Prions and protein-folding diseases: Review: Prions and protein-folding diseases
Open accessAbstract
Prions represent a group of proteins with a unique capacity to fold into different conformations. One isoform is rich in beta-pleated sheets and can aggregate into amyloid that may be pathogenic. This abnormal form propagates itself by imposing its confirmation on the homologous normal host cell protein. Pathogenic prions have been shown to cause lethal neurodegenerative diseases in humans and animals. These diseases are sometimes infectious and hence referred to as transmissible spongiform encephalopathies. In the present review, the remarkable evolution of the heterodox prion concept is summarized. The origin of this phenomenon is based on information transfer between homologous proteins, without the involvement of nucleic acid-encoded mechanisms. Historically, kuru and Creutzfeldt-Jakob disease (CJD) were the first infectious prion diseases to be identified in man. It was their relationship to scrapie in sheep and experimental rodents that allowed an unravelling of the particular molecular mechanism that underlie the disease process. Transmission between humans has been documented to have occurred in particular contexts, including ritual cannibalism, iatrogenic transmission because of pituitary gland-derived growth hormone or the use in neurosurgical procedures of dura mater from cadavers, and the temporary use of a prion-contaminated protein-rich feed for cows. The latter caused a major outbreak of bovine spongiform encephalopathy, which spread to man by human consumption of contaminated meat, causing approximately 200 cases of variant CJD. All these epidemics now appear to be over because of measures taken to curtail further spread of prions. Recent studies have shown that the mechanism of protein aggregation may apply to a wider range of diseases in and possibly also outside the brain, some of which are relatively common such as Alzheimer's and Parkinson's diseases. Furthermore, it has become apparent that the phenomenon of prion aggregation may have a wider physiological importance, but a full understanding of this remains to be defined. It may involve maintaining neuronal functions and possibly contributing to the establishment of long-term memory.
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Templated modification of protein structure subserves the transfer and storage of useful biological information in systems ranging from microbes to mammals.
“Moreover, the templated modification of protein structure also subserves the transfer and storage of useful biological information in systems ranging from microbes to mammals107-110.”
From Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders (2011) · cites this paper as [110]
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- Authors
- Norrby, E.
- Affiliations
- Royal Swedish Academy of Sciences (SE)
- Corresponding author
- Norrby, E.
- Venue
- Journal of Internal Medicine
- Publisher
- Wiley
- Published
- 2011-05-12
- Volume
- 270
- Issue
- 1
- Pages
- 1-14
- ISSN
- 0954-6820 (ISSN-L)
- OpenAlex
- W1485459398
- Cited by
- 75
- References
- 79
- Citations by year
- 2025: 4 · 2024: 2 · 2023: 7 · 2022: 6 · 2021: 1 · 2020: 6 · 2019: 3 · 2018: 2 · 2017: 3 · 2016: 8 · 2015: 6 · 2014: 2 · 2013: 7 · 2012: 12
- FWCI
- 0.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Internal Medicine (publishedVersion)
- PubMed (publishedVersion)
- 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
- prions, protein folding diseases, prion disease, prion aggregation, amyloid, prion transmission, kuru, Creutzfeldt-Jakob disease, scrapie, bovine spongiform encephalopathy, variant Creutzfeldt-Jakob disease, iatrogenic transmission, Alzheimer's disease, Parkinson's disease, long-term memory, neurodegeneration
- MeSH terms
- Animals, Cattle, Humans, Creutzfeldt-Jakob Syndrome, Prions, Encephalopathy, Bovine Spongiform, Proteostasis Deficiencies
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