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Unformatted text preview: John Belew 2/24/2011 Professor Gronlund Biol 2420 Creutzfeldt-Jakob Outbreak Creutzfeldt-Jakob disease (CJD) in humans is one of several prion-associated encephalaopathies. This outbreak that occurred in the mid nineteen nineties in the United Kingdom (UK) was a worldwide scare due to the type of cases and how it was contracted in humans known later as the variant CJD (vCJD). (Will, Ironside) CJD is a potent neurodegenerative disease that is most certainly fatal. Transmissible spongiform encephalopathies (TSE) of both animals and humans require a protein component for mode of transmission. These prion proteins (PrP) are rogue or abnormal proteins, a molecule of about 250 amino acids. What makes these PrP abnormal is in the way that they are folded this allows them to resist protease degradation. In turn they to build up, and infect surrounding molecules causing the proteins of the molecules around them to transform and fold like its infectious self, especially in the brain infecting the neurons with tangled proteins. It is an unconventional disease that affects the central nervous system (CNS). (Beeks, McBride) TSEs are believed to have existed a long time in its original form known as scrapie in sheep, the presumption is that scrapie jumped the species barrier when left over parts of butchered sheep were mixed in the feed of cattle as a protein supplement. Then Cattle began to get sick and bovine spongiform encephalopathy (BSE) was identified as the culprit. What seems to have amplified this is that when cattle began to die, their remains were mixed in as protein supplements in several feeds, causing several forms now known as, chronic wasting disease (CWD) in captive deer, feline spongiform encephalopathy (FSE) in cats, transmissible mink...
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- Spring '11
- Bovine spongiform encephalopathy, Prion, Transmissible spongiform encephalopathy, CJD, National CJD Surveillance, CJD Surveillance Unit