Partial Deletion of the Carboxyl-Terminal Signal Sequence of the Cellular Prion Protein Alters Protein Expression via Endoplasmic Reticulum-Associated Degradation.

Cellular prion protein (PrP) is a glycoprotein tethered to the plasma membrane via a GPI-anchor, and it plays a crucial role in prion diseases by undergoing conformational change to PrP. To generate a knock-in (KI) mouse model expressing bank vole PrP (BVPrP), a KI targeting construct was designed. However, a Prnp gene sequence that encodes PrP lacking seven C-terminal amino acid residues of the GPI-anchoring signal sequence (GPI-SS) was unintentionally introduced into the construct.

The Effect of Valeton (Zingiberaceae) Extract on Prion Propagation in Cell-Based and Animal Models.

Prion diseases are neurodegenerative disorders in humans and animals for which no therapies are currently available. Here, we report that Valeton (Zingiberaceae) () extract was partly effective in decreasing prion aggregation and propagation in both in vitro and in vivo models. extract inhibited self-aggregation of recombinant prion protein (PrP) in a test tube assay and decreased the accumulation of scrapie PrP (PrP) in ScN2a cells, a cultured neuroblastoma cell line with chronic prion infection, in a concentration-dependent manner.

Endoproteolysis of cellular prion protein by plasmin hinders propagation of prions.

Many questions surround the underlying mechanism for the differential metabolic processing observed for the prion protein (PrP) in healthy and prion-infected mammals. Foremost, the physiological α-cleavage of PrP interrupts a region critical for both toxicity and conversion of cellular PrP (PrP ) into its misfolded pathogenic isoform (PrP ) by generating a glycosylphosphatidylinositol (GPI)-anchored C1 fragment. During prion diseases, alternative β-cleavage of PrP becomes prominent, producing a GPI-anchored C2 fragment with this particular region intact.

Self-Assembling Peptides and Their Application in the Treatment of Diseases.

Self-assembling peptides are biomedical materials with unique structures that are formed in response to various environmental conditions. Governed by their physicochemical characteristics, the peptides can form a variety of structures with greater reactivity than conventional non-biological materials. The structural divergence of self-assembling peptides allows for various functional possibilities; when assembled, they can be used as scaffolds for cell and tissue regeneration, and vehicles for drug delivery, conferring controlled release, stability, and targeting, and avoiding side effects of drugs.

Non-ionic detergents Nonidet P-40 and Triton X-100 increase enzymatic activity of plasmin.

Plasmin is a potent serin protease involved in a variety of biological functions, such as fibrinolysis and tissue remodeling. On performing an in vitro control assay to measure the activity of endogenous plasmin in cell lysates, a stimulatory effect of non-ionic detergent NP-40 on plasmin activity was discovered. Another non-ionic detergent, TX-100, also enhanced plasmin activity, while ionic detergents sodium deoxycholate and sodiem dodecyl sulfate abolished plasmin enzyme activity.