Prion-like transmission of protein aggregates in neurodegenerative diseases
Open accessAbstract
Neurodegenerative diseases are commonly associated with the accumulation of intracellular or extracellular protein aggregates. Recent studies suggest that these aggregates are capable of crossing cellular membranes and can directly contribute to the propagation of neurodegenerative disease pathogenesis. We propose that, once initiated, neuropathological changes might spread in a 'prion-like' manner and that disease progression is associated with the intercellular transfer of pathogenic proteins. The transfer of naked infectious particles between cells could therefore be a target for new disease-modifying therapies.
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In Parkinson's disease and Lewy body disease, α-synuclein aggregates initially spread through brainstem and olfactory bulb, followed by limbic structures, and only then to neocortex.
“In Parkinson’s disease and Lewy body disease, α-synuclein aggregates initially spread through the brainstem and olfactory bulb followed by limbic structures, and only thence to the neocortex.”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [73]
In these neurodegenerative diseases, aggregates initially deposit at the ventral base of the forebrain and midbrain and then extend rostrally and dorsally to the cortex.
“In each of these cases, the aggregates initially deposit at the ventral base of the forebrain and midbrain, and then extend rostrally and dorsally to the cortex.”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [73]
Recent neuroimaging advances provide approaches to map the human glymphatic system and assess its functional competence in disease and effects on sleep-dependent glymphatic cyclicity.
“In that regard, recent advances in neuroimaging have provided multiple approaches to map the human glymphatic system, and hence to assess its functional competence in the context of disease, as well as of the effects thereof on sleep-dependent glymphatic cyclicity (72, 73, 108).”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [73]
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Bhatia, S., Singh, M., Singh, T., & Singh, V. (2023) · Neurochemical Research · doi:10.1007/s11064-022-03722-w · Cited by 22 · see citing works
Potential Role for Herpesviruses in Alzheimer’s Disease
Duggan, M. R., Torkzaban, B., Ahooyi, T. M., & Khalili, K. (2020) · Journal of Alzheimer's Disease · doi:10.3233/jad-200814 · Cited by 13 · see citing works
- Authors
- Brundin, P., Melki, R., & Kopito, R.
- Affiliations
- Lund University (SE)
- Centre National de la Recherche Scientifique (FR)
- Stanford University (US)
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2010-04
- Volume
- 11
- Issue
- 4
- Pages
- 301-307
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC2892479
- OpenAlex
- W2004185979
- Cited by
- 778
- References
- 52
- Citations by year
- 2026: 29 · 2025: 36 · 2024: 31 · 2023: 29 · 2022: 34 · 2021: 45 · 2020: 55 · 2019: 67 · 2018: 45 · 2017: 67 · 2016: 55 · 2015: 57 · 2014: 62 · 2013: 56 · 2012: 45
- FWCI
- 4.63
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (R01NS042842)
- 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
- prion-like transmission, protein aggregates, neurodegenerative diseases, protein misfolding, intercellular transfer, disease-modifying therapy
- MeSH terms
- Amyloid, Animals, Humans, Prions, Neurodegenerative Diseases
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