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...

The key pathogenic event in prion disease involves misfolding and aggregation of the cellular prion protein (PrP). Beyond this fundamental observation, the mechanism by which PrP misfolding in neurons leads to injury and death remains enigmatic. Prion toxicity may come about by perverting the normal function of PrP. If so, understanding the normal function of PrP may help to elucidate the molec...

Abstract Background Wound healing is impaired in patients with diabetes due to the multifactorial etiology of disease, which limits therapeutic efficacy various approaches. This study hypothesizes that combination adipose-derived stem cells (ADSCs) and platelet-rich plasma (PRP) might achieve optimally efficient diabetic wound healing. Methods ADSCs were isolated from adipose tissues Sprague-Da...

The prion diseases seem to be caused by a conformational change of the prion protein (PrP) from the benign cellular form PrPC to the infectious scrapie form PrPSc; thus, detailed information about PrP structure may provide essential insights into the mechanism by which these diseases develop. In this study, the secondary structure of the recombinant Syrian hamster PrP of residues 29-231 [PrP(29...

Prion diseases are linked to the accumulation of a misfolded isoform (PrP(Sc)) of prion protein (PrP). Evidence suggests that lysosomes are degradation endpoints and sites of the accumulation of PrP(Sc). We questioned whether lysosomes participate in the early quality control of newly generated misfolded PrP. We found PrP carrying the disease-associated T182A mutation (Mut-PrP) was delivered to...