Mice devoid of PrP are resistant to scrapie

Article Abstract:

Experiments reveal that the ordinary host protein that is believed to be the original version of the infectious agent of the prion scrapie, is PrPsc. At probably almost ordinary levels, PrPsc is needed for normal vulnerability to scrapie. Disease is inhibited by the absence of homology between the host's PrP gene and incoming prions, which is proven by demonstrating that Prn-p0/0 mice that lacked PrPc exhibited ordinary growth and behavior. The resistance to scrapie was demonstrated even by heterozygous Prn-p0/+ mice.

Observations, Mice, Mice (Rodents), Scrapie, Golden hamster

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Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?

Article Abstract:

Alzheimer's disease (AD), a neurodegenerative disease, is characterized by the accumulation of amyloid protein (beta protein) which is similar to processes involving ordered protein aggregation. Scrapie, a human prion disease, is characterized by the aggregation of a normal cellular protein, prion protein (Pr P), and is analogous to AD. The transmission of scrapie and the initiation of AD involve the seeding of amyloid formation. AD and prion diseases can be treated by retarding the rate of amyloid formation.

Causes of, Amyloidosis, Nerve degeneration, Polymerization

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PAR-1 for the course of Neurodegenaration

Article Abstract:

An elegant fusion of loss-of-function genetics and transgenic overexpression is used to make the case that the PAR-1 kinase stands at the head of a temporally ordered series of tau phosphorylations. Overexpression of PAR-1 alone causes eye degeneration in transgenic files in the absence of pathogenic human tau overexpression.

Protein binding, Phosphorylation, Neurodegenerative diseases

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