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Creutzfeldt-Jakob Disease (and Other Prion Diseases)
Published in Alexander R. Toftness, Incredible Consequences of Brain Injury, 2023
What is particularly interesting about CJD and other prion diseases is that there are subtypes that a person can acquire in different ways. Prion diseases can be acquired from the environment if exposed to infectious prions, such as through ingesting brain tissue. This is one reason that you shouldn't eat human brains (see Kuru). Elsewise, they can appear spontaneously due to an unexpected mutation from a protein into a prion. Or, they can be obtained genetically because the body's ability to produce prions, and susceptibility to them, is passed down through family bloodlines. Respectively, these routes of getting the disease are called acquired, sporadic, and familial. The term iatrogenic is also used to describe CJD in a few cases. These people acquired the disease via medical treatment, such as by infected medical instruments, implants, transplants, or transfusions. In other words, prion diseases can hitch a ride in hospitals through infected metal, tissue, blood, etc. Are you alarmed yet?
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].
Epidemiology and subtypes of dementia
Published in Marjolein de Vugt, Janet Carter, Understanding Young Onset Dementia, 2021
The study of prion diseases has improved the understanding of neurodegenerative and other diseases involving the accumulation of misfolded host proteins (protein‐folding diseases). Mutations of prion protein (PRNP) is implicated in a clinical phenotype that closely resembles familial Alzheimer's disease (Mead et al., 2006). An octa-repeat deletion around codon 82 with a familial inheritance has been linked to a phenotype similar to Alzheimer's disease (Perry et al., 1995). Further to this, PRNP STOP mutations, Q160X and Q227X, have also been implicated in Alzheimer disease-like pathology with either amyloid plaques, neurofibrillary tangle lesions, or both (Jansen et al., 2010; Schmitz et al., 2017).
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.
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].
Tackling prion diseases: a review of the patent landscape
Published in Expert Opinion on Therapeutic Patents, 2021
Marco Zattoni, Giuseppe Legname
Therapeutic approaches directed toward the identification of treatment against prion diseases require a series of additional precautions compared to other infectious pathologies, such as virus- or bacteria- caused pathologies. The main difficulty in developing anti-prion drugs consists in the modulation of the physiological expression of the PrPC, which shares the same amino acidic sequence to pathological, infectious PrPSc. This hurdle, unique to prion disorders, requires for example overcoming of host self-tolerance to PrPC in order to induce an immunological response using anti-PrP antibodies. Thus, the use of immune response booster or molecular tool able to increase the immunogen recognition would play an important role in strengthening immune system of prion-infected individuals.