Detection of the GPI-anchorless prion protein fragment PrP226* in human brain.

ABSTRACT:

Background

The accumulation of the misfolded forms of cellular prion protein, i.e. prions (PrPSc), in the brain is one of the crucial characteristics of fatal neurodegenerative disorders, called transmissible spongiform encephalopathies (TSEs). Cellular prion protein is normally linked to the cell surface by the glycosylphosphatidylinositol (GPI) anchor. There is accumulating evidence that the GPI-anchorless prion protein may act as an accelerator of formation and propagation of prions. In the TSE affected human brain we have previously discovered a novel GPI-anchorless prion protein fragment, named PrP226*, which ends with the tyrosine 226. This fragment can be labeled specifically by the monoclonal antibody V5B2.

Methods

We developed a DELFIA based assay for quick and sens

SUBMITTER: Dvorakova E 

PROVIDER: S-EPMC3849060 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature