Regular ArticleThe Metabolism and Imaging in Live Cells of the Bovine Prion Protein in Its Native Form or Carrying Single Amino Acid Substitutions
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Possible involvement of calpain-like activity in normal processing of cellular prion protein
2011, Neuroscience LettersMutant prion protein expression is associated with an alteration of the rab GDP dissociation inhibitor α (GDI)/rab11 pathway
2010, Molecular and Cellular ProteomicsInteraction between the cellular prion (PrP<sup>C</sup>) and the 2P domain K<sup>+</sup> channel TREK-1 protein
2006, Biochemical and Biophysical Research CommunicationsCitation Excerpt :To exclude interference of the fluorescent protein tags in the physiological post-translational modifications of PrPC and TREK-1, an immunoblot analysis of the PrPC/DsRed and TREK-1/EGFP proteins in transfected HeLa cells was performed. In particular, PrPC/DsRed revealed an hetero-disperse signal of 50–75 kDa, likely attributed to un-, mono-, and di-glycosylated isoforms, similar to the electrophoretic pattern recently described for the GFP-bPrP construct in mammalian transfected cell lines [34]. Furthermore, PrPC glycoforms heterogeneity has been previously described in cultured cell lines (reviewed in [5] and [35]).
GFP-tagged PrP supports compromised prion replication in transgenic mice
2006, Biochemical and Biophysical Research CommunicationsCitation Excerpt :In agreement with previous cell culture studies [4–7], Western blots of extracts from stably transfected SMB and SMB-PS cells demonstrated that EGFPrP-N existed predominantly as multiple glycoforms migrating at ∼60–72 kDa with an additional fragment migrating at ∼55 kDa in uninfected SMB-PS cells (Fig. 1A). As demonstrated previously [4,5], release of EGFPrP-N from the surface of stably transfected SMB and SMB-PS cells with phosphatidylinositol phospholipase C (PIPLC) indicated that the fusion protein was correctly targeted to the plasma membrane and anchored to the cell surface by a GPI lipid anchor (data not shown). The persistence of a 3F4-reactive EGFPrP-N protease-resistant core corresponding to PrP27–30 following PK treatment of extracts from SMB cells stably expressing EGFPrP-N (Fig. 1A, lane 8) demonstrated that EGFPrPC-N was converted to EGFPrPSc-N.
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