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Degenerative Diseases of the Nervous System
Published in Philip B. Gorelick, Fernando D. Testai, Graeme J. Hankey, Joanna M. Wardlaw, Hankey's Clinical Neurology, 2020
James A. Mastrianni, Elizabeth A. Harris
Prion diseases are fatal neurodegenerative disorders characterized by the CNS accumulation of a misfolded isoform of a membrane-bound glycoprotein, the prion protein (PrP), which acquires the property of transmissibility. These diseases were formerly known as transmissible spongiform encephalopathies (TSEs).
Prions
Published in Dongyou Liu, Handbook of Foodborne Diseases, 2018
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of rare and fatal neurological diseases [1]. Animal prion diseases include bovine spongiform encephalopathy (BSE) in cattle, chronic wasting disease (CWD) in cervids, feline spongiform encephalopathy (FSE) in cats, exotic ungulate encephalopathy (EUE) in zoo animals (e.g., kudu, nyala, gemsbok, eland, and oryx), scrapie in goats and sheep, as well as transmissible mink encephalopathy (TME) in mink (Table 14.1). The prion agent of each prion disease is named after the disease itself (e.g., CWD agent in CWD, scrapie agent in scrapie). BSE, CWD, FSE, TME, and EUE are all thought to occur after the consumption of prion-infected materials such as meat and bone meal (MBM). Among these prion diseases, BSE is a foodborne disease that affects humans. Except for BSE, no other animal prion agents have been reported to transmit to humans. Indeed, studies using transgenic mice expressing human prion protein (PrP) show that CWD prion does not transmit to humans [2–4]. Thus, the risk of CWD transmission to humans can be dismissed. However, scrapie agent has been shown to transmit via cerebral inoculation to macaque monkeys after a prolonged incubation time [5], and to transgenic mice expressing human PrP [6]. In view of these findings, further studies are clearly necessary to establish what kinds of animal prion agents can be transmitted to humans.
Australian medical device regulations: An overview
Published in Jack Wong, Raymond K. Y. Tong, Handbook of Medical Device Regulatory Affairs in Asia, 2018
At a minimum, the TGA requires evidence to support the quality and safety of animal derived material, in accordance with the TGA approach to minimising the risk of exposure to Transmissible Spongiform Encephalopathies (TSEs) through medicines and medical devices, available on the TGA website.
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
Transmissible spongiform encephalopathies (TSEs) are a group of neurodegenerative disorders found in many mammals [1]. TSE in human, include Creutzfeldt – Jakob disease (CJD), Gerstmann – Straüssler – Sheinker syndrome (GSS), kuru, and fatal familial insomnia (FFI). The molecular pathogenesis of the disease is a conformational transformation of the normal membrane-associated sialoglycoprotein PrP (referred to as PrPC) that undergoes a post-translational conformational modification into the pathological structure of PrPSc. PrPSc has a protease-resistant core and contains substantial amounts of β sheet, whereas PrPC is largely α-helical and is sensitive to protease digestion [2,3] The accumulation of this abnormal prion protein leads to neuronal degeneration, astrocytic gliosis, and spongiform change [4].
UK guidelines for the medical and laboratory procurement and use of sperm, oocyte and embryo donors (2019)
Published in Human Fertility, 2021
Helen Clarke, Shona Harrison, Marta Jansa Perez, Jackson Kirkman-Brown
The previous guidelines have detailed discussion of the risks of transmissible spongiform encephalopathies (TSEs) such as Creutzfeldt-Jakob (CJD) disease through sperm, oocyte and embryo donation. Given the indeterminate risk of transmitting TSEs through sperm, oocyte and embryo donation, it is suggested that donors should not be accepted who have:been diagnosed with a prion-related disease or have first-degree family members similarly diagnosed;undergone invasive neurosurgical procedures;received human pituitary-derived growth hormone, cornea, sclera or dura mater.
3-Nitrotyrosine: a versatile oxidative stress biomarker for major neurodegenerative diseases
Published in International Journal of Neuroscience, 2020
Maria Bandookwala, Pinaki Sengupta
Human prion diseases or transmissible spongiform encephalopathies (TSEs) is a rare condition originating either spontaneously, due to genetically altered proteome, cellular stress response or by infection [69]. It is a group of fatal neurodegenerative diseases with approximately 1 death in a million people annually according to worldwide epidemiological data published by WHO. It includes transmissible and progressive degenerative disorders of the CNS like Kuru, fatal familial insomnia, variably protease-sensitive prionopathy (VPSPr), Gerstmann–Sträussler–Scheinker syndrome and sporadic and variant Creutzfeldt-Jakob disease among which sporadic CJD is the most common form [70]. Rapidly developing dementia, confusion, hallucinations, muscle stiffness, difficulty in speaking and shuffling gait are the symptoms affecting the quality of life of people. A clinical study by Chen et al. [71] in China revealed that patient usually dies on an average of 7.1 months after disease which coincided with the reports from epidemiological studies in the west. Damage to the nerve cells is central to the manifestation of prion disease typically characterized by the accumulation of mutated prion protein PrPSc. OS has long been recognized as a molecular and cellular mechanism as a driving force in the pathophysiology of prion disease. In vivo immunohistochemical studies by D. R. Brown in scrapie-infected mice model backed with supporting evidence validate the role of OS via confirmation of the presence of OS biomarkers [72]. Brown also conducted in vitro studies, and similar results were obtained from scrapie-infected cells where reduced levels of antioxidants were observed making the cells more vulnerable to the damage by free radicals [72]. Protein profiling experiments have revealed expressional alteration of DJ-1, an antioxidant protein and its nuclear translocalization due to OS in sCJD. Tahir et al. [73] observed a significantly higher amount of DJ-1 in the CSF of clinical sCJD patients. The same research group also detected DJ-1 upregulation in humanized PrP transgenic mice model at the pre-symptomatic and symptomatic stages indicative of OS [73]. Global metabolic profiling conducted in the hippocampus and cortex of prion protein-infected mice by Bourgognon et al. [74]showed alteration in glucose metabolism, upregulation of NO signalling, downregulation of SOD1 and SOD2 antioxidant genes which contribute to oxidative and nitrosative stress. Figure 5 shows the OS mechanism in TSE.