Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor
Biochem Biophys Res Commun 341(1): 218-24
| Authors/Editors: |
Miesbauer M Bamme T Riemer C Oidtmann B Winklhofer KF Baier M |
|---|---|
| Publication Date: | 2006 |
| Type of Publication: | Journal Article |
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.
