He and colleagues at the University of California, San Francisco, injected the brains of mice with prions they had created in the lab by
misfolding normal prion protein, known as PrP.
The scientists noted that in the CJD group, the «seeding potential»
for normal prion protein to convert to abnormal was 1,000 to 100,000 times lower in skin than brain tissue.
Biochemist Nigel Hooper of the University of Leeds in England and his colleagues found that high levels
of normal prion proteins in human cells prevent beta - amyloid formation by inhibiting an enzyme called beta - secretase.
The researchers
added normal prion proteins to a sample in the test tube, let the misfolded proteins «convert» the normal ones, broke up the resulting clumps with a sound pulse, and then repeated the process over and over until the PrPSc became detectable with ordinary methods.
Worse, instead of being destroyed and recycled by the cell — the typical fate of misfolded proteins — prions resist degradation and cause
other normal prion proteins to misfold.
Prion diseases are caused by infectious, malformed prion proteins that interact
with normal prion proteins and cause them to deform and accumulate in the body.
Scientists Show Prions Mutate and Adapt to Host Environment — The findings from the Weissmann lab point to
normal prion protein as the most effective therapeutic target for «mad cow» and related diseases.
They occur when
a normal prion protein becomes deformed and clumped.
Meanwhile Kazuo Kuwata and colleagues at Gifu University in Japan have developed a molecule called GN8 that has potential to prevent vCJD by binding to
the normal prion protein and preventing it misfolding into the abnormal form that causes disease.
In humans,
normal prion proteins may generally protect against Alzheimer's disease.