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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].
Knowledge, names, fraud and trust
Published in Geraldine Lee-Treweek, Tom Heller, Hilary MacQueen, Julie Stone, Sue Spurr, Complementary and Alternative Medicine: Structures and Safeguards, 2020
There are many other instances that seem to demonstrate the way in which lay knowledge is often seen as secondary or lesser to other forms, for example the debate over the MMR (measles, mumps and rubella) inoculation. These debates have become infused with claims that lay people’s fears are subjective or emotionally driven. This is particularly the case in the experience and knowledge of parents who allege their children have suffered because of MMR. Again, as with Camelford, lay people (parents) have often gathered information from other parents about the possible effects of MMR. In the case of the dangers to health from bovine spongiform encephalopathy or BSE (in particular, the risk of acquiring Creutzfeldt-Jakob disease or CJD from meat or blood products), lay people’s experiential knowledge was again challenged for some time before scientific research indicated that there was a problem with BSE in humans.
Risks and Rates
Published in Peter Cummings, Analysis of Incidence Rates, 2019
Peter Cummings, Peter Cummings
Epidemiologists distinguish between two types of counts: prevalent cases (existing things at one point in time) and incident cases (new things that arise over some period of time). Prevalent cases are persons with a given condition at a single moment in time, regardless of when the condition may have first appeared or how long it may be expected to last. Prevalent conditions can be habits or behaviors, such as being a smoker. They might be characteristics, such as being obese or having a high school education. Most commonly in epidemiology, the counted prevalent conditions are diseases, including acute (short duration) diseases, such as pneumonia, or chronic diseases, such as diabetes. When prevalent conditions are used as rate numerators, the resulting rates are prevalence rates. In veterinary epidemiology, a prevalent case might be a cow with bovine spongiform encephalopathy (mad-cow disease). In economics, a prevalent case may be a currently unemployed person who is seeking a job; the count of job-seeking unemployed people is the numerator for the unemployment rate. In other applications, inanimate objects may be counted, such as the number of pickup trucks in the current fleet of vehicles on the road or the number of large companies that are unionized.
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].
Tackling prion diseases: a review of the patent landscape
Published in Expert Opinion on Therapeutic Patents, 2021
Marco Zattoni, Giuseppe Legname
Human prion diseases are etiologically divided into idiopathic, genetic, and acquired. Among the idiopathic forms, which accounts for the majority of prion diseases cases, there are sporadic Creutzfeldt-Jakob disease (sCJD) and variably protease-sensitive prionopathy. Genetic prion diseases, such as, fatal familial insomnia, genetic CJD and Gerstmann-Sträussler-Scheinker syndrome are characterized by autosomal dominant mutations in human PRNP gene. The acquired forms are very rare and account for ritual cannibalism, as Kuru, contamination through surgical instruments, as in the case of iatrogenic CJD, or consumption of animal products contaminated with the agent responsible for the bovine spongiform encephalopathies (BSE) [7]. The BSE epidemic, often referred to as ‘mad cow disease,’ has attracted the attention of the public health authorities and the scientific community since it was shown to cause a new variant form of Creutzfeldt-Jakob disease (vCJD) in humans [8,9]. Besides BSE, other prion diseases discovered in animals include scrapie in sheep and goats and chronic wasting diseases (CWD) in cervids, for which no transmission to humans has been shown so far, although their potential risk cannot be dismissed [10,11]