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• W1535883711 abstract "The Prnd gene encodes a homolog of the cellular prion protein (PrPC) called doppel (Dpl). Up-regulation of Prnd mRNA in two distinct lines of PrP gene ablated (Prnp 0/0) mice, designatedRcm0 and Ngsk, is associated with death of Purkinje cells. Using recombinant Dpl expressed in Escherichia coli and mouse neuroblastoma cells we demonstrate that wild type (wt) Dpl, like PrPC, adopts a predominantly α-helical conformation, forms intramolecular disulfide bonds, has twoN-linked oligosaccharides, and is presented on the cell surface via a glycosylphosphatidylinositol anchor. Dpl protein was detected in testis of wt mice. Using Triton X-114 phase partitioning to enrich for glycosylphosphatidylinositol-anchored proteins, Dpl was detected in brain samples from Rcm0 Prnp 0/0mice but was absent in equivalent samples from wt mice and ZrchI Prnp 0/0 mice, indicating that ectopic expression of this protein may cause cerebellar pathology in Rcm0 mice. Biochemical and structural similarities between PrPC and Dpl documented here parallel the observation that ataxic Ngsk Prnp 0/0 mice can be rescued by overexpression of wild-type PrP transgenes, and suggest that cell surface PrPC can antagonize the toxic effect of Dpl expressed in the central nervous system." @default.
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• W1535883711 date "2000-06-06" @default.
• W1535883711 modified "2023-10-18" @default.
• W1535883711 title "Doppel is an N-glycosylated GPI-anchored protein: expression in testis and ectopic production in the brains of Prnp super0/0 mice predisposed to Purkinje cell loss" @default.
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• W1535883711 doi "https://doi.org/10.1074/jbc.m003888200" @default.
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