NR AUIS
AU Miesbauer,M.; Bamme,T.; Riemer,C.; Oidtmann,B.; Winklhofer,K.F.; Baier,M.; Tatzelt,J.
TI Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor
QU Biochemical and Biophysical Research Communications 2006 Mar 3; 341(1): 218-24
PT journal article
AB A hallmark of prion diseases in mammals is a conformational transition of the cellular prion protein (PrPc) into a pathogenic isoform termed PrPsc. PrPc 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.
MH Amino Acid Sequence; Animals; Endoplasmic Reticulum/*metabolism; Glycosylation; Glycosylphosphatidylinositols/*chemistry/*metabolism; Mice; Molecular Sequence Data; Prions/*chemistry/*metabolism; Research Support, Non-U.S. Gov't; Zebrafish/*metabolism
AD Max-Planck-Institute for Biochemistry, Martinsried, Germany.
SP englisch
PO USA