NR ATBY
AU Bragason,B.T.; Palsdottir,A.
TI Processing of ovine PrP(ARQ)C-EGFP chimeras containing Asn138 and Cys151 polymorphisms
QU Biochemical and Biophysical Research Communications 2005 Oct 21; 336(2): 544-53
PT journal article
AB Polymorphisms in the prion protein, PrPc, affect the susceptibility of sheep to scrapie. Three rare polymorphisms, M137T, S138N, and R151C, have been found in Icelandic sheep. Observations suggest that R151C may be associated with lower scrapie susceptibility, whereas S138N is neutral. The effects of the S138N and R151C polymorphisms on the cellular processing of PrPc were examined in a model system consisting of the expression of ovine PrPc-EGFP (green fluorescent protein) chimeras in the mouse neuroblastoma cell line N2a. Chimeras with the haplotypes A136R154Q171 (ARQ), AN138RQ, and AC151RQ were compared. The chimeras did not differ regarding their translocation into the secretory system, glycosylation, and transport to the cell surface. However, the AC151RQ chimera differed from the other chimeras regarding disulfide bonding characteristics; furthermore, a slight difference was detected between AC151RQ and the other chimeras by limited proteolysis. The processing of the ARQ and AN138RQ chimeras was identical in the experiments performed consistent with observations that it is neutral.
MH Amino Acid Substitution; Animals; Asparagine/genetics/*metabolism; COS Cells; Cattle; Cell Line, Tumor; Cercopithecus aethiops; Cysteine/genetics/*metabolism; Green Fluorescent Proteins/genetics/metabolism; Mice; Mutagenesis, Site-Directed; Neuroblastoma/*metabolism; Polymorphism, Genetic; PrPc Proteins/genetics/*metabolism; Protein Transport/*physiology; Recombinant Fusion Proteins/metabolism; Research Support, Non-U.S. Gov't; Structure-Activity Relationship
AD Institute for Experimental Pathology, Keldur, University of Iceland, Vesturlandsvegur, Reykjavik 112, Iceland.
SP englisch
PO USA