PUBLICATION
Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor
- Authors
- Miesbauer, M., Bamme, T., Riemer, C., Oidtmann, B., Winklhofer, K.F., Baier, M., and Tatzelt, J.
- ID
- ZDB-PUB-060124-19
- Date
- 2006
- Source
- Biochemical and Biophysical Research Communications 341(1): 218-224 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Endoplasmic Reticulum/metabolism*
- Glycosylation
- Glycosylphosphatidylinositols/chemistry*
- Glycosylphosphatidylinositols/metabolism*
- Mice
- Molecular Sequence Data
- Prions/chemistry*
- Prions/metabolism*
- Zebrafish/metabolism*
- PubMed
- 16414019 Full text @ Biochem. Biophys. Res. Commun.
Citation
Miesbauer, M., Bamme, T., Riemer, C., Oidtmann, B., Winklhofer, K.F., Baier, M., and Tatzelt, J. (2006) Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor. Biochemical and Biophysical Research Communications. 341(1):218-224.
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping