Prion protein transmissible spongiform

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. 

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. 

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). 

Tamguney G, Miller MW, Giles K et al (2009) Transmission of scrapie and sheep-passaged bovine spongiform encephalopathy prions to transgenic mice expressing elk prion protein. J Gen Virol 90 1035-1047... 

Race RE, Raines A, Baron TG et al (2002) Comparison of abnormal prion protein glycoform patterns from transmissible spongiform encephalopathy agent-infected deer, elk, sheep, and cattle. J Virol 76 12365-12368... 

Scott MR, Safar J, Telling G, Nguyen O, Groth D, Torchia M, Koehler R, Tremblay P, Walther D, Cohen FE, DeArmond SJ, Prusiner SB (1997) Identification of a prion protein epitope modulating transmission of bovine spongiform encephalopathy prions to transgenic mice. Proc Natl Acad Sci USA 94 14279-14284... 

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... 

PRION PROTEIN DIVERSITY AND DISEASE IN THE TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHIES... 

The prion protein PrP represents a central player in transmissible spongiform encephalopathies (TSEs), also known as prion diseases (for review see Lasmezas and Weiss, 2000)). The physiological role of the cellular isoform of PrP termed PrP is speculative so far (for review see (Weissmann, 1996)) and might involve control of circadian activity rhythms and sleep (Tobler et ai, 1996), maintenance of cerebellar Purkinje cell (Sakaguchi et al, 1996), and normal synaptic functions (Collinge et al., 1994 Fournier et al., 1995 Kitamoto et al., 1992). Because several reports do not describe any phenotype for PrP (Bueler et al, 1992 Lledo et al, 1996 Manson et al., 1994), the only proved role of prpc is its necessity for the development of TSEs (Bueler et al., 1993)... 

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