Balk, Bart (2024) Prion Diseases: the link between neurodegeneration and protein misfolding. Master's Thesis / Essay, Biomedical Sciences.
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Abstract
Prion diseases are neurodegenerative diseases characterised by misfolding of the prion proteins in the brain. During the misfolding process, the prions change its conformation from the normally functioning cellular prion protein into the pathogenic scrapie-associated prion protein. PrPSc can cause transmissible spongiform encephalopathies, which prion diseases are also known as. Misfolding and accumulation of the PrPC causes spongiform neurodegeneration in the brain. An example of a human prion disease is Creutzfeldt-Jakob Disease. Animal examples of prion diseases are Bovine spongiform encephalopathy, also known as mad cow disease and Scrapie, found in cattle, cervids and sheep or goats respectively. Prion diseases have different aetiologies. It can originate from spontaneous misfolding, a genetic mutation, or from infection from contamination of food or surgical equipment. The main underlying mechanisms in neurodegeneration are protein aggregation and neuroinflammation, however not all underlying mechanisms of prion diseases are yet fully understood. Its role in Cu2+ binding is not broadly elucidated and its role in reactive oxygen species is also yet to be fully understood. Despite not being fully understood, prion diseases do show similarities with other neurodegenerative disorders. Alzheimer's disease and Huntington’s disease also form protein aggregates and cause neuroinflammation that impairs cell function, causing neurodegeneration in the end.
| Item Type: | Thesis (Master's Thesis / Essay) |
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| Supervisor name: | Eisel, U.L.M. |
| Degree programme: | Biomedical Sciences |
| Thesis type: | Master's Thesis / Essay |
| Language: | English |
| Date Deposited: | 05 Jul 2024 10:08 |
| Last Modified: | 05 Jul 2024 10:08 |
| URI: | https://fse.studenttheses.ub.rug.nl/id/eprint/33050 |
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