title: Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor.
abstract: 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.
authors.affiliation: Max-Planck-Institute for Biochemistry, Martinsried, Germany.
authors.forename: Margit
authors.initials: M
authors.lastname: Miesbauer
authors.forename: Theresa
authors.initials: T
authors.lastname: Bamme
authors.forename: Constanze
authors.initials: C
authors.lastname: Riemer
authors.forename: Birgit
authors.initials: B
authors.lastname: Oidtmann
authors.forename: Konstanze F
authors.initials: KF
authors.lastname: Winklhofer
authors.forename: Michael
authors.initials: M
authors.lastname: Baier
authors.forename: Jörg
authors.initials: J
authors.lastname: Tatzelt
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006031:Glycosylation; D017261:Glycosylphosphatidylinositols / Q000737:chemistry* / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D011328:Prions / Q000737:chemistry* / Q000378:metabolism*; D015027:Zebrafish / Q000378:metabolism*
chemical_list: D017261:Glycosylphosphatidylinositols; D011328:Prions