Received 17 June 2004 Accepted 2 June 2005 Prion diseases involve conversion of host-encoded cellular prion protein (PrP) to a disease-related isoform (PrP). Using recombinant human b-PrP, a panel of monoclonal antibodies was produced that efficiently immunoprecipitated native PrP and recognized epitopes between residues 93–105, indicating for the first time that this region is exposed in both ...

Transmissible spongiform encephalopathies, including variant-Creutzfeldt-Jakob disease (vCJD) in humans and bovine spongiform encephalopathies in cattle, are fatal neurodegenerative disorders characterized by protein misfolding of the host cellular prion protein (PrP(C)) to the infectious scrapie form (PrP(Sc)). However, the mechanism that exogenous PrP(Sc) infects cells and where pathologic co...

PrP(Sc), a misfolded and aggregated form of the cellular prion protein PrP(C), is the only defined constituent of the transmissible agent causing prion diseases. Expression of PrP(C) in the host organism is necessary for prion replication and for prion neurotoxicity. Understanding prion diseases necessitates detailed structural insights into PrP(C) and PrP(Sc). Towards this goal, we have develo...

objective: at present, growth factor-containing products such as enamel matrix derivatives, recombinant bone morphogenetic protein (rh-bmp), recombinant platelet derived growth factor and platelet rich plasma (prp) have gained increasing attention. prp is an autologous source of platelet growth factors used to enhance healing of soft and hard tissues. prp has gained popularity due to its autolo...

Prion protein PrP is a central player in several devastating neurodegenerative disorders, including mad cow disease and Creutzfeltd-Jacob disease. Conformational alteration of PrP into an aggregation-prone infectious form PrPSc can trigger pathogenic events. How levels of PrP are regulated is poorly understood. Human PrP is known to be degraded by the proteasome, but the specific proteolytic pa...

In transmissible spongiform encephalopathies (TSE) or prion diseases, the endogenous protease-sensitive prion protein (PrP-sen) of the host is converted to an abnormal pathogenic form that has a characteristic partial protease resistance (PrP-res). Studies with cell-free reactions indicate that the PrP-res itself can directly induce this conversion of PrP-sen. This PrP-res induced conversion re...

Prion propagation involves a templating reaction in which the infectious form of the prion protein (PrP ) binds to the cellular form (PrP ), generating additional molecules of PrP . While several regions of the PrP C molecule have been suggested to play a role in PrP Sc formation based on in vitro studies, the contribution of these regions in vivo is unclear. Here, we report that mice expressin...

Formation of aberrant protein conformers is a common pathological denominator of different neurodegenerative disorders, such as Alzheimer's disease or prion diseases. Moreover, increasing evidence indicates that soluble oligomers are associated with early pathological alterations and that oligomeric assemblies of different disease-associated proteins may share common structural features. Previo...

Prion diseases are a group of fatal neurodegenerative disorders associated with structural conversion of a normal, mostly alpha-helical cellular prion protein, PrP(C), into a pathogenic beta-sheet-rich conformation, PrP(Sc). The structure of PrP(C) is well studied, whereas the insolubility of PrP(Sc) makes the characterization of its structure problematic. No proteins similar to PrP, except for...

BACKGROUND Platelet-rich plasma (PRP) can provide an assortment of growth factors, but how PRP effects bone regeneration is still unknown. The aim of the study was to explore an optimal method of using PRP and bone marrow stromal cells (BMSCs). METHODS An in vitro experiment was first conducted to determine an appropriate quantity of PRP. BMSCs were cultured with PRP of different concentratio...