process, including neuronal activity, glial cells, genetic risk factors and interactions with other pathological proteins.
Antibodies against pathological seeds, which are designed to block the transmission process, are currently in clinical trials. |
|---|---|
| AbstractList | 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. Most neurodegenerative diseases are characterized by the intracellular or extracellular aggregation of misfolded proteins such as amyloid-[beta] and tau in Alzheimer disease, [alpha]-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. In this Review, Peng et al. summarize the evidence for cell-to-cell transmission of pathological proteins in neurodegenerative diseases such as Alzheimer disease and Parkinson disease, and identify key questions for future investigation. Key points Cell-to-cell transmission and the subsequent amplification of pathological proteins is emerging as a common mechanism for the progression of various neurodegenerative diseases. Transmission within the CNS as well as from the peripheral nervous system to the CNS has been reported for multiple pathological proteins. Multiple molecular mechanisms involved in the secretion, uptake and transport of pathological seeds have been identified. Neurodegenerative disease-related pathological proteins are conformationally diverse. Various factors can modulate the transmission process, including neuronal activity, glial cells, genetic risk factors and interactions with other pathological proteins. Antibodies against pathological seeds, which are designed to block the transmission process, are currently in clinical trials. 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.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. 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.In this Review, Peng et al. summarize the evidence for cell-to-cell transmission of pathological proteins in neurodegenerative diseases such as Alzheimer disease and Parkinson disease, and identify key questions for future investigation. Most neurodegenerative diseases are characterized by the intracellular or extracellular aggregation of misfolded proteins such as amyloid-[beta] and tau in Alzheimer disease, [alpha]-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. 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. In this Review, Peng et al. summarize the evidence for cell-to-cell transmission of pathological proteins in neurodegenerative diseases such as Alzheimer disease and Parkinson disease, and identify key questions for future investigation. Key points Cell-to-cell transmission and the subsequent amplification of pathological proteins is emerging as a common mechanism for the progression of various neurodegenerative diseases. Transmission within the CNS as well as from the peripheral nervous system to the CNS has been reported for multiple pathological proteins. Multiple molecular mechanisms involved in the secretion, uptake and transport of pathological seeds have been identified. Neurodegenerative disease-related pathological proteins are conformationally diverse. Various factors can modulate the transmission process, including neuronal activity, glial cells, genetic risk factors and interactions with other pathological proteins. Antibodies against pathological seeds, which are designed to block the transmission process, are currently in clinical trials. |
| Audience | Academic |
| Author | Trojanowski, John Q. Lee, Virginia M.-Y. Peng, Chao |
| AuthorAffiliation | 1 Department of Neurology, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA, USA 2 The Department of Pathology and Laboratory Medicine, Institute on Aging and Center for Neurodegenerative Disease Research, The Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA, USA |
| AuthorAffiliation_xml | – name: 2 The Department of Pathology and Laboratory Medicine, Institute on Aging and Center for Neurodegenerative Disease Research, The Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA, USA – name: 1 Department of Neurology, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA, USA |
| Author_xml | – sequence: 1 givenname: Chao surname: Peng fullname: Peng, Chao organization: Department of Neurology, David Geffen School of Medicine, University of California Los Angeles – sequence: 2 givenname: John Q. orcidid: 0000-0002-9239-8794 surname: Trojanowski fullname: Trojanowski, John Q. organization: The Department of Pathology and Laboratory Medicine, Institute on Aging and Center for Neurodegenerative Disease Research, The Perelman School of Medicine at the University of Pennsylvania – sequence: 3 givenname: Virginia M.-Y. orcidid: 0000-0003-3536-6902 surname: Lee fullname: Lee, Virginia M.-Y. email: vmylee@upenn.edu organization: The Department of Pathology and Laboratory Medicine, Institute on Aging and Center for Neurodegenerative Disease Research, The Perelman School of Medicine at the University of Pennsylvania |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32203399$$D View this record in MEDLINE/PubMed |
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| PublicationDateYYYYMMDD | 2020-04-01 |
| PublicationDate_xml | – month: 04 year: 2020 text: 2020-04-01 day: 01 |
| PublicationDecade | 2020 |
| PublicationPlace | London |
| PublicationPlace_xml | – name: London – name: England |
| PublicationTitle | Nature reviews. Neurology |
| PublicationTitleAbbrev | Nat Rev Neurol |
| PublicationTitleAlternate | Nat Rev Neurol |
| PublicationYear | 2020 |
| Publisher | Nature Publishing Group UK Nature Publishing Group |
| Publisher_xml | – name: Nature Publishing Group UK – name: Nature Publishing Group |
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| Snippet | Most neurodegenerative diseases are characterized by the intracellular or extracellular aggregation of misfolded proteins such as amyloid-β and tau in... Most neurodegenerative diseases are characterized by the intracellular or extracellular aggregation of misfolded proteins such as amyloid-[beta] and tau in... |
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| SubjectTerms | 631/45/470/2284 692/699/375/365 alpha-Synuclein - metabolism Alzheimer Disease - metabolism Alzheimer Disease - pathology Amyloid beta-Peptides - metabolism Amyotrophic Lateral Sclerosis - metabolism Amyotrophic Lateral Sclerosis - pathology Axonal Transport Biological transport Brain - metabolism Brain - pathology Cell Communication Cell interaction Degeneration DNA-Binding Proteins - metabolism Endocytosis Exosomes - metabolism Genetic Predisposition to Disease Health aspects Humans Huntingtin Protein - metabolism Huntington Disease - metabolism Huntington Disease - pathology Medicine Medicine & Public Health Membrane Fusion Nanotubes Nervous system Neurodegenerative Diseases - metabolism Neurodegenerative Diseases - pathology Neuroglia - metabolism Neurological research Neurology Neurons - metabolism Parkinson Disease - metabolism Parkinson Disease - pathology Parkinson's disease Physiological aspects Protein Aggregation, Pathological - metabolism Protein Aggregation, Pathological - pathology Protein metabolism Protein Transport Proteins Review Article tau Proteins - metabolism |
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| Title | Protein transmission in neurodegenerative disease |
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