Publication Abstract

Prion protein-related proteins from zebrafish are complex glycoslated and contain a glycosylphosphatidylinositol anchor

M. Miesbauer, T. Bamme, C. Riemer, B. Oidtmann, K. Winklhofer and M. Baier

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.

Reference:

M. Miesbauer, T. Bamme, C. Riemer, B. Oidtmann, K. Winklhofer and M. Baier (2006) Prion protein-related proteins from zebrafish are complex glycoslated and contain a glycosylphosphatidylinositol anchor. Biochemical and Biophysical Research Communications, 341(1): 218-224