Prions

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like the
one done by Stanley B. Pruiser and his team of scientists at the School of
Medicine of the University of California at San Francisco in which a study was
carried out on mice to see if he was able to purify the scrapie agent ,another
prion disease, in mice. But mice as humans took very long to develope the
disease, for example Gerstmann-Straussler-Scheinker disease or fatal familial
insomnia, which appear mostly on humans which have passed the age of forty and
only in very rare cases before, so the experiment was changed to hamsters as
these die faster because developed the disease earlier. One of the methods used
for this purification process was using a centrifuge, that separates the
component of a mixture according to their size and density. After a decade of
experiments using the centrifuge method and other chemical methods, several
discoveries were made : It was found out that the infectious particles were
extremely heterogencous in size and density, the scrapie ...

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in the brain of scrapie-infected
hamsters contain prion proteins. This amyloid plaques have been found on
Alzheimer’s disease patients, which leads to the question if prions are related
to that disease. Although it has not been proven yet, the hypothesis is quite
reliable.

Can prions infectivity be reduced or eliminated?

There were some experiments done with substances to see if prion
infectivity could be reduced or eliminated. One of the substances used was
protease, which has only effects on proteins. Protease reduced prion infectivity
indeed, but was not totally effective. Thats why PrPc is known to be “protease
sensitive”and PrPsc is “relatively resistant to proteases” (thats ...

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