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.…before an animal shows physical signs of having a prion infection, a particular prion protein in the brain was being eradicated. This member of the prion family is known as shadoo protein.
"….the shadoo protein is simultaneously disappearing," ….
"….there is a process within the disease …..that is happening before the infected animals are getting sick. It's telling us that the brain cells are more active in defending themselves than what we thought they were.
Cangene Corporation has signed a collaborative research agreement with the University of British Columbia (UBC) under which they will develop the work of Dr. Neil Cashman , Scientific Director of PrioNet Canada , Canada Research Chair in Neurodegeneration and Protein Misfolding at UBC, and a scientist at the Vancouver Coastal Health Research Institute, aimed at developing immune-based therapies for Alzheimer's disease.
Dr. Cashman 's work, supported by PrioNet (a Network of Centres of Excellence for research on prion disease and related neurodegenerative disorders), focuses on identifying and validating targets for treating various neurological diseases. Cangene became interested in the program following a recent discovery in which Dr. Cashman , along with other PrioNet researchers, was able to specifically target a unique shape of amyloid beta "oligomers"—small aggregates that Dr. Cashman calls the "bad guys" due to their key role in the progression of Alzheimer's—while sparing normal amyloid beta molecules.
"If we're only attacking the bad guys without harming the normal molecules, then we have a basis for a safe immunotherapy infusion," explains Dr. Cashman . This approach has already been tested in the laboratory on cultured nerve cells with successful results. "PrioNet's initial investment to support this research was integral to generating the scientific results needed to attract industry partners," he says. "Our partnership with Cangene will now help move this technology forward." Cangene has initiated work with UBC on the target identified by Dr. Cashman .
...several nations are starting to "put down" people with so-called incurable dementias
Transmissible spongiform encephalopathies are diseases of animals and humans that are also termed prion diseases. These diseases are linked together because a normal brain glycoprotein termed the prion protein is converted to a readily detectable protease-resistant isoform. There is now strong evidence to suggest that apart from this difference in resistance a major difference between the isoforms is that the normal prion protein binds copper and has an anti-oxidant function. Brains from Creutzfeldt-Jakob disease patients and brains from mice with experimental mouse scrapie have been shown to have changes in the levels of both copper and manganese. There is growing evidence that links prion diseases to disturbances of metal metabolism.
Originally posted by DangerDeath
I read a report which claims that lack of copper in environment or food made prions bind some toxic metals, and those metals were the cause of prion disease, not directly prions as such.
....There is growing evidence that links prion diseases to disturbances of metal metabolism.
…environmental insults, either physical (heat, pressure, radiation) or chemical (heavy metals, arsenate, toxins), also cause proteins to misfold into toxic shapes.
….conditions that are likely to put stress on proteins and cause them to misfold - such as preexisting misfolded proteins, oxidation, or heat