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Fatal Familial Insomnia
Published in Alexander R. Toftness, Incredible Consequences of Brain Injury, 2023
One of the many unusual things about FFI is that it is an inherited prion disease. Prion diseases are thought to be caused by misfolded proteins that replicate and cause damage in the brain over time (see Creutzfeldt-Jakob Disease). FFI follows family bloodlines over generations in what's called an autosomal dominant pattern, meaning that one mutated gene is enough to develop the disease and risk passing it along to your children (Wu et al., 2018). If one parent has FFI, you have a 50% chance of having it too (Lindsley, 2017).
Miscellaneous
Published in Ibrahim Natalwala, Ammar Natalwala, E Glucksman, MCQs in Neurology and Neurosurgery for Medical Students, 2022
Ibrahim Natalwala, Ammar Natalwala, E Glucksman
Creutzfeldt-Jakob disease is a prion disease that causes a rapidly progressive (weeks to months) dementia and early death. It can be acquired through ingestion of beef from cattle affected by mad cow disease. Prion diseases are caused by the conversion of a normal cellular protein termed prion protein to a beta-pleated form. The beta-pleated form resists degradation by proteases and its accumulation results in a spongiform encephalopathy. Multiple cysts with an absence of inflammatory cells on biopsy are characteristic.5,6
A Treatise on the Role of Herpesvirus in Neurodegeneration
Published in Abhai Kumar, Debasis Bagchi, Antioxidants and Functional Foods for Neurodegenerative Disorders, 2021
Bernard W. Downs, Manashi Bagchi, Bruce S. Morrison, Jeffrey Galvin, Steve Kushner, Debasis Bagchi, Kenneth Blum
Prion diseases, also known as transmissible spongiform encephalopathies, are a group of rare, fatal brain diseases that affect animals and humans. They are thought to be caused by an infectious agent known as a prion, which is derived from a misfolded version of a normal host protein known as prion protein. Prion diseases include bovine spongiform encephalopathy (“mad cow” disease) in cattle, Creutzfeldt–Jakob disease (CJD) and variant CJD in humans, scrapie in sheep, and chronic wasting disease in deer, elk, moose, and reindeer. Something more of the pathological events needs to be understood about the bio-environment in which these misfolded proteins occur.
Synthesis and anti-prion aggregation activity of acylthiosemicarbazide analogues
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2023
Dong Hwan Kim, Jaehyeon Kim, Hakmin Lee, Dongyun Lee, So Myoung Im, Ye Eun Kim, Miryeong Yoo, Yong-Pil Cheon, Jason C. Bartz, Young-Jin Son, Eun-Kyoung Choi, Yong-Sun Kim, Jae-Ho Jeon, Hyo Shin Kim, Sungeun Lee, Chongsuk Ryou, Tae-gyu Nam
Prions are the infectious protein that cause prion diseases, including bovine spongiform encephalopathy, scrapie, and Creutzfeldt–Jakob disease (CJD)1,2. The clinical signs of prion diseases are related to impaired brain function, such as cognitive dysfunction, cerebral ataxia and motor dysfunction1,3. The neuropathological features of prion diseases include spongiform degeneration and gliosis in accociation with the accumulation of PrPsc in the brain4. Recent studies at the cellular and molecular levels report that spongiosis and neurodegeneration are caused by prion-induced chronic endoplasmic reticulum (ER) stress leading to the depletion of an intracellular lipid molecule and impaired lysosomal trafficking in brain cells5,6.
The epidemiological and clinical characteristics of patients with young-onset genetic Creutzfeldt-Jakob disease
Published in Neurological Research, 2023
Daniel Safadi, Oren S Cohen, Joab Chapman, Hanna Rosenmann, Zeev Nitsan, Esther Kahan, Shmuel Appel, Marwan Alkrenawi
Human prion disorders are heterogeneous with different phenotypes, epidemiology, and disease course. Sporadic CJD (sCJD) is the most common human prion disease, accounting for about 85% of cases; 10–15% are genetic (gCJD) and 1% are iatrogenic [5], most frequently associated with prior treatment with human pituitary-derived hormones or human dura mater grafts [6]. Variant CJD (vCJD) is a novel human prion disease that occurred predominantly in the UK and had been linked to the consumption of beef products contaminated with bovine spongiform encephalopathy (BSE) agent [7]. gCJD arises from mutations in PRNP, the gene that encodes PrP, and over 50 PRNP mutations have been described [8,9]. E200K is the most common mutation throughout the world [10], but is particularly common in Slovakia, where it is present in>65% of individuals with prion disease[10], and in Israel among the Jewish patients with Libyan ancestry [11].
Recent advances in cellular models for discovering prion disease therapeutics
Published in Expert Opinion on Drug Discovery, 2022
Lea Nikolić, Chiara Ferracin, Giuseppe Legname
Despite intensive research in this area, there are still no effective prophylactic regimens or therapies for human prion diseases. As the molecular basis of these devastating diseases remains poorly understood, there is an urgent need for more relevant cellular models that better approximate real-life conditions. The complexity of research in the prion field is largely due to the existence of different prion strains and species transmission barrier. Furthermore, de novo replication of bona fide prions is not straightforward in non-dividing cells. Each cellular model discussed in this review not only has its own benefits but also suffers different limitations (summarized in Figure 1). An ideal model would be the one that mimics most of the in vivo CNS architecture and composition, sustains prion infection, and allows for rapid and cost-effective screenings of potential anti-prion therapeutics. However, to develop such a model, intensive research in this field is still needed.