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Creutzfeldt-Jakob Disease (and Other Prion Diseases)
Published in Alexander R. Toftness, Incredible Consequences of Brain Injury, 2023
Prion diseases cause a person's brain to slowly decay, and like other neurodegenerative diseases such as Alzheimer disease, the person gradually acts less and less like themselves. Prion diseases are caused by misfolded proteins—which are called prions because one guy thought that name sounded cool (Max, 2006, p. 121). Prions are not alive, they are just molecules that are bent out of shape. Despite this, they make copies of themselves just like a living thing would do. This has been compared to the way that crystals grow bigger by replicating a chemical structure (Scheckel & Aguzzi, 2018). This self-copying damages your brain as the prions accumulate.
Consumer Views on Health Issues Arising from Food Products
Published in Megh R. Goyal, Preeti Birwal, Santosh K. Mishra, Phytochemicals and Medicinal Plants in Food Design, 2022
Harita R. Desai, Murlidhar Meghwal
Severe health hazards have been associated with food-borne pathogenic microorganisms. Pathogenic elements form the major causative factor causing food-borne ailments. Serious health perils have been caused by agents like Campylobacter jejuni, members of the Salmonella species, Listeria monocytogenes; Escherichia coli. Currently, Prion (a protein-based infectious agent) has been identified as a risk factor causing hazardous conditions in humans. The Bovine Spongiform Encephalopathy and variant Creutzfeldt–Jakob diseases in humans have been caused due to prions [100, 116].
Neuroinfectious Diseases
Published in Philip B. Gorelick, Fernando D. Testai, Graeme J. Hankey, Joanna M. Wardlaw, Hankey's Clinical Neurology, 2020
Jeremy D. Young, Jesica A. Herrick, Scott Borgetti
No effective treatment exists for CJD or other prion diseases, and management is entirely supportive. CJD is uniformly fatal, with most deaths occurring within 1 year of presentation.
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
Following the discovery of PrP as the major prion disease-causing agent, other proteins, in diverse organisms, were identified as proteinaceous infectious particles (prions). Although these proteins have different primary sequences and functions, they share many similarities with the disease-causing prions. For instance, they are PK resistant, they can spread their misfolded conformation to the native isoform, they exist in multiple distinct variants, and they can spread from one cell to another and its progeny. In yeasts, at least ten prions have been identified so far. The most studied yeast prions are Saccharomyces Cerevisiae [URE3], the prion form of Ure2p (a protein involved in the regulation of nitrogen metabolism), and [PSI+], the prion form of Sup35 (a translation termination factor); but also other engineered yeast prions have been developed. An example is an engineered Sup35 protein fused to various regions of the mouse PrP protein [107,108].