NR ATMK
AU Yokoyama,T.; Shimada,K.; Masujin,K.; Ushiki,Y.K.; Iwamaru,Y.; Imamura,M.; Kimura,K.M.; Shinagawa,M.
TI Both host prion protein 138-181 subregion and prion characteristics regulate glycoform of abnormal isoform of prion protein (PrPsc)
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Genetics, strains and emerging problems GEN-10
PT Konferenz-Poster
AB The prion protein (PrP) contains two N-linked glycosylation sites and is present in the cell in three different forms. An abnormal isoform of prion protein (PrPsc) has different glycoform patterns for different prion strains. However, the molecular basis of prion strain-specific glycoform variability has remained elusive. To understand the molecular basis of this glycoform differences, PrPsc in two lines of chimeric prion protein (PrP) expressing transgenic mice (MHM2/PrP0/0, and MH2M/PrP0/0) were analyzed. Our result indicated that PrP131-188 (the third sub-region of chimeric PrP) contributed to both PrPc and PrPsc glycoform. Furthermore, PrPsc glycoform pattern within these transgenic mice showed the subtle difference depending on the inoculated prion. This study indicated that glycoform of PrPsc were influenced by both host PrP131-188 and prion strain characteristics.
AD T.Yokoyama, K.Shimada, K.Masujin, Y.K.Ushiki, Y.Iwamaru, M.Imamura, K.M.Kimura, M.Shinagawa, National Institute of Animal Health, JAPAN; Y.K.Ushiki, Nippi Biomatrix Institute, Japan
SP englisch
PO Deutschland