Wednesday, March 13, 2013

Alleles of mouse prion protein affect time to aggregate formation

Prion diseases are neurodegnerative disorders where a the normal cellular form of the prion protein polymerizes into an infectious form that induce formation of repeating sheets of protein, the effect of which is eventually fatal. The sequence of host prion protein is the main determinant in whether disease formation occurs.
PrPsc induces conformational change in PrPc

A recent paper in the Journal of Biological Chemistry has studied two forms of mouse prion protein that are polymorphic at amino acid residues 108/189. The results have implications in understanding disease susceptibility and species barriers.

The group from University of Alberta found that the recombinant forms of the two prion protein differed with respect to aggregation and response to seeding in an in vitro kinetic assay.

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