Miesbauer M, Bamme T, Riemer C, Oidtmann B, Winklhofer KF, Baier M, Tatzelt J (2006): Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor
Biochem. Biophys. Res. Commun. 341 (1): 218-224, Epub Jan 9.

A hallmark of prion diseases in mammals is a conformational transition of the cellular prion protein (PrP^C) into a pathogenic isoform termed PrP^Sc. PrP^C is highly conserved in mammals, moreover, genes of PrP-related proteins have been recently identified in fish. While there is only little sequence homology to mammalian PrP, PrP-related fish proteins were predicted to be modified with N-linked glycans and a C-terminal glycosylphosphatidylinositol (GPI) anchor. We biochemically characterized two PrP-related proteins from zebrafish in cultured cells and show that both zePrP1 and zeSho2 are imported into the endoplasmic reticulum and are post-translationally modified with complex glycans and a C-terminal GPI anchor.