Prion diseases transmissible spongiform

Phenotypically, different neurodegenerative disorders, including AD, Parkinson disease, and prion diseases (transmissible spongiform encephalopathies), are... 

Mad cow disease Transmissible spongiform encephalopathy disease of the brain of cattle, caused by prions. 

The transmissible spongiform encephalopathies, or prion diseases, are fatal neurodegenerative diseases characterized by spongiform changes, astrocytic gliomas, and neuronal loss resulting from the deposition of insoluble protein aggregates in neural cells. They include Creutzfeldt-Jakob disease in humans, scrapie in... 

Prions—protein particles that lack nucleic acid— cause fatal transmissible spongiform encephalopathies such as Creutzfeldt-Jakob disease, scrapie, and bovine spongiform encephalopathy. Prion diseases involve an altered secondary-tertiary strucmre of a namrally occurring protein, PrPc. When PrPc interacts with its pathologic isoform PrPSc, its conformation is transformed from a predominantly a-helical strucmre to the P-sheet strucmre characteristic of PrPSc. 

The prion diseases are a closely related group of neuro-degenerative conditions which affect both humans and animals. They have previously been described as the subacute spongiform encephalopathies, slow virus diseases and transmissible dementias, and include scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle, and the human prion diseases, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker disease (GSS), fatal familial insomnia (FFI) and kuru. Prion diseases are... 

Mad cow disease—Bovine spongiform encephalopathy, or BSE, the form of transmissible spongiform encephalopathy (TSE) found in cattle. It is thought to be spread by consumption of brain tissue and caused by proteins called prions. 

Transmissible spongiform encephalopathies (TSEs)—Brain diseases transmitted from one animal to another. Under a microscope, the brain tissue of animals and people with TSEs resembles a sponge. TSEs include variant Creutzfeldt-Jacob disease (vCJD) in humans, scrapie in sheep and goats, and bovine spongiform encephalopathy (BSE) in cows (mad cow disease). These diseases are spread by consumption of brain tissue and are thought to be caused by prions, a kind of protein. 

Currently, there are some concerns regarding Transmissible Spongiform Encephalopathies (TSE) via animal-derived excipients such as gelatin. TSEs are caused by prions that are extremely resistant to heat and normal sterilization processes. TSEs have a very long incubation time with no cure and include diseases such as the following ... 

Certain brain diseases of humans and animals known as proteinopathies are associated with the accumulation of misfolded proteins both inside and around neurons [1], Alzheimer s disease in humans is by far the most common member of this group. The prion diseases, exemplified by Creutzfeldt-Jakob disease (CJD) in man, scrapie in small ruminants, and bovine spongiform encephalopathy (BSE) in cattle, constitute a peculiar sub-group within proteinopathies by being experimentally transmissible [2], Because of this feature, together with the sponge-like appearance of vacuoles in affected brain areas, prion diseases are also known as Transmissible Spongiform Encephalopathies (TSEs). 

Der Trab ist auch eine Krankheit der Schaafe, und ist ansteckend. Sie schleppen sich lange, verzehren sich nach und nach, und zuletzt miissen sie sterben. These sentences are taken from an article published in 1759 [1] and describe two hallmarks of prion diseases or transmissible spongiform encephalopathies (TSEs, summarized in Table 1) The formation and transmission of an infectious particle and the invariably fatal course of these diseases. More than 200 years later a landmark discovery paved the way to study the pathogenesis of prion diseases at a molecular level. Prusiner and colleagues reported the identification of a protease-resistant protein in brain extracts, which co-purified with the infectious scrapie agent [18]. After the N-terminal amino acid sequence of the proteinase K (PK)-resistant core of the prion protein (PrP 27-30) was published in 1984 [19], two... 

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