Prion Disease ...
- Thread starter aphexcoil
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Quote from bobcathy1:
I think a lot of these diseases come from over population and improper sanitation. Do you know how much manure these critters produce?
I think I will go back to being a vegetarian. Just thinking about that is not very appetizing.
One of the most popular theories on the origins of folded prions is cannibalism. Feeding downer cows to other cows...then the extra parts of those cows that are butchered fed to other cows..so on and so forth. Try reading "deadly feasts" by Richard Rhodes. it approaches CJD the human variant of BSE and "kuru" afflicting the people of Borneo as well as "scrapy" in sheep.
http://www.amazon.com/exec/obidos/search-handle-form/002-6216530-0932058
BSE is not known to spready from animal to animal, but rather through contaminated feed. The US Food & Drug Administration in 1997 instituted a ban on feeding ruminant-derived meat and bone neal supplements to catle. This is a firewall that prevents the spread of BSE to other animals if it were present in the U.S.
Problem is, people are greedy and have not abided by the instituted ban . . . risking the rest of us to BSE.
Problem is, people are greedy and have not abided by the instituted ban . . . risking the rest of us to BSE.
http://www.nobel.se/medicine/laureates/1997/
From the New England Journal of Medicine, March 30, 2000
The prion, or proteinaceous infectious particle, is thought to be responsible for a wide range of diseases characterized clinically by dementia and neuropathologically by neuronal loss, spongiform change, astrocytosis, and varying degrees of amyloid deposition. Prion diseases in humans include Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, and kuru; diseases in animals include scrapie and bovine spongiform encephalopathy. The cause of these diseases is thought to be a conformational change in a normal cellular protein, PrP(sup C), which is transformed into an infectious protein called PrP(sup Sc) (the superscript Sc denotes scrapie). PrP(sup Sc) does not differ from PrP(sup C) in its amino acid sequence or post-translational modifications; unlike PrP(sup C), however, PrP(sup Sc) is insoluble and resistant to proteinase K digestion, and it has a larger (beta)-sheet content and a propensity to aggregate into fibrils.
Although prion diseases in humans have thus far been rare, they are among the best-characterized "conformational diseases." Hence, the mechanisms of and potential therapeutic approaches to prion diseases may be relevant to more common conformational disorders, such as Alzheimer's disease (in which the amyloid (beta)-peptide is deposited as amyloid), Parkinson's disease (involving (alpha)-synuclein deposition in Lewy bodies), and the many neurodegenerative conditions associated with increased CAG repeats (e.g., Huntington's disease). Another reason for the importance of prion diseases is the recent reports of the transmission of bovine spongiform encephalopathy to humans through contaminated meat and bone meal, a topic that is well reviewed in this book. Evidence suggests that bovine spongiform encephalopathy has crossed the species barrier and now infects humans, resulting in new-variant Creutzfeldt-Jakob disease. It is unclear whether these cases mark the beginning of a human epidemic in Europe similar to that of bovine spongiform encephalopathy or whether the number of cases will remain small, as occurred with iatrogenic Creutzfeldt-Jakob disease after exposure to cadaveric growth hormone.
From the New England Journal of Medicine, March 30, 2000
The prion, or proteinaceous infectious particle, is thought to be responsible for a wide range of diseases characterized clinically by dementia and neuropathologically by neuronal loss, spongiform change, astrocytosis, and varying degrees of amyloid deposition. Prion diseases in humans include Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, and kuru; diseases in animals include scrapie and bovine spongiform encephalopathy. The cause of these diseases is thought to be a conformational change in a normal cellular protein, PrP(sup C), which is transformed into an infectious protein called PrP(sup Sc) (the superscript Sc denotes scrapie). PrP(sup Sc) does not differ from PrP(sup C) in its amino acid sequence or post-translational modifications; unlike PrP(sup C), however, PrP(sup Sc) is insoluble and resistant to proteinase K digestion, and it has a larger (beta)-sheet content and a propensity to aggregate into fibrils.
Although prion diseases in humans have thus far been rare, they are among the best-characterized "conformational diseases." Hence, the mechanisms of and potential therapeutic approaches to prion diseases may be relevant to more common conformational disorders, such as Alzheimer's disease (in which the amyloid (beta)-peptide is deposited as amyloid), Parkinson's disease (involving (alpha)-synuclein deposition in Lewy bodies), and the many neurodegenerative conditions associated with increased CAG repeats (e.g., Huntington's disease). Another reason for the importance of prion diseases is the recent reports of the transmission of bovine spongiform encephalopathy to humans through contaminated meat and bone meal, a topic that is well reviewed in this book. Evidence suggests that bovine spongiform encephalopathy has crossed the species barrier and now infects humans, resulting in new-variant Creutzfeldt-Jakob disease. It is unclear whether these cases mark the beginning of a human epidemic in Europe similar to that of bovine spongiform encephalopathy or whether the number of cases will remain small, as occurred with iatrogenic Creutzfeldt-Jakob disease after exposure to cadaveric growth hormone.