α2,3 linkage of sialic acid to a GPI anchor and an unpredicted GPI attachment site in human prion protein.

ABSTRACT: Prion diseases are transmissible, lethal neurodegenerative disorders caused by accumulation of the aggregated scrapie form of the prion protein (PrP^Sc) after conversion of the cellular prion protein (PrP^C). The glycosylphosphatidylinositol (GPI) anchor of PrP^C is involved in prion disease pathogenesis, and especially sialic acid in a GPI side chain reportedly affects PrP^C conversion. Thus, it is important to define the location and structure of the GPI anchor in human PrP^C Moreover, the sialic acid linkage type in the GPI side chain has not been determined for any GPI-anchored protein. Here we report GPI glycan structures of human PrP^C isolated from human brains and from brains of a knock-in mouse model in which the mouse pr

SUBMITTER: Kobayashi A 

PROVIDER: S-EPMC7261787 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature