ReviewNPJ Parkinson's disease2017
Vertebrate food products as a potential source of prion-like α-synuclein.
Review in NPJ Parkinson's disease, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Understanding alpha-synuclein aggregation propensity in animals and humans.Biochemistry and biophysics reports · 2024Article
- Addition of α-synuclein aggregates to the intestinal environment recapitulates Parkinsonian symptoms in model systems.Acta pharmacologica Sinica · 2024Article
- Gut-to-Brain α-Synuclein Transmission in Parkinson's Disease: Evidence for Prion-like Mechanisms.International journal of molecular sciences · 2023Review
- The Role of Exposomes in the Pathophysiology of Autoimmune Diseases I: Toxic Chemicals and Food.Pathophysiology : the official journal of the International Society for Pathophysiology · 2021Review
- Article
- Processed Food Additive Microbial Transglutaminase and Its Cross-Linked Gliadin Complexes Are Potential Public Health Concerns in Celiac Disease.International journal of molecular sciences · 2020Review
- Selective vulnerability in α-synucleinopathies.Acta neuropathologica · 2019Review
- Alpha-synuclein: prion or prion-like?Acta neuropathologica · 2019Article
- Health Benefits of Nut Consumption in Middle-Aged and Elderly Population.Antioxidants (Basel, Switzerland) · 2019Review
- Diet in Parkinson's Disease: Critical Role for the Microbiome.Frontiers in neurology · 2019Review
- Gastrointestinal Dysfunction in Parkinson's Disease.Current treatment options in neurology · 2018Review
- Glycotoxins: Dietary and Metabolic Origins; Possible Amelioration of Neurotoxicity by Carnosine, with Special Reference to Parkinson's Disease.Neurotoxicity research · 2018Review
- The Gut and Parkinson's Disease: Hype or Hope?Journal of Parkinson's disease · 2018Review
- Dietary and Environmental Risk Factors in Parkinson's and Alzheimer's Disease: A Semi-Quantitative Pilot Study.Annals of Indian Academy of NeurologyArticle
- Dietary and Environmental Risk Factors in Parkinson's Disease and Alzheimer's Disease: Beware of Your Food Plate and Your Surroundings!Annals of Indian Academy of NeurologyArticle
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aberrant aggregation of the protein α-synuclein is thought to be involved in Parkinson's disease (PD). However, the factors that lead to initiation and propagation of α-synuclein aggregation are not clearly understood. Recently, the hypothesis that α-synuclein aggregation spreads via a prion-like mechanism originating in the gut has gained much scientific attention. If α-synuclein spreads via a prion-like mechanism, then an important question becomes, what are the origins of this prion-like species? Here we review the possibility that α-synuclein aggregation could be seeded via the ingestion of a prion-like α-synuclein species contained within food products originating from vertebrates. To do this, we highlight current evidence for the gut-to-brain hypothesis of PD, and put this in context of available routes of α-synuclein prion infectivity via the gastrointestinal (GI) tract. We then discuss meat as a ready exogenous source of α-synuclein and how certain risk factors, including inflammation, may allow for dietary α-synuclein to pass from the GI lumen into the host to induce pathology. Lastly, we review epidemiological evidence that dietary factors may be involved in PD. Overall, research to date has yet to directly test the contribution of dietary α-synuclein to the mechanism of initiation and progression of the disease. However, numerous experimental findings, including the potent seeding and spreading behavior of α-synuclein fibrils, seem to support, at least in part, the feasibility of an infection with a prion α-synuclein particle via the GI tract. Further studies are required to determine whether dietary α-synuclein contributes to seeding pathology in the gut.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.